NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|219567478|dbj|BAH05462|]
View 

hypothetical protein CKR_0411 [Clostridium kluyveri NBRC 12016]

Protein Classification

glutamine-hydrolyzing GMP synthase( domain architecture ID 11477919)

glutamine-hydrolyzing GMP synthase catalyzes the amination of the nucleotide precursor xanthosine 5'-monophosphate to form GMP

EC:  6.3.5.2
Gene Symbol:  guaA
Gene Ontology:  GO:0003922|GO:0006177|GO:0005524
PubMed:  8548458|10387030
SCOP:  4003747|4001196

Graphical summary

 Zoom to residue level

show extra options Â»

Show site features     Horizontal zoom: Ã—

List of domain hits

Name Accession Description Interval E-value
guaA PRK00074
GMP synthase; Reviewed
1-510 0e+00

GMP synthase; Reviewed


:

Pssm-ID: 234614 [Multi-domain]  Cd Length: 511  Bit Score: 1045.40  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478   1 MERELVIVVDFGGQYNQLIARRVRENNVYCEIVPYTYSVDKIKEKNPRGIIFTGGPNSVYDDNAPKISEDIFEIGVPVLG 80
Cdd:PRK00074   1 IHHDKILILDFGSQYTQLIARRVRELGVYSEIVPYDISAEEIRAFNPKGIILSGGPASVYEEGAPRADPEIFELGVPVLG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478  81 ICYGHQLICTTLGGKVESAQVREYGKTDVVLNNSSGLFSGIDKNESCWMSHTDFVSYPPEGFKIIGKSGESPVAAVENID 160
Cdd:PRK00074  81 ICYGMQLMAHQLGGKVERAGKREYGRAELEVDNDSPLFKGLPEEQDVWMSHGDKVTELPEGFKVIASTENCPIAAIANEE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478 161 KKIYGVQFHPEVEHTPFGKKMLSNFLFDICNLKGDWSMSSFVDEKIKSIKEEVGDKKVICAMSGGVDSSVAAMIVHKAVG 240
Cdd:PRK00074 161 RKFYGVQFHPEVTHTPQGKKLLENFVFDICGCKGDWTMENFIEEAIEEIREQVGDKKVILGLSGGVDSSVAAVLLHKAIG 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478 241 KQLTCIFVDHGLLRKDEGDQVEDIFKKQFNMNFIRVNAEKRFLQKLKDISDPEKKRKIIGEEFIRVFEEEAKKLGEIAFL 320
Cdd:PRK00074 241 DQLTCVFVDHGLLRKNEAEQVMEMFREHFGLNLIHVDASDRFLSALAGVTDPEEKRKIIGREFIEVFEEEAKKLGGVKFL 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478 321 VQGTIYPDVVESGLGT-SATIKSHHNVGGLPEDMDFKLIEPLRELFKDEVRAVGEELGIPHKLVWRQPFPGPGLAIRVLG 399
Cdd:PRK00074 321 AQGTLYPDVIESGGTKkAATIKSHHNVGGLPEDMKLKLVEPLRELFKDEVRKLGLELGLPEEIVYRHPFPGPGLAIRILG 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478 400 NITEEKLQITRDADAIFREEIAKANLDETIWQYFACLPNIRSVGVMGDERTYCYTIALRAVISTDAMTSDWARIPYEVLD 479
Cdd:PRK00074 401 EVTKEKLDILREADAIFIEELRKAGLYDKIWQAFAVLLPVKSVGVMGDGRTYDYVVALRAVTSIDGMTADWARLPYDFLE 480
                        490       500       510
                 ....*....|....*....|....*....|.
gi 219567478 480 KVSRRIVNEVKGVNRIVYDITSKPPATIEWE 510
Cdd:PRK00074 481 KISNRIINEVKGVNRVVYDITSKPPATIEWE 511
 
Name Accession Description Interval E-value
guaA PRK00074
GMP synthase; Reviewed
1-510 0e+00

GMP synthase; Reviewed


Pssm-ID: 234614 [Multi-domain]  Cd Length: 511  Bit Score: 1045.40  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478   1 MERELVIVVDFGGQYNQLIARRVRENNVYCEIVPYTYSVDKIKEKNPRGIIFTGGPNSVYDDNAPKISEDIFEIGVPVLG 80
Cdd:PRK00074   1 IHHDKILILDFGSQYTQLIARRVRELGVYSEIVPYDISAEEIRAFNPKGIILSGGPASVYEEGAPRADPEIFELGVPVLG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478  81 ICYGHQLICTTLGGKVESAQVREYGKTDVVLNNSSGLFSGIDKNESCWMSHTDFVSYPPEGFKIIGKSGESPVAAVENID 160
Cdd:PRK00074  81 ICYGMQLMAHQLGGKVERAGKREYGRAELEVDNDSPLFKGLPEEQDVWMSHGDKVTELPEGFKVIASTENCPIAAIANEE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478 161 KKIYGVQFHPEVEHTPFGKKMLSNFLFDICNLKGDWSMSSFVDEKIKSIKEEVGDKKVICAMSGGVDSSVAAMIVHKAVG 240
Cdd:PRK00074 161 RKFYGVQFHPEVTHTPQGKKLLENFVFDICGCKGDWTMENFIEEAIEEIREQVGDKKVILGLSGGVDSSVAAVLLHKAIG 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478 241 KQLTCIFVDHGLLRKDEGDQVEDIFKKQFNMNFIRVNAEKRFLQKLKDISDPEKKRKIIGEEFIRVFEEEAKKLGEIAFL 320
Cdd:PRK00074 241 DQLTCVFVDHGLLRKNEAEQVMEMFREHFGLNLIHVDASDRFLSALAGVTDPEEKRKIIGREFIEVFEEEAKKLGGVKFL 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478 321 VQGTIYPDVVESGLGT-SATIKSHHNVGGLPEDMDFKLIEPLRELFKDEVRAVGEELGIPHKLVWRQPFPGPGLAIRVLG 399
Cdd:PRK00074 321 AQGTLYPDVIESGGTKkAATIKSHHNVGGLPEDMKLKLVEPLRELFKDEVRKLGLELGLPEEIVYRHPFPGPGLAIRILG 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478 400 NITEEKLQITRDADAIFREEIAKANLDETIWQYFACLPNIRSVGVMGDERTYCYTIALRAVISTDAMTSDWARIPYEVLD 479
Cdd:PRK00074 401 EVTKEKLDILREADAIFIEELRKAGLYDKIWQAFAVLLPVKSVGVMGDGRTYDYVVALRAVTSIDGMTADWARLPYDFLE 480
                        490       500       510
                 ....*....|....*....|....*....|.
gi 219567478 480 KVSRRIVNEVKGVNRIVYDITSKPPATIEWE 510
Cdd:PRK00074 481 KISNRIINEVKGVNRVVYDITSKPPATIEWE 511
GuaA2 COG0519
GMP synthase, PP-ATPase domain/subunit [Nucleotide transport and metabolism]; GMP synthase, ...
1-510 0e+00

GMP synthase, PP-ATPase domain/subunit [Nucleotide transport and metabolism]; GMP synthase, PP-ATPase domain/subunit is part of the Pathway/BioSystem: Purine biosynthesis


Pssm-ID: 440285 [Multi-domain]  Cd Length: 512  Bit Score: 954.66  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478   1 MERELVIVVDFGGQYNQLIARRVRENNVYCEIVPYTYSVDKIKEKNPRGIIFTGGPNSVYDDNAPKISEDIFEIGVPVLG 80
Cdd:COG0519    1 MDKEIIIVLDFGGQYQQLIARRRREEGVYSEIIPPDTAAEEIKAKGPPGIILSGGPSSVYEEGAPPDDPELFELGGPILG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478  81 ICYGHQLICTTLGGKVESAQVREYGKTDVVLNNSSGLFSGIDKNESCWMSHTDFVSYPPEGFKIIGKSGESPVAAVENID 160
Cdd:COG0519   81 ICYGGQLMLHLLGGGVVRAERREYGGALLLVDDESDLFAGGPEELQVWMSHGDRVTELPPGFEVIASTENCPVAAIANEE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478 161 KKIYGVQFHPEVEHTPFGKKMLSNFLFDICNLKGDWSMSSFVDEKIKSIKEEVGDKKVICAMSGGVDSSVAAMIVHKAVG 240
Cdd:COG0519  161 RKLYGVQFHPEVVHTEQGKEILKNFLFDICGCKGDWTMENFIEEAIEEIREQVGDGKVICALSGGVDSSVAAALLHKAIG 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478 241 KQLTCIFVDHGLLRKDEGDQVEDIFKKQFNMNFIRVNAEKRFLQKLKDISDPEKKRKIIGEEFIRVFEEEAKKLGEIAFL 320
Cdd:COG0519  241 DQLTCVFVDHGLLRKGEAEQVEETFKEHFGLNLIYVDASERFLSALKGVTDPEEKRKIIGEEFIEVFEEEAKKLGGAKFL 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478 321 VQGTIYPDVVESG--LGTSATIKSHHNVGGLPEDMDFKLIEPLRELFKDEVRAVGEELGIPHKLVWRQPFPGPGLAIRVL 398
Cdd:COG0519  321 AQGTLYPDVIESGsvKGPAATIKSHHNVGGLPEDMKFKLVEPLRELFKDEVRALGRELGLPEEIVYRHPFPGPGLAIRIL 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478 399 GNITEEKLQITRDADAIFREEIAKANLDETIWQYFACLPNIRSVGVMGDERTYCYTIALRAVISTDAMTSDWARIPYEVL 478
Cdd:COG0519  401 GEVTKEKLEILREADAIFIEELRKAGLYDKVWQAFAVLLPVKSVGVMGDERTYEYVVALRAVTSVDGMTADWARLPYEVL 480
                        490       500       510
                 ....*....|....*....|....*....|..
gi 219567478 479 DKVSRRIVNEVKGVNRIVYDITSKPPATIEWE 510
Cdd:COG0519  481 ERISNRIINEVKGVNRVVYDITSKPPATIEWE 512
guaA_Cterm TIGR00884
GMP synthase (glutamine-hydrolyzing), C-terminal domain or B subunit; This protein of purine ...
201-510 0e+00

GMP synthase (glutamine-hydrolyzing), C-terminal domain or B subunit; This protein of purine de novo biosynthesis is well-conserved. However, it appears to split into two separate polypeptide chains in most of the Archaea. This C-terminal region would be the larger subunit [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]


Pssm-ID: 273321 [Multi-domain]  Cd Length: 311  Bit Score: 551.95  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478  201 FVDEKIKSIKEEVGDKKVICAMSGGVDSSVAAMIVHKAVGKQLTCIFVDHGLLRKDEGDQVEDIFKKQFNMNFIRVNAEK 280
Cdd:TIGR00884   2 FIEEAVEEIREQVGDAKVIIALSGGVDSSVAAVLAHRAIGDRLTCVFVDHGLLRKGEAEQVVKTFGDRLGLNLVYVDAKE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478  281 RFLQKLKDISDPEKKRKIIGEEFIRVFEEEAKKLGEIAFLVQGTIYPDVVESGLGTSATIKSHHNVGGLPEDMDFKLIEP 360
Cdd:TIGR00884  82 RFLSALKGVTDPEEKRKIIGRVFIEVFEREAKKIGDAEYLAQGTIYPDVIESAAGTAHVIKSHHNVGGLPEDMKLKLVEP 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478  361 LRELFKDEVRAVGEELGIPHKLVWRQPFPGPGLAIRVLGNITEEKLQITRDADAIFREEIAKANLDETIWQYFACLPNIR 440
Cdd:TIGR00884 162 LRELFKDEVRKLGKELGLPEEIVWRHPFPGPGLAVRVLGEVTKEKLEILRRADAIVIEELKKAGLYDKVWQAFAVLLPVK 241
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478  441 SVGVMGDERTYCYTIALRAVISTDAMTSDWARIPYEVLDKVSRRIVNEVKGVNRIVYDITSKPPATIEWE 510
Cdd:TIGR00884 242 SVGVMGDGRTYGYVIALRAVESIDGMTADWARLPYDFLERISNRITNEVPGVNRVVYDITSKPPATIEWE 311
GMP_synthase_C cd01997
C-terminal domain of GMP synthetase (glutamine-hydrolyzing); The C-terminal domain of GMP ...
209-510 0e+00

C-terminal domain of GMP synthetase (glutamine-hydrolyzing); The C-terminal domain of GMP synthetase (glutamine-hydrolyzing, EC 6.3.5.2) contains two subdomains: the ATP pyrophosphatase domain at the N-terminal and the dimerization domain at the C-terminal end. The ATP-PPase domain is a twisted, five-stranded parallel beta-sheet sandwiched between helical layers. It has a signature nucleotide-binding motif, or PP-loop, at the end of the first-beta strand. GMP synthetase is a homodimer, but in some archaea, it is a heterodimer made up of ATP pyrophosphatase (ATP-PPase) and a GATase subunit. In eukaryotes and bacteria, the two catalytic units are encoded by a single gene producing a two-domain-type GMP with a GATase domain in the N-terminus and an ATP-PPase domain in the C-terminus.


