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Conserved domains on  [gi|679630065|gb|KFX12364|]
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2,3,4,5-tetrahydropyridine-2,6-carboxylate N-succinyltransferase [Pectobacterium atrosepticum]

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
 3-272 0e+00

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


:

Pssm-ID: 236996 [Multi-domain]  Cd Length: 272  Bit Score: 517.44  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 679630065   3 QQLQNIIETAFERRADITPANADTVTREAVNQAINLLDSGALRVAEKI-DGQWVTHQWLKKAVLLSFRINDNQLIEGGET 81
Cdd:PRK11830   2 SQLQKIIEEAWERRAELTPATADTEVREAVEEVIDLLDSGELRVAEKIdDGEWVVNQWVKKAILLSFRLNDNQVIEGGDF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 679630065  82 RFFDKVPMKFADYDEARFQREGVRVAPPASVRRGAYIARNTVLMPSYVNIGAYVDEGTMVDTWVTVGSCAQIGKNVHLSG 161
Cdd:PRK11830  82 RFYDKVPLKFAGWDEARFKEAGVRVVPGAVVRRGAYIAPNVVLMPSYVNIGAYVDEGTMVDTWATVGSCAQIGKNVHLSG 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 679630065 162 GVGIGGVLEPLQANPTIIEDNCFIGARSEVVEGVVVEEGSVISMGVFISQSTRIYDRETGEIHYGRVPAGSVVVSGNLPS 241
Cdd:PRK11830 162 GVGIGGVLEPLQANPVIIEDNCFIGARSEVVEGVIVEEGSVLGMGVFLGQSTKIYDRETGEVHYGRVPAGSVVVPGSLPS 241

                        250       260       270
                 ....*....|....*....|....*....|.
gi 679630065 242 KDGSHSMYCAIIVKKVDAKTRGKVGINELLR 272
Cdd:PRK11830 242 KDGGYSLYCAVIVKKVDAKTRSKTSINELLR 272
 
Name Accession Description Interval E-value
dapD PRK11830
2,3,4,5-tetrahydropyridine-2,6-carboxylate N-succinyltransferase; Provisional
 3-272 0e+00

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


Pssm-ID: 236996 [Multi-domain]  Cd Length: 272  Bit Score: 517.44  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 679630065   3 QQLQNIIETAFERRADITPANADTVTREAVNQAINLLDSGALRVAEKI-DGQWVTHQWLKKAVLLSFRINDNQLIEGGET 81
Cdd:PRK11830   2 SQLQKIIEEAWERRAELTPATADTEVREAVEEVIDLLDSGELRVAEKIdDGEWVVNQWVKKAILLSFRLNDNQVIEGGDF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 679630065  82 RFFDKVPMKFADYDEARFQREGVRVAPPASVRRGAYIARNTVLMPSYVNIGAYVDEGTMVDTWVTVGSCAQIGKNVHLSG 161
Cdd:PRK11830  82 RFYDKVPLKFAGWDEARFKEAGVRVVPGAVVRRGAYIAPNVVLMPSYVNIGAYVDEGTMVDTWATVGSCAQIGKNVHLSG 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 679630065 162 GVGIGGVLEPLQANPTIIEDNCFIGARSEVVEGVVVEEGSVISMGVFISQSTRIYDRETGEIHYGRVPAGSVVVSGNLPS 241
Cdd:PRK11830 162 GVGIGGVLEPLQANPVIIEDNCFIGARSEVVEGVIVEEGSVLGMGVFLGQSTKIYDRETGEVHYGRVPAGSVVVPGSLPS 241

                        250       260       270
                 ....*....|....*....|....*....|.
gi 679630065 242 KDGSHSMYCAIIVKKVDAKTRGKVGINELLR 272
Cdd:PRK11830 242 KDGGYSLYCAVIVKKVDAKTRSKTSINELLR 272
dapD TIGR00965
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase; This enzyme is part of the ...
 4-272 1.79e-170

