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Conserved domains on  [gi|1042197645|ref|WP_065252815|]
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MULTISPECIES: 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase [Moraxella]

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 0e+00

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


:

Pssm-ID: 236996 [Multi-domain]  Cd Length: 272  Bit Score: 555.19  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042197645   1 MSLQQIIEDAFENRANFNPNDATDDVRAAVNDVLAQLDAGTLRVAEKK-DGEWIVNQWVKKAVLLSFRLNDNRIMNGGrD 79
Cdd:PRK11830    2 SQLQKIIEEAWERRAELTPATADTEVREAVEEVIDLLDSGELRVAEKIdDGEWVVNQWVKKAILLSFRLNDNQVIEGG-D 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042197645  80 LQFFDKVETKFSDWGDEQFAKAGVRVVPPAVARKGSYIAKGAILMPSYVNIGAYVDEGTMVDTWATVGSCAQIGKNVHLS 159
Cdd:PRK11830   81 FRFYDKVPLKFAGWDEARFKEAGVRVVPGAVVRRGAYIAPNVVLMPSYVNIGAYVDEGTMVDTWATVGSCAQIGKNVHLS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042197645 160 GGVGIGGVLEPLQANPTIIEDNCFIGARSEIVEGVIVEEGSVISMGVYIGQSTKILDRETGEISYGRIPAGSVVVSGSLP 239
Cdd:PRK11830  161 GGVGIGGVLEPLQANPVIIEDNCFIGARSEVVEGVIVEEGSVLGMGVFLGQSTKIYDRETGEVHYGRVPAGSVVVPGSLP 240

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1042197645 240 SKDGSHSLYCAVIVKKVDAQTRSKTSINDLLR 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 0e+00

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


Pssm-ID: 236996 [Multi-domain]  Cd Length: 272  Bit Score: 555.19  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042197645   1 MSLQQIIEDAFENRANFNPNDATDDVRAAVNDVLAQLDAGTLRVAEKK-DGEWIVNQWVKKAVLLSFRLNDNRIMNGGrD 79
Cdd:PRK11830    2 SQLQKIIEEAWERRAELTPATADTEVREAVEEVIDLLDSGELRVAEKIdDGEWVVNQWVKKAILLSFRLNDNQVIEGG-D 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042197645  80 LQFFDKVETKFSDWGDEQFAKAGVRVVPPAVARKGSYIAKGAILMPSYVNIGAYVDEGTMVDTWATVGSCAQIGKNVHLS 159
Cdd:PRK11830   81 FRFYDKVPLKFAGWDEARFKEAGVRVVPGAVVRRGAYIAPNVVLMPSYVNIGAYVDEGTMVDTWATVGSCAQIGKNVHLS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042197645 160 GGVGIGGVLEPLQANPTIIEDNCFIGARSEIVEGVIVEEGSVISMGVYIGQSTKILDRETGEISYGRIPAGSVVVSGSLP 239
Cdd:PRK11830  161 GGVGIGGVLEPLQANPVIIEDNCFIGARSEVVEGVIVEEGSVLGMGVFLGQSTKIYDRETGEVHYGRVPAGSVVVPGSLP 240

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1042197645 240 SKDGSHSLYCAVIVKKVDAQTRSKTSINDLLR 271
Cdd:PRK11830  241 SKDGGYSLYCAVIVKKVDAKTRSKTSINELLR 272
DapD COG2171
Tetrahydrodipicolinate N-succinyltransferase [Amino acid transport and metabolism]; ...
 2-273 0e+00

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: 498.10  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042197645   2 SLQQIIEDAFENRANFNPNdATDDVRAAVNDVLAQLDAGTLRVAEK-KDGEWIVNQWVKKAVLLSFRLNDNRIMNGGrDL 80
Cdd:COG2171     3 DLGTVIDAAWENRAELTPL-ADREVREAVEEVIAALDAGPLRVAEPnLDGEWVVNEWVKKAILLSFRLEDNRVLEGG-GV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042197645  81 QFFDKVETKFSDwgdeqFAKAGVRVVPPAVARKGSYIAKGAILMPSYVNIGAYVDEGTMVDTWATVGSCAQIGKNVHLSG 160
Cdd:COG2171    81 TYHDKVPLKFDY-----FKPAGVRIVPGARVRLGAYLAPGVVLMPSFVNIGAYVDEGTMVDTWATVGSCAQIGKNVHLSG 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042197645 161 GVGIGGVLEPLQANPTIIEDNCFIGARSEIVEGVIVEEGSVISMGVYIGQSTKILDRETGEISYGRIPAGSVVVSGSLPS 240
Cdd:COG2171   156 GAGIGGVLEPLQAAPVIIEDNCFIGARSGVVEGVIVGEGAVLGAGVYLTASTKIYDRVTGEVYYGRVPAGSVVVPGSLPG 235