Pssm-ID: 467501 [Multi-domain]  Cd Length: 311  Bit Score: 520.95  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478 209 IKEEVGDKKVICAMSGGVDSSVAAMIVHKAVGK-QLTCIFVDHGLLRKDEGDQVEDIFKKQFNMNFIRVNAEKRFLQKLK 287
Cdd:cd01997    1 IKRTVGDKKVLCLVSGGVDSTVCAALLHKALGDeRVIAVHIDNGLMRKNESEQVEEALKKLGVINLAKVDASKRFLKKLK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478 288 DISDPEKKRKIIGEEFIRVFEEEAKKLG---EIAFLVQGTIYPDVVESG----LGTSATIKSHHNVGGLPED-MDFKLIE 359
Cdd:cd01997   81 GVTDPEEKRKIIGDTFIEVFDEVAKELNldpDDVYLAQGTLYPDLIESAsslaSSKADTIKTHHNVGGLPRElLKGKLVE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478 360 PLRELFKDEVRAVGEELGIPHKLVWRQPFPGPGLAIRVLGNITEEKLQITRDADAIFREEIAKANLDETIWQYFACLPNI 439
Cdd:cd01997  161 PLRDLFKDEVRELGRELGLPEELVWRHPFPGPGLAIRVLGEVTPEKLEILREADAIVEEELREAGLYDKISQAFAVLLPI 240
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 219567478 440 RSVGVMGDERTYCYTIALRAVISTDAMTSDWARIPYEVLDKVSRRIVNEVKGVNRIVYDITSKPPATIEWE 510
Cdd:cd01997  241 KSVGVQGDGRTYGYVVALRAVETEDFMTAEWARPPYEVLDKISNRITNEVPGVNRVVYDITSKPPATIEWE 311
GMP_synt_C pfam00958
GMP synthase C terminal domain; GMP synthetase is a glutamine amidotransferase from the de ...
418-509 1.01e-64

GMP synthase C terminal domain; GMP synthetase is a glutamine amidotransferase from the de novo purine biosynthetic pathway. This family is the C-terminal domain specific to the GMP synthases EC:6.3.5.2. In prokaryotes this domain mediates dimerization. Eukaryotic GMP synthases are monomers. This domain in eukaryotes includes several large insertions that may form globular domains.


Pssm-ID: 425963 [Multi-domain]  Cd Length: 92  Bit Score: 204.57  E-value: 1.01e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478  418 EEIAKANLDETIWQYFACLPNIRSVGVMGDERTYCYTIALRAVISTDAMTSDWARIPYEVLDKVSRRIVNEVKGVNRIVY 497
Cdd:pfam00958   1 EEIKKAGLYRKIWQAFAVLLPVKSVGVMGDERTYEYVVALRAVTSTDGMTADWARLPYEVLEKISNRIVNEVPGVNRVVY 80
                          90
                  ....*....|..
gi 219567478  498 DITSKPPATIEW 509
Cdd:pfam00958  81 DITSKPPATIEW 92
 
Name Accession Description Interval E-value
guaA PRK00074
GMP synthase; Reviewed
1-510 0e+00

GMP synthase; Reviewed


Pssm-ID: 234614 [Multi-domain]  Cd Length: 511  Bit Score: 1045.40  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478   1 MERELVIVVDFGGQYNQLIARRVRENNVYCEIVPYTYSVDKIKEKNPRGIIFTGGPNSVYDDNAPKISEDIFEIGVPVLG 80
Cdd:PRK00074   1 IHHDKILILDFGSQYTQLIARRVRELGVYSEIVPYDISAEEIRAFNPKGIILSGGPASVYEEGAPRADPEIFELGVPVLG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478  81 ICYGHQLICTTLGGKVESAQVREYGKTDVVLNNSSGLFSGIDKNESCWMSHTDFVSYPPEGFKIIGKSGESPVAAVENID 160
Cdd:PRK00074  81 ICYGMQLMAHQLGGKVERAGKREYGRAELEVDNDSPLFKGLPEEQDVWMSHGDKVTELPEGFKVIASTENCPIAAIANEE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478 161 KKIYGVQFHPEVEHTPFGKKMLSNFLFDICNLKGDWSMSSFVDEKIKSIKEEVGDKKVICAMSGGVDSSVAAMIVHKAVG 240
Cdd:PRK00074 161 RKFYGVQFHPEVTHTPQGKKLLENFVFDICGCKGDWTMENFIEEAIEEIREQVGDKKVILGLSGGVDSSVAAVLLHKAIG 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478 241 KQLTCIFVDHGLLRKDEGDQVEDIFKKQFNMNFIRVNAEKRFLQKLKDISDPEKKRKIIGEEFIRVFEEEAKKLGEIAFL 320
Cdd:PRK00074 241 DQLTCVFVDHGLLRKNEAEQVMEMFREHFGLNLIHVDASDRFLSALAGVTDPEEKRKIIGREFIEVFEEEAKKLGGVKFL 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478 321 VQGTIYPDVVESGLGT-SATIKSHHNVGGLPEDMDFKLIEPLRELFKDEVRAVGEELGIPHKLVWRQPFPGPGLAIRVLG 399
Cdd:PRK00074 321 AQGTLYPDVIESGGTKkAATIKSHHNVGGLPEDMKLKLVEPLRELFKDEVRKLGLELGLPEEIVYRHPFPGPGLAIRILG 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478 400 NITEEKLQITRDADAIFREEIAKANLDETIWQYFACLPNIRSVGVMGDERTYCYTIALRAVISTDAMTSDWARIPYEVLD 479
Cdd:PRK00074 401 EVTKEKLDILREADAIFIEELRKAGLYDKIWQAFAVLLPVKSVGVMGDGRTYDYVVALRAVTSIDGMTADWARLPYDFLE 480
                        490       500       510
                 ....*....|....*....|....*....|.
gi 219567478 480 KVSRRIVNEVKGVNRIVYDITSKPPATIEWE 510
Cdd:PRK00074 481 KISNRIINEVKGVNRVVYDITSKPPATIEWE 511
GuaA2 COG0519
GMP synthase, PP-ATPase domain/subunit [Nucleotide transport and metabolism]; GMP synthase, ...
1-510 0e+00

GMP synthase, PP-ATPase domain/subunit [Nucleotide transport and metabolism]; GMP synthase, PP-ATPase domain/subunit is part of the Pathway/BioSystem: Purine biosynthesis


Pssm-ID: 440285 [Multi-domain]  Cd Length: 512  Bit Score: 954.66  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478   1 MERELVIVVDFGGQYNQLIARRVRENNVYCEIVPYTYSVDKIKEKNPRGIIFTGGPNSVYDDNAPKISEDIFEIGVPVLG 80
Cdd:COG0519    1 MDKEIIIVLDFGGQYQQLIARRRREEGVYSEIIPPDTAAEEIKAKGPPGIILSGGPSSVYEEGAPPDDPELFELGGPILG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478  81 ICYGHQLICTTLGGKVESAQVREYGKTDVVLNNSSGLFSGIDKNESCWMSHTDFVSYPPEGFKIIGKSGESPVAAVENID 160
Cdd:COG0519   81 ICYGGQLMLHLLGGGVVRAERREYGGALLLVDDESDLFAGGPEELQVWMSHGDRVTELPPGFEVIASTENCPVAAIANEE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478 161 KKIYGVQFHPEVEHTPFGKKMLSNFLFDICNLKGDWSMSSFVDEKIKSIKEEVGDKKVICAMSGGVDSSVAAMIVHKAVG 240
Cdd:COG0519  161 RKLYGVQFHPEVVHTEQGKEILKNFLFDICGCKGDWTMENFIEEAIEEIREQVGDGKVICALSGGVDSSVAAALLHKAIG 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478 241 KQLTCIFVDHGLLRKDEGDQVEDIFKKQFNMNFIRVNAEKRFLQKLKDISDPEKKRKIIGEEFIRVFEEEAKKLGEIAFL 320
Cdd:COG0519  241 DQLTCVFVDHGLLRKGEAEQVEETFKEHFGLNLIYVDASERFLSALKGVTDPEEKRKIIGEEFIEVFEEEAKKLGGAKFL 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478 321 VQGTIYPDVVESG--LGTSATIKSHHNVGGLPEDMDFKLIEPLRELFKDEVRAVGEELGIPHKLVWRQPFPGPGLAIRVL 398
Cdd:COG0519  321 AQGTLYPDVIESGsvKGPAATIKSHHNVGGLPEDMKFKLVEPLRELFKDEVRALGRELGLPEEIVYRHPFPGPGLAIRIL 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478 399 GNITEEKLQITRDADAIFREEIAKANLDETIWQYFACLPNIRSVGVMGDERTYCYTIALRAVISTDAMTSDWARIPYEVL 478
Cdd:COG0519  401 GEVTKEKLEILREADAIFIEELRKAGLYDKVWQAFAVLLPVKSVGVMGDERTYEYVVALRAVTSVDGMTADWARLPYEVL 480
                        490       500       510
                 ....*....|....*....|....*....|..
gi 219567478 479 DKVSRRIVNEVKGVNRIVYDITSKPPATIEWE 510
Cdd:COG0519  481 ERISNRIINEVKGVNRVVYDITSKPPATIEWE 512
PLN02347 PLN02347
GMP synthetase
5-510 0e+00

GMP synthetase


Pssm-ID: 215197 [Multi-domain]  Cd Length: 536  Bit Score: 709.53  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478   5 LVIVVDFGGQYNQLIARRVRENNVYCEIVPYTYSVDKIKEKNPRGIIFTGGPNSVYDDNAPKISEDIFEI----GVPVLG 80
Cdd:PLN02347  12 VVLILDYGSQYTHLITRRVRELGVYSLLLSGTASLDRIASLNPRVVILSGGPHSVHVEGAPTVPEGFFDYcrerGVPVLG 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478  81 ICYGHQLICTTLGGKVESAQVREYGKTDVVLNNSSGLFSGID--KNESCWMSHTDFVSYPPEGFKIIGKSGESPVAAVEN 158
Cdd:PLN02347  92 ICYGMQLIVQKLGGEVKPGEKQEYGRMEIRVVCGSQLFGDLPsgETQTVWMSHGDEAVKLPEGFEVVAKSVQGAVVAIEN 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478 159 IDKKIYGVQFHPEVEHTPFGKKMLSNFLFDICNLKGDWSMSSFVDEKIKSIKEEVG-DKKVICAMSGGVDSSVAAMIVHK 237
Cdd:PLN02347 172 RERRIYGLQYHPEVTHSPKGMETLRHFLFDVCGVTADWKMQDVLEEQIELIKATVGpDEHVICALSGGVDSTVAATLVHK 251
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478 238 AVGKQLTCIFVDHGLLRKDEGDQVEDIFKKQFNMNFIRVNAEKRFLQKLKDISDPEKKRKIIGEEFIRVFEEEA----KK 313
Cdd:PLN02347 252 AIGDRLHCVFVDNGLLRYKEQERVMETFKRDLHLPVTCVDASERFLSKLKGVTDPEKKRKIIGAEFIEVFDEFAhkleQK 331
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478 314 LGEI-AFLVQGTIYPDVVES------GLGTSATIKSHHNVGGLPEDMDFKLIEPLRELFKDEVRAVGEELGIPHKLVWRQ 386
Cdd:PLN02347 332 LGKKpAFLVQGTLYPDVIEScpppgsGRTHSHTIKSHHNVGGLPKDMKLKLIEPLKLLFKDEVRKLGRLLGVPEAFLKRH 411
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478 387 PFPGPGLAIRVLGNITEE-KLQITRDADAIFREEIAKANLDETIWQYFACLPNIRSVGVMGDERTYCYTIALRAVISTDA 465
Cdd:PLN02347 412 PFPGPGLAVRVLGDVTEGnALDILRQVDEIFINSIKDAGLYDEIWQAFAVFLPVKSVGVQGDQRTHSHVVALRAVTSEDG 491
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*
gi 219567478 466 MTSDWARIPYEVLDKVSRRIVNEVKGVNRIVYDITSKPPATIEWE 510
Cdd:PLN02347 492 MTADWYHFEHKFLDDVSRKICNEVRGVNRVVYDITSKPPSTIEWE 536
guaA_Cterm TIGR00884
GMP synthase (glutamine-hydrolyzing), C-terminal domain or B subunit; This protein of purine ...
201-510 0e+00

GMP synthase (glutamine-hydrolyzing), C-terminal domain or B subunit; This protein of purine de novo biosynthesis is well-conserved. However, it appears to split into two separate polypeptide chains in most of the Archaea. This C-terminal region would be the larger subunit [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]


Pssm-ID: 273321 [Multi-domain]  Cd Length: 311  Bit Score: 551.95  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478  201 FVDEKIKSIKEEVGDKKVICAMSGGVDSSVAAMIVHKAVGKQLTCIFVDHGLLRKDEGDQVEDIFKKQFNMNFIRVNAEK 280
Cdd:TIGR00884   2 FIEEAVEEIREQVGDAKVIIALSGGVDSSVAAVLAHRAIGDRLTCVFVDHGLLRKGEAEQVVKTFGDRLGLNLVYVDAKE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478  281 RFLQKLKDISDPEKKRKIIGEEFIRVFEEEAKKLGEIAFLVQGTIYPDVVESGLGTSATIKSHHNVGGLPEDMDFKLIEP 360
Cdd:TIGR00884  82 RFLSALKGVTDPEEKRKIIGRVFIEVFEREAKKIGDAEYLAQGTIYPDVIESAAGTAHVIKSHHNVGGLPEDMKLKLVEP 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478  361 LRELFKDEVRAVGEELGIPHKLVWRQPFPGPGLAIRVLGNITEEKLQITRDADAIFREEIAKANLDETIWQYFACLPNIR 440
Cdd:TIGR00884 162 LRELFKDEVRKLGKELGLPEEIVWRHPFPGPGLAVRVLGEVTKEKLEILRRADAIVIEELKKAGLYDKVWQAFAVLLPVK 241
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478  441 SVGVMGDERTYCYTIALRAVISTDAMTSDWARIPYEVLDKVSRRIVNEVKGVNRIVYDITSKPPATIEWE 510
Cdd:TIGR00884 242 SVGVMGDGRTYGYVIALRAVESIDGMTADWARLPYDFLERISNRITNEVPGVNRVVYDITSKPPATIEWE 311
GMP_synthase_C cd01997
C-terminal domain of GMP synthetase (glutamine-hydrolyzing); The C-terminal domain of GMP ...
209-510 0e+00

C-terminal domain of GMP synthetase (glutamine-hydrolyzing); The C-terminal domain of GMP synthetase (glutamine-hydrolyzing, EC 6.3.5.2) contains two subdomains: the ATP pyrophosphatase domain at the N-terminal and the dimerization domain at the C-terminal end. The ATP-PPase domain is a twisted, five-stranded parallel beta-sheet sandwiched between helical layers. It has a signature nucleotide-binding motif, or PP-loop, at the end of the first-beta strand. GMP synthetase is a homodimer, but in some archaea, it is a heterodimer made up of ATP pyrophosphatase (ATP-PPase) and a GATase subunit. In eukaryotes and bacteria, the two catalytic units are encoded by a single gene producing a two-domain-type GMP with a GATase domain in the N-terminus and an ATP-PPase domain in the C-terminus.