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: 471.69  E-value: 1.79e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 679630065    4 QLQNIIETAFERRADITPANADTVTREAVNQAINLLDSGALRVAEKIDGQWVTHQWLKKAVLLSFRINDNQLIEGGETRF 83
Cdd:TIGR00965   1 QLQNIIETAFERRAEITPANADTVTKEAVNEVIALLDSGALRVAEKIDGQWKVNEWLKKAVLLSFRINDNQVINGAENRY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 679630065   84 FDKVPMKFADYDEARFQREGVRVAPPASVRRGAYIARNTVLMPSYVNIGAYVDEGTMVDTWVTVGSCAQIGKNVHLSGGV 163
Cdd:TIGR00965  81 FDKVPMKFADYDEARFKKAGFRVVPGAAVRQGAFIAKNVVLMPSYVNIGAYVDEGTMVDTWATVGSCAQIGKNVHLSGGV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 679630065  164 GIGGVLEPLQANPTIIEDNCFIGARSEVVEGVVVEEGSVISMGVFISQSTRIYDRETGEIHYGRVPAGSVVVSGNLPSKD 243
Cdd:TIGR00965 161 GIGGVLEPLQANPTIIEDNCFIGARSEIVEGVIVEEGSVISMGVFIGQSTKIYDRETGEIHYGRVPAGSVVVSGNLPSKD 240

                         250       260
                  ....*....|....*....|....*....
gi 679630065  244 GSHSMYCAIIVKKVDAKTRGKVGINELLR 272
Cdd:TIGR00965 241 GKYSLYCAVIVKKVDAKTRGKVSINELLR 269
DapD COG2171
Tetrahydrodipicolinate N-succinyltransferase [Amino acid transport and metabolism]; ...
 2-274 7.30e-167

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: 462.28  E-value: 7.30e-167
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 679630065   2 HQQLQNIIETAFERRADITPAnADTVTREAVNQAINLLDSGALRVAEK-IDGQWVTHQWLKKAVLLSFRINDNQLIEGGE 80
Cdd:COG2171    1 MADLGTVIDAAWENRAELTPL-ADREVREAVEEVIAALDAGPLRVAEPnLDGEWVVNEWVKKAILLSFRLEDNRVLEGGG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 679630065  81 TRFFDKVPMKFADYDEArfqreGVRVAPPASVRRGAYIARNTVLMPSYVNIGAYVDEGTMVDTWVTVGSCAQIGKNVHLS 160
Cdd:COG2171   80 VTYHDKVPLKFDYFKPA-----GVRIVPGARVRLGAYLAPGVVLMPSFVNIGAYVDEGTMVDTWATVGSCAQIGKNVHLS 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 679630065 161 GGVGIGGVLEPLQANPTIIEDNCFIGARSEVVEGVVVEEGSVISMGVFISQSTRIYDRETGEIHYGRVPAGSVVVSGNLP 240
Cdd:COG2171  155 GGAGIGGVLEPLQAAPVIIEDNCFIGARSGVVEGVIVGEGAVLGAGVYLTASTKIYDRVTGEVYYGRVPAGSVVVPGSLP 234

                        250       260       270
                 ....*....|....*....|....*....|....
gi 679630065 241 SKDGSHSMYCAIIVKKVDAKTRGKVGINELLRSI 274
Cdd:COG2171  235 GKDGDYGLYCAVIVKRRDEKTRSKTSLNELLRDN 268
LbH_THP_succinylT cd03350
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP ...
 103-240 1.74e-67

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: 206.08  E-value: 1.74e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 679630065 103 GVRVAPPASVRRGAYIARNTVLM-PSYVNIGAYVDEGTMVDTWVTVGSCAQIGKNVHLSGGVGIGGVLEPLQANPTIIED 181
Cdd:cd03350    1 GRRVPPGAIIRDGAFIGPGAVLMmPSYVNIGAYVDEGTMVDSWATVGSCAQIGKNVHLSAGAVIGGVLEPLQATPVIIED 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 679630065 182 NCFIGARSEVVEGVVVEEGSVISMGVFISQSTRIYDRETGEIHYGRVPAGSVVVSGNLP 240
Cdd:cd03350   81 DVFIGANCEVVEGVIVGKGAVLAAGVVLTQSTPIYDRETGEIYYGRVPPGSVVVAGSLP 139
THDPS_N_2 pfam14805
Tetrahydrodipicolinate N-succinyltransferase N-terminal; This is the N-terminal domain of 2,3, ...
 4-70 1.69e-38