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1042197645 241 KDGSHSLYCAVIVKKVDAQTRSKTSINDLLRMD 273
Cdd:COG2171   236 KDGDYGLYCAVIVKRRDEKTRSKTSLNELLRDN 268
dapD TIGR00965
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase; This enzyme is part of the ...
 2-271 1.66e-163

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: 453.97  E-value: 1.66e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042197645   2 SLQQIIEDAFENRANFNPNDATDDVRAAVNDVLAQLDAGTLRVAEKKDGEWIVNQWVKKAVLLSFRLNDNRIMNGGRDlQ 81
Cdd:TIGR00965   1 QLQNIIETAFERRAEITPANADTVTKEAVNEVIALLDSGALRVAEKIDGQWKVNEWLKKAVLLSFRINDNQVINGAEN-R 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042197645  82 FFDKVETKFSDWGDEQFAKAGVRVVPPAVARKGSYIAKGAILMPSYVNIGAYVDEGTMVDTWATVGSCAQIGKNVHLSGG 161
Cdd:TIGR00965  80 YFDKVPMKFADYDEARFKKAGFRVVPGAAVRQGAFIAKNVVLMPSYVNIGAYVDEGTMVDTWATVGSCAQIGKNVHLSGG 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042197645 162 VGIGGVLEPLQANPTIIEDNCFIGARSEIVEGVIVEEGSVISMGVYIGQSTKILDRETGEISYGRIPAGSVVVSGSLPSK 241
Cdd:TIGR00965 160 VGIGGVLEPLQANPTIIEDNCFIGARSEIVEGVIVEEGSVISMGVFIGQSTKIYDRETGEIHYGRVPAGSVVVSGNLPSK 239

                         250       260       270
                  ....*....|....*....|....*....|
gi 1042197645 242 DGSHSLYCAVIVKKVDAQTRSKTSINDLLR 271
Cdd:TIGR00965 240 DGKYSLYCAVIVKKVDAKTRGKVSINELLR 269
LbH_THP_succinylT cd03350
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP ...
 102-239 1.45e-78

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: 233.81  E-value: 1.45e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042197645 102 GVRVVPPAVARKGSYIAKGAILM-PSYVNIGAYVDEGTMVDTWATVGSCAQIGKNVHLSGGVGIGGVLEPLQANPTIIED 180
Cdd:cd03350     1 GRRVPPGAIIRDGAFIGPGAVLMmPSYVNIGAYVDEGTMVDSWATVGSCAQIGKNVHLSAGAVIGGVLEPLQATPVIIED 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1042197645 181 NCFIGARSEIVEGVIVEEGSVISMGVYIGQSTKILDRETGEISYGRIPAGSVVVSGSLP 239
Cdd:cd03350    81 DVFIGANCEVVEGVIVGKGAVLAAGVVLTQSTPIYDRETGEIYYGRVPPGSVVVAGSLP 139
THDPS_N_2 pfam14805
Tetrahydrodipicolinate N-succinyltransferase N-terminal; This is the N-terminal domain of 2,3, ...
 2-68 6.66e-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: 127.59  E-value: 6.66e-38
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1042197645   2 SLQQIIEDAFENRANFNPNDATDDVRAAVNDVLAQLDAGTLRVAEKKDGEWIVNQWVKKAVLLSFRL 68
Cdd:pfam14805   1 SLQKIIEAAWENRALLTPATADAEVRDAVEEVIDLLDAGELRVAEKIDGGWVVNEWVKKAVLLYFRL 67
 
Name Accession Description Interval E-value
dapD PRK11830
2,3,4,5-tetrahydropyridine-2,6-carboxylate N-succinyltransferase; Provisional
 1-271 0e+00

