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Conserved domains on  [gi|406936192|gb|EKD69980|]
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hypothetical protein ACD_46C00685G0010 [uncultured bacterium]

Protein Classification

2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase( domain architecture ID 11485562)

2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase catalyzes the formation of CoA and N-succinyl-2-amino-6-keto-L-pimelate from succinyl-CoA and tetrahydrodipicolinate

EC:  2.3.1.117
Gene Ontology:  GO:0016779|GO:0009089|GO:0008666
SCOP:  4002837

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
dapD PRK11830
2,3,4,5-tetrahydropyridine-2,6-carboxylate N-succinyltransferase; Provisional
1-271 4.20e-180

2,3,4,5-tetrahydropyridine-2,6-carboxylate N-succinyltransferase; Provisional


:

Pssm-ID: 236996 [Multi-domain]  Cd Length: 272  Bit Score: 496.25  E-value: 4.20e-180
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406936192   1 MQQTQAIIEGAFLERNQLSPQNVSAEIKQSVDSVIDLLDQGKLRVAEKINQ-EWITYEWVKKAVLLYFRINDNQTFPAGF 79
Cdd:PRK11830   1 MSQLQKIIEEAWERRAELTPATADTEVREAVEEVIDLLDSGELRVAEKIDDgEWVVNQWVKKAILLSFRLNDNQVIEGGD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406936192  80 TQFYDKVPLKFAHYSSDQFAADNVRIVPHALARKGAYIAPNTILMPSYINLGAYIDSGTLIDTWATVGSCAQIGKNVHLS 159
Cdd:PRK11830  81 FRFYDKVPLKFAGWDEARFKEAGVRVVPGAVVRRGAYIAPNVVLMPSYVNIGAYVDEGTMVDTWATVGSCAQIGKNVHLS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406936192 160 GGAGIGGVLEPLQANPTIIEDNCFIGARSEVVEGVIVEEGSVISMGVYLGQSTRIYDRATGSISYGRIPAGSVVVAGNLP 239
Cdd:PRK11830 161 GGVGIGGVLEPLQANPVIIEDNCFIGARSEVVEGVIVEEGSVLGMGVFLGQSTKIYDRETGEVHYGRVPAGSVVVPGSLP 240
                        250       260       270
                 ....*....|....*....|....*....|..
gi 406936192 240 SEDGKYSLYCAVIVKQVDAKTRAKLTLNELLR 271
Cdd:PRK11830 241 SKDGGYSLYCAVIVKKVDAKTRSKTSINELLR 272
 
Name Accession Description Interval E-value
dapD PRK11830
2,3,4,5-tetrahydropyridine-2,6-carboxylate N-succinyltransferase; Provisional
1-271 4.20e-180

2,3,4,5-tetrahydropyridine-2,6-carboxylate N-succinyltransferase; Provisional


Pssm-ID: 236996 [Multi-domain]  Cd Length: 272  Bit Score: 496.25  E-value: 4.20e-180
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406936192   1 MQQTQAIIEGAFLERNQLSPQNVSAEIKQSVDSVIDLLDQGKLRVAEKINQ-EWITYEWVKKAVLLYFRINDNQTFPAGF 79
Cdd:PRK11830   1 MSQLQKIIEEAWERRAELTPATADTEVREAVEEVIDLLDSGELRVAEKIDDgEWVVNQWVKKAILLSFRLNDNQVIEGGD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406936192  80 TQFYDKVPLKFAHYSSDQFAADNVRIVPHALARKGAYIAPNTILMPSYINLGAYIDSGTLIDTWATVGSCAQIGKNVHLS 159
Cdd:PRK11830  81 FRFYDKVPLKFAGWDEARFKEAGVRVVPGAVVRRGAYIAPNVVLMPSYVNIGAYVDEGTMVDTWATVGSCAQIGKNVHLS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406936192 160 GGAGIGGVLEPLQANPTIIEDNCFIGARSEVVEGVIVEEGSVISMGVYLGQSTRIYDRATGSISYGRIPAGSVVVAGNLP 239
Cdd:PRK11830 161 GGVGIGGVLEPLQANPVIIEDNCFIGARSEVVEGVIVEEGSVLGMGVFLGQSTKIYDRETGEVHYGRVPAGSVVVPGSLP 240
                        250       260       270
                 ....*....|....*....|....*....|..
gi 406936192 240 SEDGKYSLYCAVIVKQVDAKTRAKLTLNELLR 271
Cdd:PRK11830 241 SKDGGYSLYCAVIVKKVDAKTRSKTSINELLR 272
DapD COG2171
Tetrahydrodipicolinate N-succinyltransferase [Amino acid transport and metabolism]; ...
1-273 5.42e-164