Pssm-ID: 467501 [Multi-domain]  Cd Length: 311  Bit Score: 520.95  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478 209 IKEEVGDKKVICAMSGGVDSSVAAMIVHKAVGK-QLTCIFVDHGLLRKDEGDQVEDIFKKQFNMNFIRVNAEKRFLQKLK 287
Cdd:cd01997    1 IKRTVGDKKVLCLVSGGVDSTVCAALLHKALGDeRVIAVHIDNGLMRKNESEQVEEALKKLGVINLAKVDASKRFLKKLK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478 288 DISDPEKKRKIIGEEFIRVFEEEAKKLG---EIAFLVQGTIYPDVVESG----LGTSATIKSHHNVGGLPED-MDFKLIE 359
Cdd:cd01997   81 GVTDPEEKRKIIGDTFIEVFDEVAKELNldpDDVYLAQGTLYPDLIESAsslaSSKADTIKTHHNVGGLPRElLKGKLVE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478 360 PLRELFKDEVRAVGEELGIPHKLVWRQPFPGPGLAIRVLGNITEEKLQITRDADAIFREEIAKANLDETIWQYFACLPNI 439
Cdd:cd01997  161 PLRDLFKDEVRELGRELGLPEELVWRHPFPGPGLAIRVLGEVTPEKLEILREADAIVEEELREAGLYDKISQAFAVLLPI 240
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 219567478 440 RSVGVMGDERTYCYTIALRAVISTDAMTSDWARIPYEVLDKVSRRIVNEVKGVNRIVYDITSKPPATIEWE 510
Cdd:cd01997  241 KSVGVQGDGRTYGYVVALRAVETEDFMTAEWARPPYEVLDKISNRITNEVPGVNRVVYDITSKPPATIEWE 311
GATase1_GMP_Synthase cd01742
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine ...
6-186 3.42e-102

Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase. GMP synthetase is a glutamine amidotransferase from the de novo purine biosynthetic pathway. Glutamine amidotransferase (GATase) activity catalyse the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. GMP synthetase catalyses the amination of the nucleotide precursor xanthosine 5'-monophosphate to form GMP. GMP synthetase belongs to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site.


Pssm-ID: 153213 [Multi-domain]  Cd Length: 181  Bit Score: 304.07  E-value: 3.42e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478   6 VIVVDFGGQYNQLIARRVRENNVYCEIVPYTYSVDKIKEKNPRGIIFTGGPNSVYDDNAPKISEDIFEIGVPVLGICYGH 85
Cdd:cd01742    1 ILILDFGSQYTHLIARRVRELGVYSEILPNTTPLEEIKLKNPKGIILSGGPSSVYEEDAPRVDPEIFELGVPVLGICYGM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478  86 QLICTTLGGKVESAQVREYGKTDVVLNNSSGLFSGIDKNESCWMSHTDFVSYPPEGFKIIGKSGESPVAAVENIDKKIYG 165
Cdd:cd01742   81 QLIAKALGGKVERGDKREYGKAEIEIDDSSPLFEGLPDEQTVWMSHGDEVVKLPEGFKVIASSDNCPVAAIANEEKKIYG 160
                        170       180
                 ....*....|....*....|.
gi 219567478 166 VQFHPEVEHTPFGKKMLSNFL 186
Cdd:cd01742  161 VQFHPEVTHTEKGKEILKNFL 181
guaA_Nterm TIGR00888
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine ...
6-193 1.75e-93

GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine de novo biosynthesis is well-conserved. However, it appears to split into two separate polypeptide chains in most of the Archaea. This N-terminal region would be the smaller subunit. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]


Pssm-ID: 129966 [Multi-domain]  Cd Length: 188  Bit Score: 282.28  E-value: 1.75e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478    6 VIVVDFGGQYNQLIARRVRENNVYCEIVPYTYSVDKIKEKNPRGIIFTGGPNSVYDDNAPKISEDIFEIGVPVLGICYGH 85
Cdd:TIGR00888   1 ILVLDFGSQYTQLIARRLRELGVYSELVPNTTPLEEIREKNPKGIILSGGPSSVYAENAPRADEKIFELGVPVLGICYGM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478   86 QLICTTLGGKVESAQVREYGKTDVVLNNSSGLFSGIDKNESCWMSHTDFVSYPPEGFKIIGKSGESPVAAVENIDKKIYG 165
Cdd:TIGR00888  81 QLMAKQLGGEVGRAEKREYGKAELEILDEDDLFRGLPDESTVWMSHGDKVKELPEGFKVLATSDNCPVAAMAHEEKPIYG 160
                         170       180
                  ....*....|....*....|....*...
gi 219567478  166 VQFHPEVEHTPFGKKMLSNFLFDICNLK 193
Cdd:TIGR00888 161 VQFHPEVTHTEYGNELLENFVYDVCGCE 188
GuaA1 COG0518
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ...
6-189 1.02e-69

GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP synthase, glutamine amidotransferase domain is part of the Pathway/BioSystem: Purine biosynthesis


Pssm-ID: 440284 [Multi-domain]  Cd Length: 225  Bit Score: 222.51  E-value: 1.02e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478   6 VIVVD---FGGQYNQLIARRVREN-------NVY-CEIVPYTYSVDkikekNPRGIIFTGGPNSVYDD-----NAPKISE 69
Cdd:COG0518    2 ILILDhdpFGGQYPGLIARRLREAgieldvlRVYaGEILPYDPDLE-----DPDGLILSGGPMSVYDEdpwleDEPALIR 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478  70 DIFEIGVPVLGICYGHQLICTTLGGKVESAQVREYGKTDVVLNNSSGLFSGIDKNESCWMSHTDFVSYPPEGFKIIGKSG 149
Cdd:COG0518   77 EAFELGKPVLGICYGAQLLAHALGGKVEPGPGREIGWAPVELTEADPLFAGLPDEFTVWMSHGDTVTELPEGAEVLASSD 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478 150 ESPVAAVEnIDKKIYGVQFHPEVEHT------------------------------PFGKKMLSNFLFDI 189
Cdd:COG0518  157 NCPNQAFR-YGRRVYGVQFHPEVTHTmmeawleeradelaaeellaeaslhdpelrEAGRRLLRNFLREI 225
GMP_synt_C pfam00958
GMP synthase C terminal domain; GMP synthetase is a glutamine amidotransferase from the de ...
418-509 1.01e-64

GMP synthase C terminal domain; GMP synthetase is a glutamine amidotransferase from the de novo purine biosynthetic pathway. This family is the C-terminal domain specific to the GMP synthases EC:6.3.5.2. In prokaryotes this domain mediates dimerization. Eukaryotic GMP synthases are monomers. This domain in eukaryotes includes several large insertions that may form globular domains.


Pssm-ID: 425963 [Multi-domain]  Cd Length: 92  Bit Score: 204.57  E-value: 1.01e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478  418 EEIAKANLDETIWQYFACLPNIRSVGVMGDERTYCYTIALRAVISTDAMTSDWARIPYEVLDKVSRRIVNEVKGVNRIVY 497
Cdd:pfam00958   1 EEIKKAGLYRKIWQAFAVLLPVKSVGVMGDERTYEYVVALRAVTSTDGMTADWARLPYEVLEKISNRIVNEVPGVNRVVY 80
                          90
                  ....*....|..
gi 219567478  498 DITSKPPATIEW 509
Cdd:pfam00958  81 DITSKPPATIEW 92
PRK00758 PRK00758
GMP synthase subunit A; Validated
6-190 1.14e-54

GMP synthase subunit A; Validated


Pssm-ID: 179112 [Multi-domain]  Cd Length: 184  Bit Score: 181.59  E-value: 1.14e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478   6 VIVVDFGGQYNQLIARRVRENNVYCEIVPYTYSVDKIKEkNPRGIIFTGGPNSvydDNAPKISEDIFEIGVPVLGICYGH 85
Cdd:PRK00758   2 IVVVDNGGQYNHLIHRTLRYLGVDAKIIPNTTPVEEIKA-FEDGLILSGGPDI---ERAGNCPEYLKELDVPILGICLGH 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478  86 QLICTTLGGKVESAQVREYGKTDVVLNNSSGLFSGIDKNESCWMSHTDFVSYPPEGFKIIGKSGESPVAAVENIDKKIYG 165
Cdd:PRK00758  78 QLIAKAFGGEVGRGEYGEYALVEVEILDEDDILKGLPPEIRVWASHADEVKELPDGFEILARSDICEVEAMKHKEKPIYG 157
                        170       180
                 ....*....|....*....|....*
gi 219567478 166 VQFHPEVEHTPFGKKMLSNFLfDIC 190
Cdd:PRK00758 158 VQFHPEVAHTEYGEEIFKNFL-EIC 181
GATase pfam00117
Glutamine amidotransferase class-I;
7-189 4.89e-53

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 177.43  E-value: 4.89e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478    7 IVVDFGGQYNQLIARRVRENNVYCEIVPYTYSVDKIKEKNPRGIIFTGGPNSVYD-DNAPKISEDIFEIGVPVLGICYGH 85
Cdd:pfam00117   1 LLIDNGDSFTYNLARALRELGVEVTVVPNDTPAEEILEENPDGIILSGGPGSPGAaGGAIEAIREARELKIPILGICLGH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478   86 QLICTTLGGKVESAQVREY-GKTDVVLNNSSGLFSGIDKNESCWMSHTDFV--SYPPEGFKIIGKS--GESPVAAVENiD 160
Cdd:pfam00117  81 QLLALAFGGKVVKAKKFGHhGKNSPVGDDGCGLFYGLPNVFIVRRYHSYAVdpDTLPDGLEVTATSenDGTIMGIRHK-K 159
                         170       180
                  ....*....|....*....|....*....
gi 219567478  161 KKIYGVQFHPEVEHTPFGKKMLSNFLFDI 189
Cdd:pfam00117 160 LPIFGVQFHPESILTPHGPEILFNFFIKA 188
GATase1_1 cd01741
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
49-186 4.28e-28

Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group contains a subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain. GATase activity catalyses the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. Glutamine amidotransferases (GATase) includes the triad family of amidotransferases which have a conserved Cys-His-Glu catalytic triad in the glutaminase active site. In this subgroup this triad is conserved. GATase activity can be found in a range of biosynthetic enzymes, including: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase , anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase, cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. Glutamine amidotransferase (GATase) domains can occur either as single polypeptides, as in glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase.


Pssm-ID: 153212 [Multi-domain]  Cd Length: 188  Bit Score: 110.41  E-value: 4.28e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478  49 GIIFTGGPNSVYDDNAPKISE------DIFEIGVPVLGICYGHQLICTTLGGKVE-SAQVREYGKTDVVLNN---SSGLF 118
Cdd:cd01741   49 GLVILGGPMSVDEDDYPWLKKlkelirQALAAGKPVLGICLGHQLLARALGGKVGrNPKGWEIGWFPVTLTEagkADPLF 128
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 219567478 119 SGIDKNESCWMSHTDFVSYPPEGFKIIGKSGESPVAAVEnIDKKIYGVQFHPEvehtpfgKKMLSNFL 186
Cdd:cd01741  129 AGLPDEFPVFHWHGDTVVELPPGAVLLASSEACPNQAFR-YGDRALGLQFHPE-------ERLLRNFL 188
PRK05670 PRK05670
anthranilate synthase component II; Provisional
38-186 6.05e-26

anthranilate synthase component II; Provisional


Pssm-ID: 235552 [Multi-domain]  Cd Length: 189  Bit Score: 104.44  E-value: 6.05e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478  38 SVDKIKEKNPRGIIFTGGPNSvyddnaPK---ISEDI---FEIGVPVLGICYGHQLICTTLGGKVESAQVREYGKTDVVL 111
Cdd:PRK05670  35 TLEEIEALNPDAIVLSPGPGT------PAeagISLELireFAGKVPILGVCLGHQAIGEAFGGKVVRAKEIMHGKTSPIE 108
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 219567478 112 NNSSGLFSGIDKNESCWMSHTDFV--SYPPEGFKIIGKSGESPVAAVENIDKKIYGVQFHPEVEHTPFGKKMLSNFL 186
Cdd:PRK05670 109 HDGSGIFAGLPNPFTVTRYHSLVVdrESLPDCLEVTAWTDDGEIMGVRHKELPIYGVQFHPESILTEHGHKLLENFL 185
GATase1_Anthranilate_Synthase cd01743
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ...
15-186 7.32e-26

Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase (ASase). This group contains proteins similar to para-aminobenzoate (PABA) synthase and ASase. These enzymes catalyze similar reactions and produce similar products, PABA and ortho-aminobenzoate (anthranilate). Each enzyme is composed of non-identical subunits: a glutamine amidotransferase subunit (component II) and a subunit that produces an aminobenzoate products (component I). ASase catalyses the synthesis of anthranilate from chorismate and glutamine and is a tetrameric protein comprising two copies each of components I and II. Component II of ASase belongs to the family of triad GTases which hydrolyze glutamine and transfer nascent ammonia between the active sites. In some bacteria, such as Escherichia coli, component II can be much larger than in other organisms, due to the presence of phosphoribosyl-anthranilate transferase (PRTase) activity. PRTase catalyses the second step in tryptophan biosynthesis and results in the addition of 5-phosphoribosyl-1-pyrophosphate to anthranilate to create N-5'-phosphoribosyl-anthranilate. In E.coli, the first step in the conversion of chorismate to PABA involves two proteins: PabA and PabB which co-operate to transfer the amide nitrogen of glutamine to chorismate forming 4-amino-4 deoxychorismate (ADC). PabA acts as a glutamine amidotransferase, supplying an amino group to PabB, which carries out the amination reaction. A third protein PabC then mediates elimination of pyruvate and aromatization to give PABA. Several organisms have bipartite proteins containing fused domains homologous to PabA and PabB commonly called PABA synthases. These hybrid PABA synthases may produce ADC and not PABA.