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


Pssm-ID: 236996 [Multi-domain]  Cd Length: 272  Bit Score: 555.19  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042197645   1 MSLQQIIEDAFENRANFNPNDATDDVRAAVNDVLAQLDAGTLRVAEKK-DGEWIVNQWVKKAVLLSFRLNDNRIMNGGrD 79
Cdd:PRK11830    2 SQLQKIIEEAWERRAELTPATADTEVREAVEEVIDLLDSGELRVAEKIdDGEWVVNQWVKKAILLSFRLNDNQVIEGG-D 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042197645  80 LQFFDKVETKFSDWGDEQFAKAGVRVVPPAVARKGSYIAKGAILMPSYVNIGAYVDEGTMVDTWATVGSCAQIGKNVHLS 159
Cdd:PRK11830   81 FRFYDKVPLKFAGWDEARFKEAGVRVVPGAVVRRGAYIAPNVVLMPSYVNIGAYVDEGTMVDTWATVGSCAQIGKNVHLS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042197645 160 GGVGIGGVLEPLQANPTIIEDNCFIGARSEIVEGVIVEEGSVISMGVYIGQSTKILDRETGEISYGRIPAGSVVVSGSLP 239
Cdd:PRK11830  161 GGVGIGGVLEPLQANPVIIEDNCFIGARSEVVEGVIVEEGSVLGMGVFLGQSTKIYDRETGEVHYGRVPAGSVVVPGSLP 240

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1042197645 240 SKDGSHSLYCAVIVKKVDAQTRSKTSINDLLR 271
Cdd:PRK11830  241 SKDGGYSLYCAVIVKKVDAKTRSKTSINELLR 272
DapD COG2171
Tetrahydrodipicolinate N-succinyltransferase [Amino acid transport and metabolism]; ...
 2-273 0e+00

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: 498.10  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042197645   2 SLQQIIEDAFENRANFNPNdATDDVRAAVNDVLAQLDAGTLRVAEK-KDGEWIVNQWVKKAVLLSFRLNDNRIMNGGrDL 80
Cdd:COG2171     3 DLGTVIDAAWENRAELTPL-ADREVREAVEEVIAALDAGPLRVAEPnLDGEWVVNEWVKKAILLSFRLEDNRVLEGG-GV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042197645  81 QFFDKVETKFSDwgdeqFAKAGVRVVPPAVARKGSYIAKGAILMPSYVNIGAYVDEGTMVDTWATVGSCAQIGKNVHLSG 160
Cdd:COG2171    81 TYHDKVPLKFDY-----FKPAGVRIVPGARVRLGAYLAPGVVLMPSFVNIGAYVDEGTMVDTWATVGSCAQIGKNVHLSG 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042197645 161 GVGIGGVLEPLQANPTIIEDNCFIGARSEIVEGVIVEEGSVISMGVYIGQSTKILDRETGEISYGRIPAGSVVVSGSLPS 240
Cdd:COG2171   156 GAGIGGVLEPLQAAPVIIEDNCFIGARSGVVEGVIVGEGAVLGAGVYLTASTKIYDRVTGEVYYGRVPAGSVVVPGSLPG 235

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1042197645 241 KDGSHSLYCAVIVKKVDAQTRSKTSINDLLRMD 273
Cdd:COG2171   236 KDGDYGLYCAVIVKRRDEKTRSKTSLNELLRDN 268
dapD TIGR00965
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase; This enzyme is part of the ...
 2-271 1.66e-163

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: 453.97  E-value: 1.66e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042197645   2 SLQQIIEDAFENRANFNPNDATDDVRAAVNDVLAQLDAGTLRVAEKKDGEWIVNQWVKKAVLLSFRLNDNRIMNGGRDlQ 81
Cdd:TIGR00965   1 QLQNIIETAFERRAEITPANADTVTKEAVNEVIALLDSGALRVAEKIDGQWKVNEWLKKAVLLSFRINDNQVINGAEN-R 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042197645  82 FFDKVETKFSDWGDEQFAKAGVRVVPPAVARKGSYIAKGAILMPSYVNIGAYVDEGTMVDTWATVGSCAQIGKNVHLSGG 161
Cdd:TIGR00965  80 YFDKVPMKFADYDEARFKKAGFRVVPGAAVRQGAFIAKNVVLMPSYVNIGAYVDEGTMVDTWATVGSCAQIGKNVHLSGG 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042197645 162 VGIGGVLEPLQANPTIIEDNCFIGARSEIVEGVIVEEGSVISMGVYIGQSTKILDRETGEISYGRIPAGSVVVSGSLPSK 241
Cdd:TIGR00965 160 VGIGGVLEPLQANPTIIEDNCFIGARSEIVEGVIVEEGSVISMGVFIGQSTKIYDRETGEIHYGRVPAGSVVVSGNLPSK 239