Tetrahydrodipicolinate N-succinyltransferase [Amino acid transport and metabolism]; Tetrahydrodipicolinate N-succinyltransferase is part of the Pathway/BioSystem: Lysine biosynthesis


Pssm-ID: 441774 [Multi-domain]  Cd Length: 268  Bit Score: 455.35  E-value: 5.42e-164
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406936192   1 MQQTQAIIEGAFLERNQLSPqNVSAEIKQSVDSVIDLLDQGKLRVAEK-INQEWITYEWVKKAVLLYFRINDNQTFPAGF 79
Cdd:COG2171    1 MADLGTVIDAAWENRAELTP-LADREVREAVEEVIAALDAGPLRVAEPnLDGEWVVNEWVKKAILLSFRLEDNRVLEGGG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406936192  80 TQFYDKVPLKFahyssDQFAADNVRIVPHALARKGAYIAPNTILMPSYINLGAYIDSGTLIDTWATVGSCAQIGKNVHLS 159
Cdd:COG2171   80 VTYHDKVPLKF-----DYFKPAGVRIVPGARVRLGAYLAPGVVLMPSFVNIGAYVDEGTMVDTWATVGSCAQIGKNVHLS 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406936192 160 GGAGIGGVLEPLQANPTIIEDNCFIGARSEVVEGVIVEEGSVISMGVYLGQSTRIYDRATGSISYGRIPAGSVVVAGNLP 239
Cdd:COG2171  155 GGAGIGGVLEPLQAAPVIIEDNCFIGARSGVVEGVIVGEGAVLGAGVYLTASTKIYDRVTGEVYYGRVPAGSVVVPGSLP 234
                        250       260       270
                 ....*....|....*....|....*....|....
gi 406936192 240 SEDGKYSLYCAVIVKQVDAKTRAKLTLNELLRNI 273
Cdd:COG2171  235 GKDGDYGLYCAVIVKRRDEKTRSKTSLNELLRDN 268
dapD TIGR00965
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase; This enzyme is part of the ...
3-271 3.97e-143

2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase; This enzyme is part of the diaminopimelate pathway of lysine biosynthesis. Alternate name: tetrahydrodipicolinate N-succinyltransferase. The closely related TabB protein of Pseudomonas syringae (pv. tabaci), SP|P31852|TABB_PSESZ, appears to act in the biosynthesis of tabtoxin rather than lysine. The trusted cutoff is set high enough to exclude this gene. Sequences below trusted also include a version of this enzyme which apparently utilize acetate rather than succinate (EC: 2.3.1.89). [Amino acid biosynthesis, Aspartate family]


Pssm-ID: 130038 [Multi-domain]  Cd Length: 269  Bit Score: 402.74  E-value: 3.97e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406936192    3 QTQAIIEGAFLERNQLSPQNVSAEIKQSVDSVIDLLDQGKLRVAEKINQEWITYEWVKKAVLLYFRINDNQTFPAGFTQF 82
Cdd:TIGR00965   1 QLQNIIETAFERRAEITPANADTVTKEAVNEVIALLDSGALRVAEKIDGQWKVNEWLKKAVLLSFRINDNQVINGAENRY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406936192   83 YDKVPLKFAHYSSDQFAADNVRIVPHALARKGAYIAPNTILMPSYINLGAYIDSGTLIDTWATVGSCAQIGKNVHLSGGA 162
Cdd:TIGR00965  81 FDKVPMKFADYDEARFKKAGFRVVPGAAVRQGAFIAKNVVLMPSYVNIGAYVDEGTMVDTWATVGSCAQIGKNVHLSGGV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406936192  163 GIGGVLEPLQANPTIIEDNCFIGARSEVVEGVIVEEGSVISMGVYLGQSTRIYDRATGSISYGRIPAGSVVVAGNLPSED 242
Cdd:TIGR00965 161 GIGGVLEPLQANPTIIEDNCFIGARSEIVEGVIVEEGSVISMGVFIGQSTKIYDRETGEIHYGRVPAGSVVVSGNLPSKD 240
                         250       260
                  ....*....|....*....|....*....
gi 406936192  243 GKYSLYCAVIVKQVDAKTRAKLTLNELLR 271
Cdd:TIGR00965 241 GKYSLYCAVIVKKVDAKTRGKVSINELLR 269
LbH_THP_succinylT cd03350
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP ...
102-239 1.09e-70