Pssm-ID: 153214 [Multi-domain]  Cd Length: 184  Bit Score: 104.15  E-value: 7.32e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478  15 YNqlIARRVRENNVYCEIVPYT-YSVDKIKEKNPRGIIFTGGPNSvyddnaPKISEDIFEI------GVPVLGICYGHQL 87
Cdd:cd01743   12 YN--LVQYLRELGAEVVVVRNDeITLEELELLNPDAIVISPGPGH------PEDAGISLEIiralagKVPILGVCLGHQA 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478  88 ICTTLGGKVESAQVREYGKTDVVLNNSSGLFSGIDKNESCWMSHT---DFVSyPPEGFKIIGKSGESPVAAVENIDKKIY 164
Cdd:cd01743   84 IAEAFGGKVVRAPEPMHGKTSEIHHDGSGLFKGLPQPFTVGRYHSlvvDPDP-LPDLLEVTASTEDGVIMALRHRDLPIY 162
                        170       180
                 ....*....|....*....|..
gi 219567478 165 GVQFHPEVEHTPFGKKMLSNFL 186
Cdd:cd01743  163 GVQFHPESILTEYGLRLLENFL 184
PabA COG0512
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ...
15-186 5.35e-25

Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid transport and metabolism, Coenzyme transport and metabolism]; Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis


Pssm-ID: 440278 [Multi-domain]  Cd Length: 189  Bit Score: 101.65  E-value: 5.35e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478  15 YNqlIARRVRENNVYCEIVPYT-YSVDKIKEKNPRGIIFTGGPNSVydDNAPkISEDI---FEIGVPVLGICYGHQLICT 90
Cdd:COG0512   12 YN--LVQYLGELGAEVVVVRNDeITLEEIEALAPDGIVLSPGPGTP--EEAG-ISLEViraFAGKIPILGVCLGHQAIGE 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478  91 TLGGKVESAQVREYGKTDVVLNNSSGLFSGIDKNESCWMSHTDFVSYP--PEGFKIIGKSGESPVAAVENIDKKIYGVQF 168
Cdd:COG0512   87 AFGGKVVRAPEPMHGKTSPITHDGSGLFAGLPNPFTATRYHSLVVDREtlPDELEVTAWTEDGEIMGIRHRELPIEGVQF 166
                        170
                 ....*....|....*...
gi 219567478 169 HPEVEHTPFGKKMLSNFL 186
Cdd:COG0512  167 HPESILTEHGHQLLANFL 184
PRK14607 PRK14607
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;
38-186 2.83e-22

bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;


Pssm-ID: 237764 [Multi-domain]  Cd Length: 534  Bit Score: 100.18  E-value: 2.83e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478  38 SVDKIKEKNPRGIIFTGGPNSvyddnaPK---ISEDI---FEIGVPVLGICYGHQLICTTLGGKVESAQVREYGKTDVVL 111
Cdd:PRK14607  36 TIEEIEALNPSHIVISPGPGR------PEeagISVEVirhFSGKVPILGVCLGHQAIGYAFGGKIVHAKRILHGKTSPID 109
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 219567478 112 NNSSGLFSGIDKNESCWMSHTDFV--SYPPEGFKIIGKSGESPVAAVENIDKKIYGVQFHPEVEHTPFGKKMLSNFL 186
Cdd:PRK14607 110 HNGKGLFRGIPNPTVATRYHSLVVeeASLPECLEVTAKSDDGEIMGIRHKEHPIFGVQFHPESILTEEGKRILKNFL 186
trpG CHL00101
anthranilate synthase component 2
38-186 1.90e-18

anthranilate synthase component 2


Pssm-ID: 214365 [Multi-domain]  Cd Length: 190  Bit Score: 83.24  E-value: 1.90e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478  38 SVDKIKEKNPRGIIFTGGPNSVYDDNapkISEDI---FEIGVPVLGICYGHQLICTTLGGKVESAQVREYGKTDVVLNNS 114
Cdd:CHL00101  35 DLSKIKNLNIRHIIISPGPGHPRDSG---ISLDVissYAPYIPILGVCLGHQSIGYLFGGKIIKAPKPMHGKTSKIYHNH 111
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 219567478 115 SGLFSGIDKNESCWMSHTDFV--SYPPEGFKIIGKSGESPVAAVENID-KKIYGVQFHPEVEHTPFGKKMLSNFL 186
Cdd:CHL00101 112 DDLFQGLPNPFTATRYHSLIIdpLNLPSPLEITAWTEDGLIMACRHKKyKMLRGIQFHPESLLTTHGQQILRNFL 186
PRK07649 PRK07649
aminodeoxychorismate/anthranilate synthase component II;
38-186 3.42e-16

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181066 [Multi-domain]  Cd Length: 195  Bit Score: 76.77  E-value: 3.42e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478  38 SVDKIKEKNPRGIIFTGGPNSvydDNAPKISEDI---FEIGVPVLGICYGHQLICTTLGGKVESAQVREYGKTDVVLNNS 114
Cdd:PRK07649  35 TISDIENMKPDFLMISPGPCS---PNEAGISMEViryFAGKIPIFGVCLGHQSIAQVFGGEVVRAERLMHGKTSLMHHDG 111
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 219567478 115 SGLFSGIDKNESCWMSHTDFVSYP--PEGFKIIGKSGESPVAAVENIDKKIYGVQFHPEVEHTPFGKKMLSNFL 186
Cdd:PRK07649 112 KTIFSDIPNPFTATRYHSLIVKKEtlPDCLEVTSWTEEGEIMAIRHKTLPIEGVQFHPESIMTSHGKELLQNFI 185
GATase1_CPSase cd01744
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ...
6-171 1.53e-15

Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This group of sequences represents the small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II. CPSase II catalyzes the production of carbomyl phosphate (CP) from bicarbonate, glutamine and two molecules of MgATP. The reaction is believed to proceed by a series of four biochemical reactions involving a minimum of three discrete highly reactive intermediates. The synthesis of CP is critical for the initiation of two separate biosynthetic pathways. In one CP is coupled to aspartate, its carbon and nitrogen nuclei ultimately incorporated into the aromatic moieties of pyrimidine nucleotides. In the second pathway CP is condensed with ornithine at the start of the urea cycle and is utilized for the detoxification of ammonia and biosynthesis of arginine. CPSases may be encoded by one or by several genes, depending on the species. The E.coli enzyme is a heterodimer consisting of two polypeptide chains referred to as the small and large subunit. Ammonia an intermediate during the biosynthesis of carbomyl phosphate produced by the hydrolysis of glutamine in the small subunit of the enzyme is delivered via a molecular tunnel between the remotely located carboxyphosphate active site in the large subunit. CPSase IIs belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site. This group also contains the sequence from the mammalian urea cycle form which has lost the active site Cys, resulting in an ammonia-dependent form, CPSase I.


Pssm-ID: 153215 [Multi-domain]  Cd Length: 178  Bit Score: 74.46  E-value: 1.53e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478   6 VIVVDFGGQYNQLiaRRVRENNVYCEIVPYTYSVDKIKEKNPRGIIFTGGPNSVYD-DNAPKISEDIFEIGVPVLGICYG 84
Cdd:cd01744    1 VVVIDFGVKHNIL--RELLKRGCEVTVVPYNTDAEEILKLDPDGIFLSNGPGDPALlDEAIKTVRKLLGKKIPIFGICLG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478  85 HQLICTTLGGKVESAQVREYGKTDVVLNNSSGlfsgidkneSCWMS---HtdfvsyppeGFKIIGKSGESPVAA------ 155
Cdd:cd01744   79 HQLLALALGAKTYKMKFGHRGSNHPVKDLITG---------RVYITsqnH---------GYAVDPDSLPGGLEVthvnln 140
                        170       180
                 ....*....|....*....|..
gi 219567478 156 ---VENI---DKKIYGVQFHPE 171
Cdd:cd01744  141 dgtVEGIrhkDLPVFSVQFHPE 162
PRK09065 PRK09065
glutamine amidotransferase; Provisional
48-171 1.70e-15

glutamine amidotransferase; Provisional


Pssm-ID: 181635 [Multi-domain]  Cd Length: 237  Bit Score: 75.77  E-value: 1.70e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478  48 RGIIFTGGPNSVyDDNAP---KISEDIFE---IGVPVLGICYGHQLICTTLGGKV-ESAQVREYGKTDVVLNNSSG---L 117
Cdd:PRK09065  56 AGVIITGSWAMV-TDRLDwseRTADWLRQaaaAGMPLLGICYGHQLLAHALGGEVgYNPAGRESGTVTVELHPAAAddpL 134
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 219567478 118 FSGIDKNESCWMSHTDFVSYPPEGFKIIGKSGESPVAAVEnIDKKIYGVQFHPE 171
Cdd:PRK09065 135 FAGLPAQFPAHLTHLQSVLRLPPGAVVLARSAQDPHQAFR-YGPHAWGVQFHPE 187
PLN02335 PLN02335
anthranilate synthase
30-186 2.61e-15

anthranilate synthase


Pssm-ID: 177969 [Multi-domain]  Cd Length: 222  Bit Score: 75.22  E-value: 2.61e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478  30 CEIVPY---TYSVDKIKEKNPRGIIFTGGPNSVYDDNapkIS-EDIFEIG--VPVLGICYGHQLICTTLGGKVesaqVRE 103
Cdd:PLN02335  43 CHFEVYrndELTVEELKRKNPRGVLISPGPGTPQDSG---ISlQTVLELGplVPLFGVCMGLQCIGEAFGGKI----VRS 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478 104 -----YGKTDVVLNNS---SGLFSGIDKNESCWMSHTDFV---SYPPEGFKIIGKSGESPVAAVEN-IDKKIYGVQFHPE 171
Cdd:PLN02335 116 pfgvmHGKSSPVHYDEkgeEGLFSGLPNPFTAGRYHSLVIekdTFPSDELEVTAWTEDGLIMAARHrKYKHIQGVQFHPE 195
                        170
                 ....*....|....*
gi 219567478 172 VEHTPFGKKMLSNFL 186
Cdd:PLN02335 196 SIITTEGKTIVRNFI 210
CPSaseIIsmall TIGR01368
carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small ...
3-188 1.80e-14

carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small chain of the glutamine-dependent form (EC 6.3.5.5) of carbamoyl phosphate synthase, CPSase II. The C-terminal domain has glutamine amidotransferase activity. Note that the sequence from the mammalian urea cycle form has lost the active site Cys, resulting in an ammonia-dependent form, CPSase I (EC 6.3.4.16). CPSases of pyrimidine biosynthesis, arginine biosynthesis, and the urea cycle may be encoded by one or by several genes, depending on the species. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]


Pssm-ID: 273580 [Multi-domain]  Cd Length: 357  Bit Score: 74.58  E-value: 1.80e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478    3 RELVIVVDFGGQYNqlIARRVRENNVYCEIVPYTYSVDKIKEKNPRGIIFTGGPN--SVYDDNAPKISEDIFEIgvPVLG 80
Cdd:TIGR01368 172 GKRVVVIDFGVKRN--ILRRLVKRGCEVTVVPYDTDAEEIKKYNPDGIFLSNGPGdpAAVEPAIETIRKLLEKI--PIFG 247
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478   81 ICYGHQLICTTLGGKVESAQVREYGKTDVVLNNSSGlfsgidkneSCWMS---H---TDFVSYPPEGFKIIGKS-GESPV 153
Cdd:TIGR01368 248 ICLGHQLLALAFGAKTYKMKFGHRGGNHPVKDLITG---------RVEITsqnHgyaVDPDSLPAGDLEVTHVNlNDGTV 318
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 219567478  154 AAVENIDKKIYGVQFHPEVEHTPFGkkmlSNFLFD 188
Cdd:TIGR01368 319 EGIRHKDLPVFSVQYHPEASPGPHD----TEYLFD 349
PRK08007 PRK08007
aminodeoxychorismate synthase component 2;
38-186 2.16e-14

aminodeoxychorismate synthase component 2;


Pssm-ID: 181194 [Multi-domain]  Cd Length: 187  Bit Score: 71.49  E-value: 2.16e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478  38 SVDKIKEKNPRGIIFTGGPNSvydDNAPKISEDI---FEIGVPVLGICYGHQLICTTLGGKVESAQVREYGKTDVVLNNS 114
Cdd:PRK08007  35 TLADIDALKPQKIVISPGPCT---PDEAGISLDVirhYAGRLPILGVCLGHQAMAQAFGGKVVRAAKVMHGKTSPITHNG 111
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 219567478 115 SGLFSGIDKNESCWMSHTDFVSYP--PEGFKIIGKSGESPVAAVENIDKKIYGVQFHPEVEHTPFGKKMLSNFL 186
Cdd:PRK08007 112 EGVFRGLANPLTVTRYHSLVVEPDslPACFEVTAWSETREIMGIRHRQWDLEGVQFHPESILSEQGHQLLANFL 185
trpG_papA TIGR00566
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This ...
40-186 5.54e-14

glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This model describes the glutamine amidotransferase domain or peptide of the tryptophan-biosynthetic pathway enzyme anthranilate synthase or of the folate biosynthetic pathway enzyme para-aminobenzoate synthase. In at least one case, a single polypeptide from Bacillus subtilis was shown to have both functions. This model covers a subset of the sequences described by the Pfam model GATase.


Pssm-ID: 273144 [Multi-domain]  Cd Length: 188  Bit Score: 70.20  E-value: 5.54e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478   40 DKIKEKNPRGIIFTGGPnsVYDDNApKISEDIFE--IG-VPVLGICYGHQLICTTLGGKVESAQVREYGKTDVVLNNSSG 116
Cdd:TIGR00566  37 QEIEALLPLLIVISPGP--CTPNEA-GISLEAIRhfAGkLPILGVCLGHQAMGQAFGGDVVRANTVMHGKTSEIEHNGAG 113
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 219567478  117 LFSGIDKNESCWMSHTDFVSypPEG----FKIIGKSGESP-VAAVENIDKKIYGVQFHPEVEHTPFGKKMLSNFL 186
Cdd:TIGR00566 114 IFRGLFNPLTATRYHSLVVE--PETlptcFPVTAWEEENIeIMAIRHRDLPLEGVQFHPESILSEQGHQLLANFL 186
Peptidase_C26 pfam07722
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ...
49-171 4.40e-13

Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze the cleavage of the gamma-glutamyl bond in poly-gamma-glutamyl substrates. They are structurally related to pfam00117, but contain extensions in four loops and at the C terminus.