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: 129.51  E-value: 1.69e-38
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 679630065    4 QLQNIIETAFERRADITPANADTVTREAVNQAINLLDSGALRVAEKIDGQWVTHQWLKKAVLLSFRI 70
Cdd:pfam14805   1 SLQKIIEAAWENRALLTPATADAEVRDAVEEVIDLLDAGELRVAEKIDGGWVVNEWVKKAVLLYFRL 67
 
Name Accession Description Interval E-value
dapD PRK11830
2,3,4,5-tetrahydropyridine-2,6-carboxylate N-succinyltransferase; Provisional
 3-272 0e+00

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


Pssm-ID: 236996 [Multi-domain]  Cd Length: 272  Bit Score: 517.44  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 679630065   3 QQLQNIIETAFERRADITPANADTVTREAVNQAINLLDSGALRVAEKI-DGQWVTHQWLKKAVLLSFRINDNQLIEGGET 81
Cdd:PRK11830   2 SQLQKIIEEAWERRAELTPATADTEVREAVEEVIDLLDSGELRVAEKIdDGEWVVNQWVKKAILLSFRLNDNQVIEGGDF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 679630065  82 RFFDKVPMKFADYDEARFQREGVRVAPPASVRRGAYIARNTVLMPSYVNIGAYVDEGTMVDTWVTVGSCAQIGKNVHLSG 161
Cdd:PRK11830  82 RFYDKVPLKFAGWDEARFKEAGVRVVPGAVVRRGAYIAPNVVLMPSYVNIGAYVDEGTMVDTWATVGSCAQIGKNVHLSG 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 679630065 162 GVGIGGVLEPLQANPTIIEDNCFIGARSEVVEGVVVEEGSVISMGVFISQSTRIYDRETGEIHYGRVPAGSVVVSGNLPS 241
Cdd:PRK11830 162 GVGIGGVLEPLQANPVIIEDNCFIGARSEVVEGVIVEEGSVLGMGVFLGQSTKIYDRETGEVHYGRVPAGSVVVPGSLPS 241

                        250       260       270
                 ....*....|....*....|....*....|.
gi 679630065 242 KDGSHSMYCAIIVKKVDAKTRGKVGINELLR 272
Cdd:PRK11830 242 KDGGYSLYCAVIVKKVDAKTRSKTSINELLR 272
dapD TIGR00965
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase; This enzyme is part of the ...
 4-272 1.79e-170

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: 471.69  E-value: 1.79e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 679630065    4 QLQNIIETAFERRADITPANADTVTREAVNQAINLLDSGALRVAEKIDGQWVTHQWLKKAVLLSFRINDNQLIEGGETRF 83
Cdd:TIGR00965   1 QLQNIIETAFERRAEITPANADTVTKEAVNEVIALLDSGALRVAEKIDGQWKVNEWLKKAVLLSFRINDNQVINGAENRY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 679630065   84 FDKVPMKFADYDEARFQREGVRVAPPASVRRGAYIARNTVLMPSYVNIGAYVDEGTMVDTWVTVGSCAQIGKNVHLSGGV 163
Cdd:TIGR00965  81 FDKVPMKFADYDEARFKKAGFRVVPGAAVRQGAFIAKNVVLMPSYVNIGAYVDEGTMVDTWATVGSCAQIGKNVHLSGGV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 679630065  164 GIGGVLEPLQANPTIIEDNCFIGARSEVVEGVVVEEGSVISMGVFISQSTRIYDRETGEIHYGRVPAGSVVVSGNLPSKD 243
Cdd:TIGR00965 161 GIGGVLEPLQANPTIIEDNCFIGARSEIVEGVIVEEGSVISMGVFIGQSTKIYDRETGEIHYGRVPAGSVVVSGNLPSKD 240