2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP succinyltransferase): THDP N-succinyltransferase catalyzes the conversion of tetrahydrodipicolinate and succinyl-CoA to N-succinyltetrahydrodipicolinate and CoA. It is the committed step in the succinylase pathway by which bacteria synthesize L-lysine and meso-diaminopimelate, a component of peptidoglycan. The enzyme is homotrimeric and each subunit contains an N-terminal region with alpha helices and hairpin loops, as well as a C-terminal region with a left-handed parallel alpha-helix (LbH) structural motif encoded by hexapeptide repeat motifs.


Pssm-ID: 100041 [Multi-domain]  Cd Length: 139  Bit Score: 214.17  E-value: 1.09e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406936192 102 NVRIVPHALARKGAYIAPNTILM-PSYINLGAYIDSGTLIDTWATVGSCAQIGKNVHLSGGAGIGGVLEPLQANPTIIED 180
Cdd:cd03350    1 GRRVPPGAIIRDGAFIGPGAVLMmPSYVNIGAYVDEGTMVDSWATVGSCAQIGKNVHLSAGAVIGGVLEPLQATPVIIED 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 406936192 181 NCFIGARSEVVEGVIVEEGSVISMGVYLGQSTRIYDRATGSISYGRIPAGSVVVAGNLP 239
Cdd:cd03350   81 DVFIGANCEVVEGVIVGKGAVLAAGVVLTQSTPIYDRETGEIYYGRVPPGSVVVAGSLP 139
THDPS_N_2 pfam14805
Tetrahydrodipicolinate N-succinyltransferase N-terminal; This is the N-terminal domain of 2,3, ...
5-69 1.36e-31

Tetrahydrodipicolinate N-succinyltransferase N-terminal; This is the N-terminal domain of 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase.


Pssm-ID: 464325 [Multi-domain]  Cd Length: 67  Bit Score: 111.41  E-value: 1.36e-31
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 406936192    5 QAIIEGAFLERNQLSPQNVSAEIKQSVDSVIDLLDQGKLRVAEKINQEWITYEWVKKAVLLYFRI 69
Cdd:pfam14805   3 QKIIEAAWENRALLTPATADAEVRDAVEEVIDLLDAGELRVAEKIDGGWVVNEWVKKAVLLYFRL 67
 
Name Accession Description Interval E-value
dapD PRK11830
2,3,4,5-tetrahydropyridine-2,6-carboxylate N-succinyltransferase; Provisional
1-271 4.20e-180

2,3,4,5-tetrahydropyridine-2,6-carboxylate N-succinyltransferase; Provisional


Pssm-ID: 236996 [Multi-domain]  Cd Length: 272  Bit Score: 496.25  E-value: 4.20e-180
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406936192   1 MQQTQAIIEGAFLERNQLSPQNVSAEIKQSVDSVIDLLDQGKLRVAEKINQ-EWITYEWVKKAVLLYFRINDNQTFPAGF 79
Cdd:PRK11830   1 MSQLQKIIEEAWERRAELTPATADTEVREAVEEVIDLLDSGELRVAEKIDDgEWVVNQWVKKAILLSFRLNDNQVIEGGD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406936192  80 TQFYDKVPLKFAHYSSDQFAADNVRIVPHALARKGAYIAPNTILMPSYINLGAYIDSGTLIDTWATVGSCAQIGKNVHLS 159
Cdd:PRK11830  81 FRFYDKVPLKFAGWDEARFKEAGVRVVPGAVVRRGAYIAPNVVLMPSYVNIGAYVDEGTMVDTWATVGSCAQIGKNVHLS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406936192 160 GGAGIGGVLEPLQANPTIIEDNCFIGARSEVVEGVIVEEGSVISMGVYLGQSTRIYDRATGSISYGRIPAGSVVVAGNLP 239
Cdd:PRK11830 161 GGVGIGGVLEPLQANPVIIEDNCFIGARSEVVEGVIVEEGSVLGMGVFLGQSTKIYDRETGEVHYGRVPAGSVVVPGSLP 240
                        250       260       270
                 ....*....|....*....|....*....|..
gi 406936192 240 SEDGKYSLYCAVIVKQVDAKTRAKLTLNELLR 271
Cdd:PRK11830 241 SKDGGYSLYCAVIVKKVDAKTRSKTSINELLR 272
DapD COG2171
Tetrahydrodipicolinate N-succinyltransferase [Amino acid transport and metabolism]; ...
1-273 5.42e-164