Pssm-ID: 429620 [Multi-domain]  Cd Length: 219  Bit Score: 68.44  E-value: 4.40e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478   49 GIIFTGGPN---SVYDDNA-PKISE-----DIFEI---------GVPVLGICYGHQLICTTLGG--------------KV 96
Cdd:pfam07722  61 GLLLTGGPNvdpHFYGEEPsESGGPydparDAYELaliraalarGKPILGICRGFQLLNVALGGtlyqdiqeqpgftdHR 140
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 219567478   97 ESAQVREYGKTDVVLNNSSGLFSGIDKNESCWMS--HTDFVSYPPEGFKIIGKSGESPVAAVE--NIDKKIYGVQFHPE 171
Cdd:pfam07722 141 EHCQVAPYAPSHAVNVEPGSLLASLLGSEEFRVNslHHQAIDRLAPGLRVEAVAPDGTIEAIEspNAKGFALGVQWHPE 219
PRK07765 PRK07765
aminodeoxychorismate/anthranilate synthase component II;
75-214 5.35e-13

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181107 [Multi-domain]  Cd Length: 214  Bit Score: 68.15  E-value: 5.35e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478  75 GVPVLGICYGHQLICTTLGGKVESAQVREYGKTDVVLNNSSGLFSGIDKNESCWMSHTDFV---SYPPEgFKIIGKSGES 151
Cdd:PRK07765  76 GTPLLGVCLGHQAIGVAFGATVDRAPELLHGKTSSVHHTGVGVLAGLPDPFTATRYHSLTIlpeTLPAE-LEVTARTDSG 154
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 219567478 152 PVAAVENIDKKIYGVQFHPEVEHTPFGKKMLSNFLfDICNLKGDwsmssfvDEKIKSIKEEVG 214
Cdd:PRK07765 155 VIMAVRHRELPIHGVQFHPESVLTEGGHRMLANWL-TVCGWAPD-------EALVRRLENEVA 209
PRK08857 PRK08857
aminodeoxychorismate/anthranilate synthase component II;
39-186 2.64e-12

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181566 [Multi-domain]  Cd Length: 193  Bit Score: 65.67  E-value: 2.64e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478  39 VDKIKEKNPRGIIFTGGPNSVYDDNAPKISEDIFEIGVPVLGICYGHQLICTTLGGKVESAQVREYGKTDVVLNNSSGLF 118
Cdd:PRK08857  36 IDGIEALNPTHLVISPGPCTPNEAGISLQAIEHFAGKLPILGVCLGHQAIAQVFGGQVVRARQVMHGKTSPIRHTGRSVF 115
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 219567478 119 SGIDKNESCWMSHTDFVSYP--PEGFKIIG----KSGE-SPVAAVENIDKKIYGVQFHPEVEHTPFGKKMLSNFL 186
Cdd:PRK08857 116 KGLNNPLTVTRYHSLVVKNDtlPECFELTAwtelEDGSmDEIMGFQHKTLPIEAVQFHPESIKTEQGHQLLANFL 190
CarA COG0505
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ...
6-95 3.21e-12

Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Carbamoylphosphate synthase small subunit is part of the Pathway/BioSystem: Arginine biosynthesis


Pssm-ID: 440271 [Multi-domain]  Cd Length: 361  Bit Score: 67.74  E-value: 3.21e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478   6 VIVVDFGGQYNqlIARRVRENNVYCEIVPYTYSVDKIKEKNPRGIIFTGGPN--SVYDDNAPKISEdIFEIGVPVLGICY 83
Cdd:COG0505  179 VVALDFGVKRN--ILRELAERGCRVTVVPATTSAEEILALNPDGVFLSNGPGdpAALDYAIETIRE-LLGKGIPIFGICL 255
                         90
                 ....*....|..
gi 219567478  84 GHQLICTTLGGK 95
Cdd:COG0505  256 GHQLLALALGAK 267
hisH PRK13181
imidazole glycerol phosphate synthase subunit HisH; Provisional
73-186 3.23e-12

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 183878 [Multi-domain]  Cd Length: 199  Bit Score: 65.66  E-value: 3.23e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478  73 EIGVPVLGICYGHQLICTT--------LG---GKV-----ESAQVREYGKTDVVLNNSSGLFSGIDKNESCWMSHTDFVs 136
Cdd:PRK13181  70 EKKQPVLGICLGMQLLFESseegnvkgLGlipGDVkrfrsEPLKVPQMGWNSVKPLKESPLFKGIEEGSYFYFVHSYYV- 148
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 219567478 137 yPPEGFKIIGKS---GESPVAAVENidKKIYGVQFHPEVEHtPFGKKMLSNFL 186
Cdd:PRK13181 149 -PCEDPEDVLATteyGVPFCSAVAK--DNIYAVQFHPEKSG-KAGLKLLKNFA 197
PRK06895 PRK06895
anthranilate synthase component II;
78-186 1.74e-11

anthranilate synthase component II;


Pssm-ID: 235882 [Multi-domain]  Cd Length: 190  Bit Score: 63.22  E-value: 1.74e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478  78 VLGICYGHQLICTTLGGKVES-AQVREYGKTDVVLNNSSGLFSGIDKNESCWMSHTDFVSYP--PEGFKIIGKSGESPVA 154
Cdd:PRK06895  75 ILGVCLGHQTLCEFFGGELYNlNNVRHGQQRPLKVRSNSPLFDGLPEEFNIGLYHSWAVSEEnfPTPLEITAVCDENVVM 154
                         90       100       110
                 ....*....|....*....|....*....|..
gi 219567478 155 AVENIDKKIYGVQFHPEVEHTPFGKKMLSNFL 186
Cdd:PRK06895 155 AMQHKTLPIYGVQFHPESYISEFGEQILRNWL 186
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
6-105 1.78e-11

Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase (GATase1)-like domain. This group includes proteins similar to Class I glutamine amidotransferases, the intracellular PH1704 from Pyrococcus horikoshii, the C-terminal of the large catalase: Escherichia coli HP-II, Sinorhizobium meliloti Rm1021 ThuA. and, the A4 beta-galactosidase middle domain. The majority of proteins in this group have a reactive Cys found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For Class I glutamine amidotransferases proteins which transfer ammonia from the amide side chain of glutamine to an acceptor substrate, this Cys forms a Cys-His-Glu catalytic triad in the active site. Glutamine amidotransferases activity can be found in a range of biosynthetic enzymes included in this cd: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase, anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase, cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. For Pyrococcus horikoshii PH1704, the Cys of the nucleophile elbow together with a different His and, a Glu from an adjacent monomer form a catalytic triad different from the typical GATase1 triad. The E. coli HP-II C-terminal domain, S. meliloti Rm1021 ThuA and the A4 beta-galactosidase middle domain lack the catalytic triad typical GATaseI domains. GATase1-like domains can occur either as single polypeptides, as in Class I glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase.


Pssm-ID: 153210 [Multi-domain]  Cd Length: 115  Bit Score: 61.08  E-value: 1.78e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478   6 VIVVDFGGQYN---QLIARRVRENNVYCEIVPYT--YSVDKIKEKNPRGIIFTGGPNSVYD--DNAPKISE--DIFEIGV 76
Cdd:cd01653    1 VAVLLFPGFEElelASPLDALREAGAEVDVVSPDggPVESDVDLDDYDGLILPGGPGTPDDlaRDEALLALlrEAAAAGK 80
                         90       100
                 ....*....|....*....|....*....
gi 219567478  77 PVLGICYGHQLICTTLGGKVESAQVREYG 105
Cdd:cd01653   81 PILGICLGAQLLVLGVQFHPEAIDGAEAG 109
PRK12564 PRK12564
carbamoyl-phosphate synthase small subunit;
6-97 1.80e-11

carbamoyl-phosphate synthase small subunit;


Pssm-ID: 237139 [Multi-domain]  Cd Length: 360  Bit Score: 65.48  E-value: 1.80e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478   6 VIVVDFGGQYNqlIARRVRENNVYCEIVPYTYSVDKIKEKNPRGIIFTGGPN--SVYDDNAPKISEdIFEIGVPVLGICY 83
Cdd:PRK12564 180 VVAIDFGVKRN--ILRELAERGCRVTVVPATTTAEEILALNPDGVFLSNGPGdpAALDYAIEMIRE-LLEKKIPIFGICL 256
                         90
                 ....*....|....
gi 219567478  84 GHQLICTTLGGKVE 97
Cdd:PRK12564 257 GHQLLALALGAKTY 270
PLN02771 PLN02771
carbamoyl-phosphate synthase (glutamine-hydrolyzing)
6-116 2.04e-11

carbamoyl-phosphate synthase (glutamine-hydrolyzing)


Pssm-ID: 178370 [Multi-domain]  Cd Length: 415  Bit Score: 65.77  E-value: 2.04e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478   6 VIVVDFGGQYNqlIARRVRENNVYCEIVPYTYSVDKIKEKNPRGIIFTGGPNsvyDDNA-PKISEDIFEI--GVPVLGIC 82
Cdd:PLN02771 243 VIAYDFGIKHN--ILRRLASYGCKITVVPSTWPASEALKMKPDGVLFSNGPG---DPSAvPYAVETVKELlgKVPVFGIC 317
                         90       100       110
                 ....*....|....*....|....*....|....
gi 219567478  83 YGHQLICTTLGGKVESAQVREYGKTDVVLNNSSG 116
Cdd:PLN02771 318 MGHQLLGQALGGKTFKMKFGHHGGNHPVRNNRTG 351
PRK12838 PRK12838
carbamoyl phosphate synthase small subunit; Reviewed
6-171 9.04e-11

carbamoyl phosphate synthase small subunit; Reviewed


Pssm-ID: 183784 [Multi-domain]  Cd Length: 354  Bit Score: 63.37  E-value: 9.04e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478   6 VIVVDFGgqYNQLIARRVRENNVYCEIVPYTYSVDKIKEKNPRGIIFTGGPNSV--YDDNAPKIsEDIFEiGVPVLGICY 83
Cdd:PRK12838 170 VALIDFG--YKKSILRSLSKRGCKVTVLPYDTSLEEIKNLNPDGIVLSNGPGDPkeLQPYLPEI-KKLIS-SYPILGICL 245
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478  84 GHQLICTTLGGKVESAQVREYGKTDVVLNNSSGlfsgidkneSCWMS---HtDFV----SYPPEGFKI--IGKSGESpVA 154
Cdd:PRK12838 246 GHQLIALALGADTEKLPFGHRGANHPVIDLTTG---------RVWMTsqnH-GYVvdedSLDGTPLSVrfFNVNDGS-IE 314
                        170
                 ....*....|....*..
gi 219567478 155 AVENIDKKIYGVQFHPE 171
Cdd:PRK12838 315 GLRHKKKPVLSVQFHPE 331
PRK05665 PRK05665
amidotransferase; Provisional
69-174 2.23e-10

amidotransferase; Provisional


Pssm-ID: 168162 [Multi-domain]  Cd Length: 240  Bit Score: 60.98  E-value: 2.23e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478  69 EDIFEIGVPVLGICYGHQLICTTLGGKVESA-QVREYGKTDVVLNNSSGLFSGIDKNESCWMSHTDFVSYPPEGFKIIGK 147
Cdd:PRK05665  85 LKLYERGDKLLGVCFGHQLLALLLGGKAERAsQGWGVGIHRYQLAAHAPWMSPAVTELTLLISHQDQVTALPEGATVIAS 164
                         90       100
                 ....*....|....*....|....*..
gi 219567478 148 SGESPVAAVeNIDKKIYGVQFHPEVEH 174
Cdd:PRK05665 165 SDFCPFAAY-HIGDQVLCFQGHPEFVH 190
carA CHL00197
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional
6-188 2.78e-10

carbamoyl-phosphate synthase arginine-specific small subunit; Provisional


Pssm-ID: 214392 [Multi-domain]  Cd Length: 382  Bit Score: 62.12  E-value: 2.78e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478   6 VIVVDFGGQYNqlIARRVRENNVYCEIVPYTYSVDKIKEKNPRGIIFTGGPN--SVYDDNAPKISEdIFEIGVPVLGICY 83
Cdd:CHL00197 195 IIVIDFGVKYN--ILRRLKSFGCSITVVPATSPYQDILSYQPDGILLSNGPGdpSAIHYGIKTVKK-LLKYNIPIFGICM 271
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478  84 GHQLICTTLGGKVESAQVREYGktdvvLNNSSGLFSgidKNESCWMSH---TDFVSYPPEGFKIIGKS-GESPVAAVENI 159
Cdd:CHL00197 272 GHQILSLALEAKTFKLKFGHRG-----LNHPSGLNQ---QVEITSQNHgfaVNLESLAKNKFYITHFNlNDGTVAGISHS 343
                        170       180
                 ....*....|....*....|....*....
gi 219567478 160 DKKIYGVQFHPEVEHTPFGkkmlSNFLFD 188
Cdd:CHL00197 344 PKPYFSVQYHPEASPGPHD----ADYLFE 368
IMP_synth_hisH TIGR01855
imidazole glycerol phosphate synthase, glutamine amidotransferase subunit; This model ...
66-186 4.27e-10

imidazole glycerol phosphate synthase, glutamine amidotransferase subunit; This model represents the glutamine amidotransferase subunit (or domain, in eukaryotic systems) of imidazole glycerol phosphate synthase. This subunit catalyzes step 5 of histidine biosynthesis from PRPP. The other subunit, the cyclase, catalyzes step 6. [Amino acid biosynthesis, Histidine family]