                         250       260
                  ....*....|....*....|....*....
gi 679630065  244 GSHSMYCAIIVKKVDAKTRGKVGINELLR 272
Cdd:TIGR00965 241 GKYSLYCAVIVKKVDAKTRGKVSINELLR 269
DapD COG2171
Tetrahydrodipicolinate N-succinyltransferase [Amino acid transport and metabolism]; ...
 2-274 7.30e-167

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: 462.28  E-value: 7.30e-167
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 679630065   2 HQQLQNIIETAFERRADITPAnADTVTREAVNQAINLLDSGALRVAEK-IDGQWVTHQWLKKAVLLSFRINDNQLIEGGE 80
Cdd:COG2171    1 MADLGTVIDAAWENRAELTPL-ADREVREAVEEVIAALDAGPLRVAEPnLDGEWVVNEWVKKAILLSFRLEDNRVLEGGG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 679630065  81 TRFFDKVPMKFADYDEArfqreGVRVAPPASVRRGAYIARNTVLMPSYVNIGAYVDEGTMVDTWVTVGSCAQIGKNVHLS 160
Cdd:COG2171   80 VTYHDKVPLKFDYFKPA-----GVRIVPGARVRLGAYLAPGVVLMPSFVNIGAYVDEGTMVDTWATVGSCAQIGKNVHLS 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 679630065 161 GGVGIGGVLEPLQANPTIIEDNCFIGARSEVVEGVVVEEGSVISMGVFISQSTRIYDRETGEIHYGRVPAGSVVVSGNLP 240
Cdd:COG2171  155 GGAGIGGVLEPLQAAPVIIEDNCFIGARSGVVEGVIVGEGAVLGAGVYLTASTKIYDRVTGEVYYGRVPAGSVVVPGSLP 234

                        250       260       270
                 ....*....|....*....|....*....|....
gi 679630065 241 SKDGSHSMYCAIIVKKVDAKTRGKVGINELLRSI 274
Cdd:COG2171  235 GKDGDYGLYCAVIVKRRDEKTRSKTSLNELLRDN 268
LbH_THP_succinylT cd03350
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP ...
 103-240 1.74e-67

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: 206.08  E-value: 1.74e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 679630065 103 GVRVAPPASVRRGAYIARNTVLM-PSYVNIGAYVDEGTMVDTWVTVGSCAQIGKNVHLSGGVGIGGVLEPLQANPTIIED 181
Cdd:cd03350    1 GRRVPPGAIIRDGAFIGPGAVLMmPSYVNIGAYVDEGTMVDSWATVGSCAQIGKNVHLSAGAVIGGVLEPLQATPVIIED 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 679630065 182 NCFIGARSEVVEGVVVEEGSVISMGVFISQSTRIYDRETGEIHYGRVPAGSVVVSGNLP 240
Cdd:cd03350   81 DVFIGANCEVVEGVIVGKGAVLAAGVVLTQSTPIYDRETGEIYYGRVPPGSVVVAGSLP 139
THDPS_N_2 pfam14805
Tetrahydrodipicolinate N-succinyltransferase N-terminal; This is the N-terminal domain of 2,3, ...
 4-70 1.69e-38

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: 129.51  E-value: 1.69e-38
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 679630065    4 QLQNIIETAFERRADITPANADTVTREAVNQAINLLDSGALRVAEKIDGQWVTHQWLKKAVLLSFRI 70
Cdd:pfam14805   1 SLQKIIEAAWENRALLTPATADAEVRDAVEEVIDLLDAGELRVAEKIDGGWVVNEWVKKAVLLYFRL 67
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 133-188 1.60e-11

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: 58.80  E-value: 1.60e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 679630065 133 AYVDEGTMVDTWVTVGSCAQIGKNVHLSGGVGIGGVLEPLQANPTIIEDNCFIGAR 188
Cdd:cd00208    1 VFIGEGVKIHPKAVIRGPVVIGDNVNIGPGAVIGAATGPNEKNPTIIGDNVEIGAN 56
LbH_THP_succinylT_putative cd04649
Putative 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (THP ...
 103-187 2.15e-08