Tetrahydrodipicolinate N-succinyltransferase [Amino acid transport and metabolism]; Tetrahydrodipicolinate N-succinyltransferase is part of the Pathway/BioSystem: Lysine biosynthesis


Pssm-ID: 441774 [Multi-domain]  Cd Length: 268  Bit Score: 455.35  E-value: 5.42e-164
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406936192   1 MQQTQAIIEGAFLERNQLSPqNVSAEIKQSVDSVIDLLDQGKLRVAEK-INQEWITYEWVKKAVLLYFRINDNQTFPAGF 79
Cdd:COG2171    1 MADLGTVIDAAWENRAELTP-LADREVREAVEEVIAALDAGPLRVAEPnLDGEWVVNEWVKKAILLSFRLEDNRVLEGGG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406936192  80 TQFYDKVPLKFahyssDQFAADNVRIVPHALARKGAYIAPNTILMPSYINLGAYIDSGTLIDTWATVGSCAQIGKNVHLS 159
Cdd:COG2171   80 VTYHDKVPLKF-----DYFKPAGVRIVPGARVRLGAYLAPGVVLMPSFVNIGAYVDEGTMVDTWATVGSCAQIGKNVHLS 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406936192 160 GGAGIGGVLEPLQANPTIIEDNCFIGARSEVVEGVIVEEGSVISMGVYLGQSTRIYDRATGSISYGRIPAGSVVVAGNLP 239
Cdd:COG2171  155 GGAGIGGVLEPLQAAPVIIEDNCFIGARSGVVEGVIVGEGAVLGAGVYLTASTKIYDRVTGEVYYGRVPAGSVVVPGSLP 234
                        250       260       270
                 ....*....|....*....|....*....|....
gi 406936192 240 SEDGKYSLYCAVIVKQVDAKTRAKLTLNELLRNI 273
Cdd:COG2171  235 GKDGDYGLYCAVIVKRRDEKTRSKTSLNELLRDN 268
dapD TIGR00965
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase; This enzyme is part of the ...
3-271 3.97e-143

2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase; This enzyme is part of the diaminopimelate pathway of lysine biosynthesis. Alternate name: tetrahydrodipicolinate N-succinyltransferase. The closely related TabB protein of Pseudomonas syringae (pv. tabaci), SP|P31852|TABB_PSESZ, appears to act in the biosynthesis of tabtoxin rather than lysine. The trusted cutoff is set high enough to exclude this gene. Sequences below trusted also include a version of this enzyme which apparently utilize acetate rather than succinate (EC: 2.3.1.89). [Amino acid biosynthesis, Aspartate family]


Pssm-ID: 130038 [Multi-domain]  Cd Length: 269  Bit Score: 402.74  E-value: 3.97e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406936192    3 QTQAIIEGAFLERNQLSPQNVSAEIKQSVDSVIDLLDQGKLRVAEKINQEWITYEWVKKAVLLYFRINDNQTFPAGFTQF 82
Cdd:TIGR00965   1 QLQNIIETAFERRAEITPANADTVTKEAVNEVIALLDSGALRVAEKIDGQWKVNEWLKKAVLLSFRINDNQVINGAENRY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406936192   83 YDKVPLKFAHYSSDQFAADNVRIVPHALARKGAYIAPNTILMPSYINLGAYIDSGTLIDTWATVGSCAQIGKNVHLSGGA 162
Cdd:TIGR00965  81 FDKVPMKFADYDEARFKKAGFRVVPGAAVRQGAFIAKNVVLMPSYVNIGAYVDEGTMVDTWATVGSCAQIGKNVHLSGGV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406936192  163 GIGGVLEPLQANPTIIEDNCFIGARSEVVEGVIVEEGSVISMGVYLGQSTRIYDRATGSISYGRIPAGSVVVAGNLPSED 242
Cdd:TIGR00965 161 GIGGVLEPLQANPTIIEDNCFIGARSEIVEGVIVEEGSVISMGVFIGQSTKIYDRETGEIHYGRVPAGSVVVSGNLPSKD 240
                         250       260
                  ....*....|....*....|....*....
gi 406936192  243 GKYSLYCAVIVKQVDAKTRAKLTLNELLR 271
Cdd:TIGR00965 241 GKYSLYCAVIVKKVDAKTRGKVSINELLR 269
LbH_THP_succinylT cd03350
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP ...
102-239 1.09e-70