Pssm-ID: 273836 [Multi-domain]  Cd Length: 196  Bit Score: 59.26  E-value: 4.27e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478   66 KISEDIFEIGVPVLGICYGHQLI---------CTTLG---GKV---ESAQVREYGKTDVVLNNSSGLFSGIDKNESCWMS 130
Cdd:TIGR01855  62 LFVELVVRLGKPVLGICLGMQLLferseegggVPGLGlikGNVvklEARKVPHMGWNEVHPVKESPLLNGIDEGAYFYFV 141
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478  131 HtdfvSY--PPEGFKIIGKS--GESPVAAVEniDKKIYGVQFHPEVEHTpFGKKMLSNFL 186
Cdd:TIGR01855 142 H----SYyaVCEEEAVLAYAdyGEKFPAAVQ--KGNIFGTQFHPEKSGK-TGLKLLENFL 194
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
6-88 6.48e-10

Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase (GATase1)-like domain. This group contains proteins similar to Class I glutamine amidotransferases, the intracellular PH1704 from Pyrococcus horikoshii, the C-terminal of the large catalase: Escherichia coli HP-II, Sinorhizobium meliloti Rm1021 ThuA, the A4 beta-galactosidase middle domain and peptidase E. The majority of proteins in this group have a reactive Cys found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For Class I glutamine amidotransferases proteins which transfer ammonia from the amide side chain of glutamine to an acceptor substrate, this Cys forms a Cys-His-Glu catalytic triad in the active site. Glutamine amidotransferases activity can be found in a range of biosynthetic enzymes included in this cd: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase, anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase (CPSase), cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. For Pyrococcus horikoshii PH1704, the Cys of the nucleophile elbow together with a different His and, a Glu from an adjacent monomer form a catalytic triad different from the typical GATase1 triad. Peptidase E is believed to be a serine peptidase having a Ser-His-Glu catalytic triad which differs from the Cys-His-Glu catalytic triad of typical GATase1 domains, by having a Ser in place of the reactive Cys at the nucleophile elbow. The E. coli HP-II C-terminal domain, S. meliloti Rm1021 ThuA and the A4 beta-galactosidase middle domain lack the catalytic triad typical GATaseI domains. GATase1-like domains can occur either as single polypeptides, as in Class I glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase. Peptidase E has a circular permutation in the common core of a typical GTAse1 domain.


Pssm-ID: 153222 [Multi-domain]  Cd Length: 92  Bit Score: 56.05  E-value: 6.48e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478   6 VIVVDFGGQYN---QLIARRVRENNVYCEIVPYT--YSVDKIKEKNPRGIIFTGGPNSVYD--DNAPKISE--DIFEIGV 76
Cdd:cd03128    1 VAVLLFGGSEElelASPLDALREAGAEVDVVSPDggPVESDVDLDDYDGLILPGGPGTPDDlaWDEALLALlrEAAAAGK 80
                         90
                 ....*....|..
gi 219567478  77 PVLGICYGHQLI 88
Cdd:cd03128   81 PVLGICLGAQLL 92
GATase1_IGP_Synthase cd01748
Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate ...
75-186 7.32e-10

Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate synthase (IGPS); Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate synthase (IGPS). IGPS incorporates ammonia derived from glutamine into N1-[(5'-phosphoribulosyl)-formimino]-5-aminoimidazole-4-carboxamide ribonucleotide (PRFAR) to form 5'-(5-aminoimidazole-4-carboxamide) ribonucleotide (AICAR) and imidazole glycerol phosphate (IGP). The glutamine amidotransferase domain generates the ammonia nucleophile which is channeled from the glutaminase active site to the PRFAR active site. IGPS belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site.


Pssm-ID: 153219 [Multi-domain]  Cd Length: 198  Bit Score: 58.66  E-value: 7.32e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478  75 GVPVLGICYGHQLICTT---------LG---GKVESAQVREYGKT------DVVLNNSSGLFSGIDKNescwmSHTDFV- 135
Cdd:cd01748   71 GKPFLGICLGMQLLFESseegggtkgLGlipGKVVRFPASEGLKVphmgwnQLEITKESPLFKGIPDG-----SYFYFVh 145
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 219567478 136 SY---PPEGFKIIGKS--GESPVAAVENidKKIYGVQFHPEVEHTpFGKKMLSNFL 186
Cdd:cd01748  146 SYyapPDDPDYILATTdyGGKFPAAVEK--DNIFGTQFHPEKSGK-AGLKLLKNFL 198
GATase1_2 cd01745
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
32-171 7.71e-10

Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group contains a subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain. GATase activity catalyses the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. Glutamine amidotransferases (GATase) includes the triad family of amidotransferases which have a conserved Cys-His-Glu catalytic triad in the glutaminase active site. In this subgroup this triad is conserved. GATase activity can be found in a range of biosynthetic enzymes, including: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase , anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase, cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. Glutamine amidotransferase (GATase) domains can occur either as single polypeptides, as in glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase.


Pssm-ID: 153216 [Multi-domain]  Cd Length: 189  Bit Score: 58.36  E-value: 7.71e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478  32 IVPYTYSVDKIKE--KNPRGIIFTGGPN----SVYDDNAPKISE-----DIFEI---------GVPVLGICYGHQLICTT 91
Cdd:cd01745   37 LLPPVDDEEDLEQylELLDGLLLTGGGDvdppLYGEEPHPELGPidperDAFELallraalerGKPILGICRGMQLLNVA 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478  92 LGGKVEsaQvreygktDVVLNnsSGLFSGIDKnescwmshtdfvsyPPEGFKIIGKSGESPVAAVENIDKK-IYGVQFHP 170
Cdd:cd01745  117 LGGTLY--Q-------DIRVN--SLHHQAIKR--------------LADGLRVEARAPDGVIEAIESPDRPfVLGVQWHP 171

                 .
gi 219567478 171 E 171
Cdd:cd01745  172 E 172
PRK06774 PRK06774
aminodeoxychorismate synthase component II;
42-186 9.87e-10

aminodeoxychorismate synthase component II;


Pssm-ID: 180689 [Multi-domain]  Cd Length: 191  Bit Score: 57.95  E-value: 9.87e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478  42 IKEKNPRGIIFTGGPNSvydDNAPKISEDI---FEIGVPVLGICYGHQLICTTLGGKVESAQVREYGKTDVVLNNSSGLF 118
Cdd:PRK06774  39 IEQLAPSHLVISPGPCT---PNEAGISLAVirhFADKLPILGVCLGHQALGQAFGARVVRARQVMHGKTSAICHSGQGVF 115
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 219567478 119 SGIDKNESCWMSHTDFVSYP--PEGFKIIGKSGES----PVAAVENIDKKIYGVQFHPEVEHTPFGKKMLSNFL 186
Cdd:PRK06774 116 RGLNQPLTVTRYHSLVIAADslPGCFELTAWSERGgemdEIMGIRHRTLPLEGVQFHPESILSEQGHQLLDNFL 189
LarE-like cd01990
Lactate racemization operon protein LarE and similar proteins; This subfamily includes ...
217-407 9.94e-10

Lactate racemization operon protein LarE and similar proteins; This subfamily includes Lactiplantibacillus plantarum LarE, a sacrificial sulfur insertase of the N-type ATP pyrophosphatase family. LarE is part of the lar operon, encoding five Lar proteins (LarA-E) that collaboratively synthesize and incorporate a niacin-derived Ni-containing cofactor into LarA, an Ni-dependent lactate racemase. It catalyzes successive thiolation reactions by donating the sulfur atom of their exclusive cysteine residues to the substrate. The LarE-like subfamily belongs to the nucleotide alpha hydrolase (AANH) superfamily that includes N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to the adenosine group. Proteins from this subfamily probably binds ATP. This domain is about 200 amino acids long with a strongly conserved motif SGGxDS at the N-terminus.


Pssm-ID: 467494 [Multi-domain]  Cd Length: 222  Bit Score: 58.81  E-value: 9.94e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478 217 KVICAMSGGVDSSVAAMIVHKAVGKQLTCIFVDHGLLRKDEGDQVEDIFKKqfnmnfIRVNAEKRFLQKLKD---ISDPE 293
Cdd:cd01990    1 KVVVAFSGGVDSSLLAKLAKEVLGDNVVAVTADSPLVPREELEEAKRIAEE------IGIRHEIIKTDELDDeeyVANDP 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478 294 KK----RKIIGEEFIrvfeEEAKKLGeIAFLVQGTIYPDVVESGLGTSATIKSHHNVgglpedmdfkliePLRE--LFKD 367
Cdd:cd01990   75 DRcyhcKKALYSTLK----EIAKERG-YDVVLDGTNADDLKDYRPGLLAAAELGIRS-------------PLPElgLTKS 136
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 219567478 368 EVRAVGEELGIPhklVWRQPfPGPGLAIRVLGN--ITEEKLQ 407
Cdd:cd01990  137 EIRELARELGLP---NWDKP-ASACLASRIPYGeeITPERLK 174
hisH PRK13141
imidazole glycerol phosphate synthase subunit HisH; Provisional
75-186 1.13e-09

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237288 [Multi-domain]  Cd Length: 205  Bit Score: 58.22  E-value: 1.13e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478  75 GVPVLGICYGHQLI---------CTTLG---GKVESAQVREYGK------TDVVLNNSSGLFSGIDKNescwmSHTDFV- 135
Cdd:PRK13141  72 GKPLLGICLGMQLLfesseefgeTEGLGllpGRVRRFPPEEGLKvphmgwNQLELKKESPLLKGIPDG-----AYVYFVh 146
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 219567478 136 SY---PPEGFKIIGKS--GESPVAAVENidKKIYGVQFHPEVEHTPfGKKMLSNFL 186
Cdd:PRK13141 147 SYyadPCDEEYVAATTdyGVEFPAAVGK--DNVFGAQFHPEKSGDV-GLKILKNFV 199
PRK09522 PRK09522
bifunctional anthranilate synthase glutamate amidotransferase component TrpG/anthranilate ...
15-186 2.09e-09

bifunctional anthranilate synthase glutamate amidotransferase component TrpG/anthranilate phosphoribosyltransferase TrpD;


Pssm-ID: 181927 [Multi-domain]  Cd Length: 531  Bit Score: 59.65  E-value: 2.09e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478  15 YNqlIARRVRENN----VYCEIVPYTYSVDKIKEKNPRGIIFTGGPNSVYDdnAPKISEDIFEI--GVPVLGICYGHQLI 88
Cdd:PRK09522  15 YN--LADQLRSNGhnvvIYRNHIPAQTLIERLATMSNPVLMLSPGPGVPSE--AGCMPELLTRLrgKLPIIGICLGHQAI 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478  89 CTTLGGKVESAQVREYGKTDVVLNNSSGLFSGIDKNESCWMSHTDFVSYPPEGFKiIGKSGESPVAAVENIDKKIYGVQF 168
Cdd:PRK09522  91 VEAYGGYVGQAGEILHGKASSIEHDGQAMFAGLTNPLPVARYHSLVGSNIPAGLT-INAHFNGMVMAVRHDADRVCGFQF 169
                        170
                 ....*....|....*...
gi 219567478 169 HPEVEHTPFGKKMLSNFL 186
Cdd:PRK09522 170 HPESILTTQGARLLEQTL 187
hisH PRK13143
imidazole glycerol phosphate synthase subunit HisH; Provisional
49-186 1.99e-08

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237289 [Multi-domain]  Cd Length: 200  Bit Score: 54.49  E-value: 1.99e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478  49 GIIFTG-GPNSVYDDNAPKISEDIFEI---GVPVLGICYGHQLICTT---------LG---GKV----ESAQVREYGKTD 108
Cdd:PRK13143  41 GIVLPGvGAFGAAMENLSPLRDVILEAarsGKPFLGICLGMQLLFESseegggvrgLGlfpGRVvrfpAGVKVPHMGWNT 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478 109 VVLNNSSGLFSGIDkNESCWMSHTdFVSYPPEGFKIIGKS--GESPVAAVENidKKIYGVQFHPEVEHTPfGKKMLSNFL 186
Cdd:PRK13143 121 VKVVKDCPLFEGID-GEYVYFVHS-YYAYPDDEDYVVATTdyGIEFPAAVCN--DNVFGTQFHPEKSGET-GLKILENFV 195
hisH PRK13146
imidazole glycerol phosphate synthase subunit HisH; Provisional
75-186 3.29e-08

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237290 [Multi-domain]  Cd Length: 209  Bit Score: 54.02  E-value: 3.29e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478  75 GVPVLGICYGHQLICTT------------LGGKVESAQVRE-------YGKTDVVLNNSSGLFSGIDKNEscwmsHTDFV 135
Cdd:PRK13146  77 GRPFLGICVGMQLLFERglehgdtpglglIPGEVVRFQPDGpalkvphMGWNTVDQTRDHPLFAGIPDGA-----RFYFV 151
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 219567478 136 -SY---PPEGFKIIGKS--GESPVAAVENidKKIYGVQFHPEVEHTpFGKKMLSNFL 186
Cdd:PRK13146 152 hSYyaqPANPADVVAWTdyGGPFTAAVAR--DNLFATQFHPEKSQD-AGLALLRNFL 205
hisH PRK13170
imidazole glycerol phosphate synthase subunit HisH; Provisional
77-186 3.79e-08

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 183877 [Multi-domain]  Cd Length: 196  Bit Score: 53.32  E-value: 3.79e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478  77 PVLGICYGHQLI---------CTTLG---GKVESAQVREY-----GKTDVVLNNSSGLFSGIDKNescwmSHTDFV-SY- 137
Cdd:PRK13170  72 PVLGICLGMQLLgerseesggVDCLGiidGPVKKMTDFGLplphmGWNQVTPQAGHPLFQGIEDG-----SYFYFVhSYa 146
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 219567478 138 -PPEGFKI-IGKSGESPVAAVENidKKIYGVQFHPEVEHTPfGKKMLSNFL 186
Cdd:PRK13170 147 mPVNEYTIaQCNYGEPFSAAIQK--DNFFGVQFHPERSGAA-GAQLLKNFL 194
HisH COG0118
Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH [Amino acid ...
69-171 1.08e-07

Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH [Amino acid transport and metabolism]; Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH is part of the Pathway/BioSystem: Histidine biosynthesis


Pssm-ID: 439888 [Multi-domain]  Cd Length: 196  Bit Score: 51.96  E-value: 1.08e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478  69 EDIFEIGVPVLGICYGHQLICT---------TLG---GKVESAQVREY-----GKTDVVLNNSSGLFSGIDKNEscwmsH 131
Cdd:COG0118   67 REAVAGGKPVLGICLGMQLLFErseengdteGLGlipGEVVRFPASDLkvphmGWNTVEIAKDHPLFAGIPDGE-----Y 141
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 219567478 132 TDFV-SY--PPEGFK-IIGKS--GESPVAAVENidKKIYGVQFHPE 171
Cdd:COG0118  142 FYFVhSYyvPPDDPEdVVATTdyGVPFTAAVER--GNVFGTQFHPE 185
tRNA_Me_trans pfam03054
tRNA methyl transferase HUP domain; This family represents the N-terminal HUP domain in tRNA ...
216-379 1.33e-07

tRNA methyl transferase HUP domain; This family represents the N-terminal HUP domain in tRNA(5-methylaminomethyl-2-thiouridine)-methyltransferase which is involved in the biosynthesis of the modified nucleoside 5-methylaminomethyl-2-thiouridine present in the wobble position of some tRNAs.