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: 52.03  E-value: 2.15e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 679630065 103 GVRVAPPASVRRGAYIARNTVLMP-SYVNIGAYVDEGTMVDTWVTVGscAQIGKNVHLSGGVGIGGVLEPLQANPTIIED 181
Cdd:cd04649    1 GVRIADADRVRLGAYLAEGTTVMHeGFVNFNAGTLGNCMVEGRISSG--VIVGKGSDVGGGASIMGTLSGGGNNVISIGK 78


                 ....*.
gi 679630065 182 NCFIGA 187
Cdd:cd04649   79 RCLLGA 84
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 106-187 1.23e-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: 47.86  E-value: 1.23e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 679630065 106 VAPPASVRRGAYIARNTVLMP-SYVNIGAYVDEGTMVDTWVTVGSCAQIGKNVHLSGGVGI-GGVleplqanptIIEDNC 183
Cdd:cd03360   87 IHPSAVVSPSAVIGEGCVIMAgAVINPDARIGDNVIINTGAVIGHDCVIGDFVHIAPGVVLsGGV---------TIGEGA 157


                 ....
gi 679630065 184 FIGA 187
Cdd:cd03360  158 FIGA 161
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
110-188 2.16e-06

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 46.02  E-value: 2.16e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 679630065 110 ASVRRGAYIARNTVLMPSYVNIGAYVDEGTmvDTWVTVGSCAQIGKNVHLSGGVGIGGV--------LEPLQANPTIIED 181
Cdd:COG0110    9 ARIGDGVVIGPGVRIYGGNITIGDNVYIGP--GVTIDDPGGITIGDNVLIGPGVTILTGnhpiddpaTFPLRTGPVTIGD 86


                 ....*..
gi 679630065 182 NCFIGAR 188
Cdd:COG0110   87 DVWIGAG 93
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 102-187 2.51e-04

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: 41.93  E-value: 2.51e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 679630065 102 EGVRVAPPASVRRGAYIARNTVLMPsyvniGAYVDEGTMV--DTW----VTVGSCAQIGKNVHLSGGVGIG--------- 166
Cdd:COG1044  113 EGVSIGPFAVIGAGVVIGDGVVIGP-----GVVIGDGVVIgdDCVlhpnVTIYERCVIGDRVIIHSGAVIGadgfgfapd 187

                         90       100
                 ....*....|....*....|....
gi 679630065 167 --GVLEPL-QANPTIIEDNCFIGA 187
Cdd:COG1044  188 edGGWVKIpQLGRVVIGDDVEIGA 211
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 102-187 3.89e-04

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: 40.47  E-value: 3.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 679630065 102 EGVRVAPPASVRRGAYIARNTVLMPSyVNIGAYV--DEGTMVDTWVTVGSCAQIGKNVHLSGGVGIG----------GVL 169
Cdd:cd03352    6 ENVSIGPNAVIGEGVVIGDGVVIGPG-VVIGDGVviGDDCVIHPNVTIYEGCIIGDRVIIHSGAVIGsdgfgfapdgGGW 84

                         90
                 ....*....|....*....
gi 679630065 170 EPL-QANPTIIEDNCFIGA 187
Cdd:cd03352   85 VKIpQLGGVIIGDDVEIGA 103
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 132-187 7.53e-04

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: 39.30  E-value: 7.53e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 679630065 132 GAYVDEGTMVD--TWVTVGSCAQIGKNVHLSGGVGIGGV-LEPLQANPTiIEDNCFIGA 187
Cdd:COG1045   71 GATIGRGFFIDhgTGVVIGETAVIGDNVTIYQGVTLGGTgKEKGKRHPT-IGDNVVIGA 128
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 145-187 1.73e-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: 37.03  E-value: 1.73e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 679630065 145 VTVGSCAQIGKNVHLSGGVGIGGVLEPLQANPTIIEDNCFIGA 187
Cdd:cd03354   23 IVIGETAVIGDNCTIYQGVTLGGKGKGGGKRHPTIGDNVVIGA 65
 
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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