2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP succinyltransferase): THDP N-succinyltransferase catalyzes the conversion of tetrahydrodipicolinate and succinyl-CoA to N-succinyltetrahydrodipicolinate and CoA. It is the committed step in the succinylase pathway by which bacteria synthesize L-lysine and meso-diaminopimelate, a component of peptidoglycan. The enzyme is homotrimeric and each subunit contains an N-terminal region with alpha helices and hairpin loops, as well as a C-terminal region with a left-handed parallel alpha-helix (LbH) structural motif encoded by hexapeptide repeat motifs.


Pssm-ID: 100041 [Multi-domain]  Cd Length: 139  Bit Score: 214.17  E-value: 1.09e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406936192 102 NVRIVPHALARKGAYIAPNTILM-PSYINLGAYIDSGTLIDTWATVGSCAQIGKNVHLSGGAGIGGVLEPLQANPTIIED 180
Cdd:cd03350    1 GRRVPPGAIIRDGAFIGPGAVLMmPSYVNIGAYVDEGTMVDSWATVGSCAQIGKNVHLSAGAVIGGVLEPLQATPVIIED 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 406936192 181 NCFIGARSEVVEGVIVEEGSVISMGVYLGQSTRIYDRATGSISYGRIPAGSVVVAGNLP 239
Cdd:cd03350   81 DVFIGANCEVVEGVIVGKGAVLAAGVVLTQSTPIYDRETGEIYYGRVPPGSVVVAGSLP 139
THDPS_N_2 pfam14805
Tetrahydrodipicolinate N-succinyltransferase N-terminal; This is the N-terminal domain of 2,3, ...
5-69 1.36e-31

Tetrahydrodipicolinate N-succinyltransferase N-terminal; This is the N-terminal domain of 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase.


Pssm-ID: 464325 [Multi-domain]  Cd Length: 67  Bit Score: 111.41  E-value: 1.36e-31
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 406936192    5 QAIIEGAFLERNQLSPQNVSAEIKQSVDSVIDLLDQGKLRVAEKINQEWITYEWVKKAVLLYFRI 69
Cdd:pfam14805   3 QKIIEAAWENRALLTPATADAEVRDAVEEVIDLLDAGELRVAEKIDGGWVVNEWVKKAVLLYFRL 67
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
132-209 7.03e-13

Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity, however, some subfamilies in this hierarchy also show activities related to ion transport or translation initiation. Many are trimeric in their active forms.


Pssm-ID: 100038 [Multi-domain]  Cd Length: 78  Bit Score: 62.65  E-value: 7.03e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 406936192 132 AYIDSGTLIDTWATVGSCAQIGKNVHLSGGAGIGGVLEPLQANPTIIEDNCFIGARSEVVEGVIVEEGSVISMGVYLG 209
Cdd:cd00208    1 VFIGEGVKIHPKAVIRGPVVIGDNVNIGPGAVIGAATGPNEKNPTIIGDNVEIGANAVIHGGVKIGDNAVIGAGAVVT 78
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
113-237 4.47e-10

Acetyltransferase, isoleucine patch superfamily [General function prediction only];


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 56.42  E-value: 4.47e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406936192 113 KGAYIAPNTILMPSYINLGA--YIDSGTLIDTWA--TVGSCAQIGKNVHLSGG--AGIGGVLEPLQANPTIIEDNCFIGA 186
Cdd:COG0110   13 DGVVIGPGVRIYGGNITIGDnvYIGPGVTIDDPGgiTIGDNVLIGPGVTILTGnhPIDDPATFPLRTGPVTIGDDVWIGA 92
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 406936192 187 RsevvegviveegSVISMGVYLGQSTRIydrATGSISYGRIPAGSvVVAGN 237
Cdd:COG0110   93 G------------ATILPGVTIGDGAVV---GAGSVVTKDVPPYA-IVAGN 127
LbH_THP_succinylT_putative cd04649
Putative 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (THP ...
102-188 1.46e-07

Putative 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (THP succinyltransferase), C-terminal left-handed parallel alpha-helix (LbH) domain: This group is composed of mostly uncharacterized proteins containing an N-terminal domain of unknown function and a C-terminal LbH domain with similarity to THP succinyltransferase LbH. THP succinyltransferase catalyzes the conversion of tetrahydrodipicolinate and succinyl-CoA to N-succinyltetrahydrodipicolinate and CoA. It is the committed step in the succinylase pathway by which bacteria synthesize L-lysine and meso-diaminopimelate, a component of peptidoglycan. The enzyme is trimeric and displays the left-handed parallel alpha-helix (LbH) structural motif encoded by the hexapeptide repeat motif.