Pssm-ID: 460787 [Multi-domain]  Cd Length: 202  Bit Score: 51.87  E-value: 1.33e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478  216 KKVICAMSGGVDSSVAAMIVHKAvGKQLTCIFV---DHGLLRKDEG-----DQVEDIFK--KQFNMNFIRVNAEKRFlqk 285
Cdd:pfam03054   1 MKVVVAMSGGVDSSVAAYLLKEQ-GHNVIGVFMknwDEEQSLDEEGkccseEDLADAQRvcEQLGIPLYVVNFEKEY--- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478  286 lkdisdpekKRKIIgEEFIRVFEE-----------EAKKLGeiAFLvqgtiypDVVESGLGTSATIKSH-----HNVGGL 349
Cdd:pfam03054  77 ---------WEDVF-EPFLDEYKNgrtpnpdvlcnKEIKFG--ALL-------DYALENLGADYVATGHyarvsLNKDGG 137
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 219567478  350 PE-----DMD-----F----------KLIEPLRELFKDEVRAVGEELGIP 379
Cdd:pfam03054 138 SEllralDKNkdqsyFlstlsqeqleKLLFPLGELTKEEVRKIAKEAGLA 187
PRK13566 PRK13566
anthranilate synthase component I;
75-171 1.46e-07

anthranilate synthase component I;


Pssm-ID: 237429 [Multi-domain]  Cd Length: 720  Bit Score: 54.15  E-value: 1.46e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478  75 GVPVLGICYGHQLICTTLGGKVESAQVREYGKTDVVLNN-SSGLFSGIDKNESCWMSHTDFVSYP--PEGFKIIGKSGES 151
Cdd:PRK13566 598 NLPIFGVCLGLQAIVEAFGGELGQLAYPMHGKPSRIRVRgPGRLFSGLPEEFTVGRYHSLFADPEtlPDELLVTAETEDG 677
                         90       100
                 ....*....|....*....|
gi 219567478 152 PVAAVENIDKKIYGVQFHPE 171
Cdd:PRK13566 678 VIMAIEHKTLPVAAVQFHPE 697
PuuD COG2071
Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (putrescine degradation), contains ...
49-185 3.65e-07

Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (putrescine degradation), contains GATase1-like domain [Amino acid transport and metabolism];


Pssm-ID: 441674 [Multi-domain]  Cd Length: 231  Bit Score: 51.32  E-value: 3.65e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478  49 GIIFTGGPN---SVYD-DNAPKISE-----DIFEI---------GVPVLGICYGHQLICTTLGG--------KVESA--- 99
Cdd:COG2071   52 GLVLTGGADvdpALYGeEPHPELGPidperDAFELaliraalerGKPVLGICRGMQLLNVALGGtlyqdlpdQVPGAldh 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478 100 ---QVREYGKTDVVLNNSSGLFS---------------GIDKnescwmshtdfvsyPPEGFKIIGKSG----EspvaAVE 157
Cdd:COG2071  132 rqpAPRYAPRHTVEIEPGSRLARilgeeeirvnslhhqAVKR--------------LGPGLRVSARAPdgviE----AIE 193
                        170       180       190
                 ....*....|....*....|....*....|.
gi 219567478 158 NIDKK-IYGVQFHPE--VEHTPFGKKMLSNF 185
Cdd:COG2071  194 SPGAPfVLGVQWHPEwlAASDPLSRRLFEAF 224
mnmA PRK00143
tRNA-specific 2-thiouridylase MnmA; Reviewed
216-305 4.93e-07

tRNA-specific 2-thiouridylase MnmA; Reviewed


Pssm-ID: 234664 [Multi-domain]  Cd Length: 346  Bit Score: 51.61  E-value: 4.93e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478 216 KKVICAMSGGVDSSVAAMIVHKAvGKQLTCIFV---DHGLLRKDEGD-QVEDIFK-----KQFNMNFIRVNAEKRFlqkl 286
Cdd:PRK00143   1 KRVVVGMSGGVDSSVAAALLKEQ-GYEVIGVFMklwDDDDETGKGGCcAEEDIADarrvaDKLGIPHYVVDFEKEF---- 75
                         90
                 ....*....|....*....
gi 219567478 287 kdisdpekKRKIIgEEFIR 305
Cdd:PRK00143  76 --------WDRVI-DYFLD 85
MnmA COG0482
tRNA U34 2-thiouridine synthase MnmA/TrmU, contains the PP-loop ATPase domain [Translation, ...
216-282 7.82e-07

tRNA U34 2-thiouridine synthase MnmA/TrmU, contains the PP-loop ATPase domain [Translation, ribosomal structure and biogenesis]; tRNA U34 2-thiouridine synthase MnmA/TrmU, contains the PP-loop ATPase domain is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440250 [Multi-domain]  Cd Length: 353  Bit Score: 51.21  E-value: 7.82e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 219567478 216 KKVICAMSGGVDSSVAAMIVHKAvGKQLTCIFV---DHGLLRKDEGD-QVEDIFK-----KQFNMNFIRVNAEKRF 282
Cdd:COG0482    1 KRVVVGMSGGVDSSVAAALLKEQ-GYEVIGVTMklwDDDDASGSGGCcSLEDIEDarrvaDKLGIPHYVVDFEEEF 75
COG1606 COG1606
ATP-utilizing enzyme, PP-loop superfamily [General function prediction only];
202-407 2.36e-06

ATP-utilizing enzyme, PP-loop superfamily [General function prediction only];


Pssm-ID: 441214 [Multi-domain]  Cd Length: 265  Bit Score: 48.95  E-value: 2.36e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478 202 VDEKIKSIKEEVGD-KKVICAMSGGVDSSVAAMIVHKAVGKQLTCIFVDHGLLRKDEGDQVEDiFKKQFNMNFIRVNAEk 280
Cdd:COG1606    1 LEEKLERLKAILKElGSVLVAFSGGVDSTLLAKVAHDVLGDRVLAVTADSPSLPERELEEAKE-LAKEIGIRHEVIETD- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478 281 rflqklkDISDPE------------KKrkiigeEFIRVFEEEAKKLGeIAFLVQGTIYPD----------VVESGlgtsa 338
Cdd:COG1606   79 -------ELEDPEfvanppdrcyhcKK------ELFSKLKELAKELG-YAVVADGTNADDlgdyrpglraAKELG----- 139
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 219567478 339 tIKShhnvgglpedmdfkliePLRE--LFKDEVRAVGEELGIPhklVWRQPfPGPGLAIRVLGN--ITEEKLQ 407
Cdd:COG1606  140 -VRS-----------------PLAEagLTKAEIRELARELGLP---TWDKP-SSACLASRIPYGeeITPEKLR 190
hisH PRK13152
imidazole glycerol phosphate synthase subunit HisH; Provisional
67-186 3.12e-06

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 171876 [Multi-domain]  Cd Length: 201  Bit Score: 47.91  E-value: 3.12e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478  67 ISEDIFEIGVPVLGICYGHQLICT--TLGGKVES-----AQVREY-----------GKTDVVLNNSSGLFSGIDKNESCW 128
Cdd:PRK13152  65 LKEQVLVQKKPILGICLGMQLFLErgYEGGVCEGlgfieGEVVKFeedlnlkiphmGWNELEILKQSPLYQGIPEKSDFY 144
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 219567478 129 MSHTDFVSYPPEGFKIIGKSGESPVAAVENidKKIYGVQFHPEVEHTpFGKKMLSNFL 186
Cdd:PRK13152 145 FVHSFYVKCKDEFVSAKAQYGHKFVASLQK--DNIFATQFHPEKSQN-LGLKLLENFA 199
PRK07053 PRK07053
glutamine amidotransferase; Provisional
54-105 5.09e-06

glutamine amidotransferase; Provisional


Pssm-ID: 235919 [Multi-domain]  Cd Length: 234  Bit Score: 47.63  E-value: 5.09e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 219567478  54 GGPNSVYDDNA-PKISEDI------FEIGVPVLGICYGHQLICTTLGGKVESAQVREYG 105
Cdd:PRK07053  55 GGPIGVYDDELyPFLAPEIallrqrLAAGLPTLGICLGAQLIARALGARVYPGGQKEIG 113
NAD_synthase cd00553
NAD(+) synthase; NAD(+) synthase (EC 6.3.5.1), a homodimer, catalyzes the final step in the de ...
214-409 6.22e-06

NAD(+) synthase; NAD(+) synthase (EC 6.3.5.1), a homodimer, catalyzes the final step in the de novo nicotinamide adenine dinucleotide (NAD(+)) biosynthesis, an amide transfer from either ammonia or glutamine to nicotinic acid adenine dinucleotide (NaAD). The conversion of NaAD to NAD(+) occurs via a NAD-adenylate intermediate and requires ATP and Mg(2+). The intermediate is subsequently cleaved into NAD(+) and AMP. In many prokaryotes, such as Escherichia coli, NAD synthase consists of a single domain and is strictly ammonia dependent. In contrast, eukaryotes and other prokaryotes have an additional N-terminal amidohydrolase domain that prefer glutamine. Interestingly, NAD(+) synthases in these prokaryotes, can also utilize ammonia as an amide source.


Pssm-ID: 467484 [Multi-domain]  Cd Length: 248  Bit Score: 47.55  E-value: 6.22e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478 214 GDKKVICAMSGGVDSSVAAMIVHKAVGK-QLTCIFVDHGLLRKDEGDQVEDiFKKQFNMNFIRVN---AEKRFLQKLKDI 289
Cdd:cd00553   22 GAKGFVLGLSGGIDSAVVAALAVRALGAeNVLALIMPSRYSSKETRDDAKA-LAENLGIEYRTIDidpIVDAFLKALEHA 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478 290 SDPEKKRKIIG-----EEFIRVFeEEAKKLGeiaFLVQGTiyPDVVESGLGTsATIkshhnvGGlpeDM--DfklIEPLR 362
Cdd:cd00553  101 GGSEAEDLALGniqarLRMVLLY-ALANLLG---GLVLGT--GNKSELLLGY-FTK------YG---DGaaD---INPIG 161
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 219567478 363 ELFKDEVRAVGEELGIPHKlVWRQPfPGPGLAIrvlGNITEEKLQIT 409
Cdd:cd00553  162 DLYKTQVRELARYLGVPEE-IIEKP-PSAELWP---GQTDEDELGMP 203
PRK06490 PRK06490
glutamine amidotransferase; Provisional
50-174 8.02e-06

glutamine amidotransferase; Provisional


Pssm-ID: 180590 [Multi-domain]  Cd Length: 239  Bit Score: 47.26  E-value: 8.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478  50 IIFtGGPNSVYDDNaPKISEDIFEIGVPV------LGICYGHQLICTTLGGKVESaqvREYGKTDV------VLNNSSGL 117
Cdd:PRK06490  57 VIF-GGPMSANDPD-DFIRREIDWISVPLkenkpfLGICLGAQMLARHLGARVAP---HPDGRVEIgyyplrPTEAGRAL 131
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 219567478 118 FSgidknescWMSHTdfvsYP--------PEGFKIIGKSGESPVAAVENiDKKIYGVQFHPEVEH 174
Cdd:PRK06490 132 MH--------WPEMV----YHwhregfdlPAGAELLATGDDFPNQAFRY-GDNAWGLQFHPEVTR 183
PRK05637 PRK05637
anthranilate synthase component II; Provisional
30-183 8.70e-06

anthranilate synthase component II; Provisional


Pssm-ID: 180178 [Multi-domain]  Cd Length: 208  Bit Score: 46.76  E-value: 8.70e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478  30 CEIVPYTYSVDKIKEKNPRGIIFTGGPNsvYDDNAPKISEDIFE-IG-VPVLGICYGHQLICTTLGGKVESAQvREYGKT 107
Cdd:PRK05637  28 CTVFRNTVPVEEILAANPDLICLSPGPG--HPRDAGNMMALIDRtLGqIPLLGICLGFQALLEHHGGKVEPCG-PVHGTT 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478 108 D-VVLNNS---SGLFSGID-----KNESCWMSHTDFVSY-------PPEGFKIIG--KSGESPVA-AVENIDKKIYGVQF 168
Cdd:PRK05637 105 DnMILTDAgvqSPVFAGLAtdvepDHPEIPGRKVPIARYhslgcvvAPDGMESLGtcSSEIGPVImAAETTDGKAIGLQF 184
                        170
                 ....*....|....*
gi 219567478 169 HPEVEHTPFGKKMLS 183
Cdd:PRK05637 185 HPESVLSPTGPIILS 199
PRK07567 PRK07567
glutamine amidotransferase; Provisional
49-171 1.33e-05

glutamine amidotransferase; Provisional


Pssm-ID: 181035 [Multi-domain]  Cd Length: 242  Bit Score: 46.47  E-value: 1.33e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478  49 GIIFTGGPNSVYDDNAPK-------------ISEDIFEIGVPVLGICYGHQLICTTLGGKVESAQVREYGKTDVVLNNSS 115
Cdd:PRK07567  54 GVIVGGSPFNVSDPAESKspwqrrveaelsgLLDEVVARDFPFLGACYGVGTLGHHQGGVVDRTYGEPVGAVTVSLTDAG 133
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 219567478 116 G---LFSGIDKNESCWMSHTDFVSYPPEGFKIIGKSGESPVAAVEnIDKKIYGVQFHPE 171
Cdd:PRK07567 134 RadpLLAGLPDTFTAFVGHKEAVSALPPGAVLLATSPTCPVQMFR-VGENVYATQFHPE 191
MnmA_TRMU-like cd01998
MnmA/TRMU family 2-thiouridylases and similar proteins; This family is composed of bacterial ...
217-282 1.49e-05

MnmA/TRMU family 2-thiouridylases and similar proteins; This family is composed of bacterial tRNA-specific 2-thiouridylase MnmA (EC 2.8.1.13) and mitochondrial tRNA-specific 2-thiouridylase 1 (TRMU or MTU1, EC 2.8.1.14). MnmA catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34. TRMU/MTU1 catalyzes the 2-thiolation of uridine at the wobble position (U34) of mitochondrial tRNA(Lys), tRNA(Glu) and tRNA(Gln); this is required for the formation of 5-taurinomethyl-2-thiouridine (tm5s2U) of mitochondrial tRNA(Lys), tRNA(Glu), and tRNA(Gln) at the wobble position. This family belongs to the adenine nucleotide alpha hydrolase (AANH) superfamily that also includes other N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to the adenosine group.


Pssm-ID: 467502 [Multi-domain]  Cd Length: 349  Bit Score: 47.12  E-value: 1.49e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 219567478 217 KVICAMSGGVDSSVAAMIVHKAvGKQLTCIFV---DHGLLRKDE---GDQVEDIFK--KQFNMNFIRVNAEKRF 282
Cdd:cd01998    1 KVAVAMSGGVDSSVAAALLKEQ-GYDVIGVFMknwDDEDNEKGGccsEEDIEDARRvaDQLGIPLYVVDFSEEY 73
NAD_synthase pfam02540
NAD synthase; NAD synthase (EC:6.3.5.1) is involved in the de novo synthesis of NAD and is ...
206-432 8.84e-05

NAD synthase; NAD synthase (EC:6.3.5.1) is involved in the de novo synthesis of NAD and is induced by stress factors such as heat shock and glucose limitation.


Pssm-ID: 396888 [Multi-domain]  Cd Length: 241  Bit Score: 43.91  E-value: 8.84e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478  206 IKSIKEEVGDKKVICAMSGGVDSSVAAMIVHKAVGKQLTcifvdHGLL----RKDEGDqVEDI--FKKQFNMNFIRVNAE 279
Cdd:pfam02540   9 LRDYVQKAGFKGVVLGLSGGIDSSLVAYLAVKALGKENV-----LALImpssQSSEED-VQDAlaLAENLGIEYKTIDIK 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478  280 ---KRFLQKLKDISDPEKKRKIIGEEFIRVFEEEAKKLGeiaFLVQGTIYPDVVESGLGTSatikshhnVGGLPEDmdfk 356
Cdd:pfam02540  83 pivRAFSQLFQDASEDFAKGNLKARIRMAILYYIANKFN---YLVLGTGNKSELAVGYFTK--------YGDGACD---- 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478  357 lIEPLRELFKDEVRAVGEELGIPHKLVWRQP----FPgpglairvlGNITEEKLQITRDA-DAIF--------REEIAKA 423
Cdd:pfam02540 148 -IAPIGDLYKTQVYELARYLNVPERIIKKPPsadlWP---------GQTDEEELGIPYDElDDILklvekklsPEEIIGK 217

                  ....*....
gi 219567478  424 NLDETIWQY 432
Cdd:pfam02540 218 GLPAEVVRR 226
AANH-like cd01986
adenine nucleotide alpha hydrolase (AANH)-like proteins; This group of adenine nucleotide ...
218-283 1.02e-04

adenine nucleotide alpha hydrolase (AANH)-like proteins; This group of adenine nucleotide alpha hydrolase (AANH)-like proteins includes N-type ATP PPases and ATP sulfurylases. The domain forms an alpha/beta/alpha fold which binds to adenosine nucleotide.


Pssm-ID: 467490 [Multi-domain]  Cd Length: 74  Bit Score: 40.51  E-value: 1.02e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 219567478 218 VICAMSGGVDSSVAAMIVHKAVGK-QLTCIFVDHGLLRKDEGDQVEDIFKKQFnMNFIRVNAEKRFL 283
Cdd:cd01986    1 VVVGYSGGKDSSVALHLASRLGRKaEVAVVHIDHGIGFKEEAESVASIARRSI-LKKLAEKGARAIA 66
TilS_N cd01992
N-terminal domain of tRNA(Ile)-lysidine synthase and similar proteins; tRNA(Ile)-lysidine ...
217-379 1.16e-04

N-terminal domain of tRNA(Ile)-lysidine synthase and similar proteins; tRNA(Ile)-lysidine synthase (EC 6.3.4.19), also called tRNA(Ile)-2-lysyl-cytidine synthase or tRNA(Ile)-lysidine synthetase, catalyzes the ligation of lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine. This subfamily belongs to the adenine nucleotide alpha hydrolase superfamily that also includes N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to adenosine group. This domain has a strongly conserved motif SGGXD at the N-terminus.


Pssm-ID: 467496 [Multi-domain]  Cd Length: 185  Bit Score: 42.97  E-value: 1.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478 217 KVICAMSGGVDSSV---AAMIVHKAVGKQLTCIFVDHGlLR---KDEGDQVEDIFkKQFNMNFIRVNAEKRFlqklKDIS 290
Cdd:cd01992    1 KILVAVSGGPDSMAllhLLKELRPKLGLKLVAVHVDHG-LReesAEEAQFVAKLC-KKLGIPLHILTVTEAP----KSGG 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478 291 DPEKK-RKiigeefIR--VFEEEAKKLGeIAFLV----QGtiypDVVE---------SGLGTSATIKSHHNVGGLPedmd 354
Cdd:cd01992   75 NLEAAaRE------ARyaFLERAAKEHG-IDVLLtahhLD----DQAEtvlmrllrgSGLSGLAGMAARSKAGGIR---- 139
                        170       180
                 ....*....|....*....|....*
gi 219567478 355 fkLIEPLRELFKDEVRAVGEELGIP 379
Cdd:cd01992  140 --LIRPLLGISKAELLAYCRENGLP 162
trmU TIGR00420
tRNA (5-methylaminomethyl-2-thiouridylate)-methyltransferase; tRNA ...
216-247 1.76e-04

tRNA (5-methylaminomethyl-2-thiouridylate)-methyltransferase; tRNA (5-methylaminomethyl-2-thiouridylate)-methyltransferase (trmU, asuE, or mnmA) is involved in the biosynthesis of the modified nucleoside 5-methylaminomethyl-2-thiouridine (mnm5s2U34) present in the wobble position of some tRNAs. This enzyme appears not to occur in the Archaea. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 273069 [Multi-domain]  Cd Length: 352  Bit Score: 43.91  E-value: 1.76e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 219567478  216 KKVICAMSGGVDSSVAAMIVHKAvGKQLTCIF 247
Cdd:TIGR00420   1 KKVIVGLSGGVDSSVSAYLLKQQ-GYEVVGVF 31
PRK13794 PRK13794
hypothetical protein; Provisional
201-287 1.22e-03

hypothetical protein; Provisional


Pssm-ID: 237509 [Multi-domain]  Cd Length: 479  Bit Score: 41.19  E-value: 1.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478 201 FVDEKIKSIKeevgdKKVICAMSGGVDSSVAAMIVHKAVGKQLTCIFVDHGLLRKDEGDQVEDIfKKQFNMNFIRVNAEK 280
Cdd:PRK13794 238 FIRNTAEKIN-----KPVTVAYSGGKDSLATLLLALKALGINFPVLFNDTGLEFPETLENVEDV-EKHYGLEIIRTKSEE 311

                 ....*..
gi 219567478 281 rFLQKLK 287
Cdd:PRK13794 312 -FWEKLE 317
NadE COG0171
NH3-dependent NAD+ synthetase [Coenzyme transport and metabolism]; NH3-dependent NAD+ ...
209-242 1.26e-03

NH3-dependent NAD+ synthetase [Coenzyme transport and metabolism]; NH3-dependent NAD+ synthetase is part of the Pathway/BioSystem: NAD biosynthesis


Pssm-ID: 439941 [Multi-domain]  Cd Length: 542  Bit Score: 41.37  E-value: 1.26e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 219567478 209 IKEEV---GDKKVICAMSGGVDSSVAAMIVHKAVGKQ 242
Cdd:COG0171  277 LRDYVrknGFKGVVLGLSGGIDSALVAALAVDALGPE 313
hisH PRK14004
imidazole glycerol phosphate synthase subunit HisH; Provisional
35-186 1.40e-03

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 172505 [Multi-domain]  Cd Length: 210  Bit Score: 40.27  E-value: 1.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478  35 YTYSVDKIKEKNPRGIIFTGGPN---SVYDDNAPKISEDI---FEIGVPVLGICYGHQLIC-----TTLGGKVES----- 98
Cdd:PRK14004  26 FVFTSDPETIENSKALILPGDGHfdkAMENLNSTGLRSTIdkhVESGKPLFGICIGFQILFesseeTNQGTKKEQieglg 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478  99 ---AQVREYGKTD------------VVLNNSSGLFSGIDKNESCWMSHtdfvSYPP---EGFKIIGKS---GESPVAAVE 157
Cdd:PRK14004 106 yikGKIKKFEGKDfkvphigwnrlqIRRKDKSKLLKGIGDQSFFYFIH----SYRPtgaEGNAITGLCdyyQEKFPAVVE 181
                        170       180
                 ....*....|....*....|....*....
gi 219567478 158 NidKKIYGVQFHPEVEHTpFGKKMLSNFL 186
Cdd:PRK14004 182 K--ENIFGTQFHPEKSHT-HGLKLLENFI 207
TilS COG0037
tRNA(Ile)-lysidine synthase TilS/MesJ [Translation, ribosomal structure and biogenesis]; tRNA ...
215-268 2.10e-03

tRNA(Ile)-lysidine synthase TilS/MesJ [Translation, ribosomal structure and biogenesis]; tRNA(Ile)-lysidine synthase TilS/MesJ is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 439807 [Multi-domain]  Cd Length: 235  Bit Score: 39.82  E-value: 2.10e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 219567478 215 DKKVICAMSGGVDSSV---AAMIVHKAVGKQLTCIFVDHGLlrKDEGDQVEDIFKKQ 268
Cdd:COG0037   15 GDRILVAVSGGKDSLAllhLLAKLRRRLGFELVAVHVDHGL--REESDEDAEFVAEL 69
PRK13980 PRK13980
NAD synthetase; Provisional
198-390 4.32e-03

NAD synthetase; Provisional


Pssm-ID: 184435 [Multi-domain]  Cd Length: 265  Bit Score: 39.04  E-value: 4.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478 198 MSSFVDEKIksikEEVGDKKVICAMSGGVDSSVAAMIVHKAVGKQLTcifvdHGLL---RKDEGDQVEDIFK--KQFNMN 272
Cdd:PRK13980  17 IVDFIREEV----EKAGAKGVVLGLSGGIDSAVVAYLAVKALGKENV-----LALLmpsSVSPPEDLEDAELvaEDLGIE 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478 273 FIRVnaekrflqklkDISDpekkrkiIGEEFIRVFEEEAKK-LGEIAFLVQGTIYPDVVESG----LGTSAtiKSHHNVG 347
Cdd:PRK13980  88 YKVI-----------EITP-------IVDAFFSAIPDADRLrVGNIMARTRMVLLYDYANREnrlvLGTGN--KSELLLG 147
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 219567478 348 -----GlpeDM--DFkliEPLRELFKDEVRAVGEELGIPHKLVWRQPFPG 390
Cdd:PRK13980 148 yftkyG---DGavDL---NPIGDLYKTQVRELARHLGVPEDIIEKPPSAD 191
lysidine_TilS_N TIGR02432
tRNA(Ile)-lysidine synthetase, N-terminal domain; The only examples in which the wobble ...
217-315 6.27e-03

tRNA(Ile)-lysidine synthetase, N-terminal domain; The only examples in which the wobble position of a tRNA must discriminate between G and A of mRNA are AUA (Ile) vs. AUG (Met) and UGA (stop) vs. UGG (Trp). In all bacteria, the wobble position of the tRNA(Ile) recognizing AUA is lysidine, a lysine derivative of cytidine. This family describes a protein domain found, apparently, in all bacteria in a single copy. Eukaryotic sequences appear to be organellar. The domain archictecture of this protein family is variable; some, including characterized proteins of E. coli and B. subtilis known to be tRNA(Ile)-lysidine synthetase, include a conserved 50-residue domain that many other members lack. This protein belongs to the ATP-binding PP-loop family ( pfam01171). It appears in the literature and protein databases as TilS, YacA, and putative cell cycle protein MesJ (a misnomer). [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 274129 [Multi-domain]  Cd Length: 189  Bit Score: 38.00  E-value: 6.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219567478  217 KVICAMSGGVDSSV---AAMIVHKAVGKQLTCIFVDHGlLR---KDEGDQVEDiFKKQFNMNFIRVNAEKRFLQKLKDIS 290
Cdd:TIGR02432   1 RILVAVSGGVDSMAllhLLLKLQPKIKIKLIAAHVDHG-LRpesDEEAEFVQQ-FCRKLNIPLEIKKVDVKALAKGKKKN 78
                          90       100
                  ....*....|....*....|....*..
gi 219567478  291 DPEKKRKiigeefIR--VFEEEAKKLG 315
Cdd:TIGR02432  79 LEEAARE------ARydFFEEIAKKHG 99
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH
HHS Vulnerability Disclosure