Pssm-ID: 100054  Cd Length: 147  Bit Score: 49.72  E-value: 1.46e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406936192 102 NVRIVPHALARKGAYIAPNTILMP-SYINLGAYIDSGTLIDtwATVGSCAQIGKNVHLSGGAGIGGVLEPLQANPTIIED 180
Cdd:cd04649    1 GVRIADADRVRLGAYLAEGTTVMHeGFVNFNAGTLGNCMVE--GRISSGVIVGKGSDVGGGASIMGTLSGGGNNVISIGK 78

                 ....*...
gi 406936192 181 NCFIGARS 188
Cdd:cd04649   79 RCLLGANS 86
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
126-237 6.90e-07

Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, galactoside O-acetyltransferase (GAT), xenobiotic acyltransferase (XAT) and similar proteins. MAT and GAT catalyze the CoA-dependent acetylation of the 6-hydroxyl group of their respective sugar substrates. MAT acetylates maltose and glucose exclusively while GAT specifically acetylates galactopyranosides. XAT catalyzes the CoA-dependent acetylation of a variety of hydroxyl-bearing acceptors such as chloramphenicol and streptogramin, among others. XATs are implicated in inactivating xenobiotics leading to xenobiotic resistance in patients. Members of this family contain a a left-handed parallel beta-helix (LbH) domain with at least 5 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). They are trimeric in their active form.


Pssm-ID: 100053 [Multi-domain]  Cd Length: 109  Bit Score: 46.68  E-value: 6.90e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406936192 126 SYINLGAYIDSGTLIDtwatvgscaqIGKNVHLSGGAGI-----------GGVLEPLQANPTIIEDNCFIGARsevvegv 194
Cdd:cd04647    8 VYIGPGCVISAGGGIT----------IGDNVLIGPNVTIydhnhdiddpeRPIEQGVTSAPIVIGDDVWIGAN------- 70
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 406936192 195 iveegSVISMGVYLGQSTRIydrATGSISYGRIPAGSvVVAGN 237
Cdd:cd04647   71 -----VVILPGVTIGDGAVV---GAGSVVTKDVPPNS-IVAGN 104
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
107-237 1.73e-06

Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is composed of mostly uncharacterized proteins containing an N-terminal helical subdomain followed by a LbH domain. The alignment contains 6 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity. A few members are identified as NeuD, a sialic acid (Sia) O-acetyltransferase that is required for Sia synthesis and surface polysaccharide sialylation.


Pssm-ID: 100050 [Multi-domain]  Cd Length: 197  Bit Score: 47.48  E-value: 1.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406936192 107 PHALARKGAYIAPNTILMP-SYINLGAYIDSGTLIDTWATVGSCAQIGKNVHLSGGAGI-GGVleplqanptIIEDNCFI 184
Cdd:cd03360   89 PSAVVSPSAVIGEGCVIMAgAVINPDARIGDNVIINTGAVIGHDCVIGDFVHIAPGVVLsGGV---------TIGEGAFI 159
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 406936192 185 GARsevvegviveegSVISMGVYLGQSTRIydrATGSISYGRIPAGSVVVaGN 237
Cdd:cd03360  160 GAG------------ATIIQGVTIGAGAII---GAGAVVTKDVPDGSVVV-GN 196
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
100-186 1.11e-05

UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of 3-hydroxymyristic acid or 3-hydroxy-arachidic acid, depending on the organism, from the acyl carrier protein (ACP) to UDP-3-O-acyl-glucosamine to produce UDP-2,3-diacyl-GlcNAc. This constitutes the third step in the lipid A biosynthetic pathway in Gram-negative bacteria. LpxD is a homotrimer, with each subunit consisting of a novel combination of an N-terminal uridine-binding domain, a core lipid-binding left-handed parallel beta helix (LbH) domain, and a C-terminal alpha-helical extension. The LbH domain contains 9 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X).


Pssm-ID: 100043 [Multi-domain]  Cd Length: 205  Bit Score: 45.09  E-value: 1.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406936192 100 ADNVRIVPHALARKGAYIAPNTILMP-SYINLGAYIDSGTLIDTWATVGSCAQIGKNVHLSGGAGIG----------GVL 168
Cdd:cd03352    5 GENVSIGPNAVIGEGVVIGDGVVIGPgVVIGDGVVIGDDCVIHPNVTIYEGCIIGDRVIIHSGAVIGsdgfgfapdgGGW 84
                         90
                 ....*....|....*....
gi 406936192 169 EPL-QANPTIIEDNCFIGA 186
Cdd:cd03352   85 VKIpQLGGVIIGDDVEIGA 103
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
100-186 3.31e-05

UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope biogenesis]; UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase is part of the Pathway/BioSystem: Lipid A biosynthesis


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 44.62  E-value: 3.31e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406936192 100 ADNVRIVPHALARKGAYIAPNTILMP-SYINLGAYIDSGTLIDTWATVGSCAQIGKNVHLSGGAGIG-----------GV 167
Cdd:COG1044  112 GEGVSIGPFAVIGAGVVIGDGVVIGPgVVIGDGVVIGDDCVLHPNVTIYERCVIGDRVIIHSGAVIGadgfgfapdedGG 191
                         90       100
                 ....*....|....*....|
gi 406936192 168 LEPL-QANPTIIEDNCFIGA 186
Cdd:COG1044  192 WVKIpQLGRVVIGDDVEIGA 211
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
80-186 6.85e-04

UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 40.51  E-value: 6.85e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406936192  80 TQFYDKVPLKF--------AHYSSDQFAADNVRIVPHALARKGAYIAPNTILMP-SYINLGAYIDSGTLIDTWATVGSCA 150
Cdd:PRK00892  88 AQLFDPPATPSpaagihpsAVIDPSAKIGEGVSIGPNAVIGAGVVIGDGVVIGAgAVIGDGVKIGADCRLHANVTIYHAV 167
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 406936192 151 QIGKNVHLSGGAGIG----GVleplqANPT------------IIEDNCFIGA 186
Cdd:PRK00892 168 RIGNRVIIHSGAVIGsdgfGF-----ANDRggwvkipqlgrvIIGDDVEIGA 214
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
128-186 1.08e-03

Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain hydroxyl group of L-serine to form O-acetylserine, as the first step of a two-step biosynthetic pathway in bacteria and plants leading to the formation of L-cysteine. This reaction represents a key metabolic point of regulation for the cysteine biosynthetic pathway due to its feedback inhibition by cysteine. The enzyme is a 175 kDa homohexamer, composed of a dimer of homotrimers. Each subunit contains an N-terminal alpha helical region and a C-terminal left-handed beta-helix (LbH) subdomain with 5 turns, each containing a hexapeptide repeat motif characteristic of the acyltransferase superfamily of enzymes. The trimer interface mainly involves the C-terminal LbH subdomain while the dimer (of trimers) interface is mediated by the N-terminal alpha helical subdomain.


Pssm-ID: 100045 [Multi-domain]  Cd Length: 101  Bit Score: 37.42  E-value: 1.08e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 406936192 128 INLGAYIDSGTLID--TWATVGSCAQIGKNVHLSGGAGIGGVLEPLQANPTIIEDNCFIGA 186
Cdd:cd03354    5 IHPGAKIGPGLFIDhgTGIVIGETAVIGDNCTIYQGVTLGGKGKGGGKRHPTIGDNVVIGA 65
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
108-186 6.00e-03

Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is part of the Pathway/BioSystem: Cysteine biosynthesis


Pssm-ID: 440667 [Multi-domain]  Cd Length: 174  Bit Score: 36.60  E-value: 6.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406936192 108 HALARKGAYIAP------NTILMPSYINLGAYIDSGTLID--TWATVGSCAQIGKNVHLSGGAGIGGV-LEPLQANPTiI 178
Cdd:COG1045   42 HWLWKRGLPLLArllserARFLTGIDIHPGATIGRGFFIDhgTGVVIGETAVIGDNVTIYQGVTLGGTgKEKGKRHPT-I 120

                 ....*...
gi 406936192 179 EDNCFIGA 186
Cdd:COG1045  121 GDNVVIGA 128
 
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.
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