                         250       260       270
                  ....*....|....*....|....*....|
gi 1042197645 242 DGSHSLYCAVIVKKVDAQTRSKTSINDLLR 271
Cdd:TIGR00965 240 DGKYSLYCAVIVKKVDAKTRGKVSINELLR 269
LbH_THP_succinylT cd03350
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP ...
 102-239 1.45e-78

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: 233.81  E-value: 1.45e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042197645 102 GVRVVPPAVARKGSYIAKGAILM-PSYVNIGAYVDEGTMVDTWATVGSCAQIGKNVHLSGGVGIGGVLEPLQANPTIIED 180
Cdd:cd03350     1 GRRVPPGAIIRDGAFIGPGAVLMmPSYVNIGAYVDEGTMVDSWATVGSCAQIGKNVHLSAGAVIGGVLEPLQATPVIIED 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1042197645 181 NCFIGARSEIVEGVIVEEGSVISMGVYIGQSTKILDRETGEISYGRIPAGSVVVSGSLP 239
Cdd:cd03350    81 DVFIGANCEVVEGVIVGKGAVLAAGVVLTQSTPIYDRETGEIYYGRVPPGSVVVAGSLP 139
THDPS_N_2 pfam14805
Tetrahydrodipicolinate N-succinyltransferase N-terminal; This is the N-terminal domain of 2,3, ...
 2-68 6.66e-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: 127.59  E-value: 6.66e-38
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1042197645   2 SLQQIIEDAFENRANFNPNDATDDVRAAVNDVLAQLDAGTLRVAEKKDGEWIVNQWVKKAVLLSFRL 68
Cdd:pfam14805   1 SLQKIIEAAWENRALLTPATADAEVRDAVEEVIDLLDAGELRVAEKIDGGWVVNEWVKKAVLLYFRL 67
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 132-209 1.19e-18

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: 78.06  E-value: 1.19e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1042197645 132 AYVDEGTMVDTWATVGSCAQIGKNVHLSGGVGIGGVLEPLQANPTIIEDNCFIGARSEIVEGVIVEEGSVISMGVYIG 209
Cdd:cd00208     1 VFIGEGVKIHPKAVIRGPVVIGDNVNIGPGAVIGAATGPNEKNPTIIGDNVEIGANAVIHGGVKIGDNAVIGAGAVVT 78
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
113-205 2.16e-11

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 60.27  E-value: 2.16e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042197645 113 KGSYIAKGAILMPSYVNIGAYVD--EGTMVDTWATVgscaQIGKNVHLSGGVGIGGV--------LEPLQANPTIIEDNC 182
Cdd:COG0110    13 DGVVIGPGVRIYGGNITIGDNVYigPGVTIDDPGGI----TIGDNVLIGPGVTILTGnhpiddpaTFPLRTGPVTIGDDV 88

                          90       100
                  ....*....|....*....|...
gi 1042197645 183 FIGARSEIVEGVIVEEGSVISMG 205
Cdd:COG0110    89 WIGAGATILPGVTIGDGAVVGAG 111
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 96-234 1.13e-10

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: 59.42  E-value: 1.13e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042197645  96 EQFAKAGVRVV----PPAVARKGSYIAKGAILMP-SYVNIGAYVDEGTMVDTWATVGSCAQIGKNVHLSGGVGI-GGVle 169
Cdd:cd03360    74 EKLLAAGYRFAtlihPSAVVSPSAVIGEGCVIMAgAVINPDARIGDNVIINTGAVIGHDCVIGDFVHIAPGVVLsGGV-- 151

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1042197645 170 plqanptIIEDNCFIGARSEIVEGVIVEEGSVISMGVYIgqsTKildretgeisygRIPAGSVVV 234
Cdd:cd03360   152 -------TIGEGAFIGAGATIIQGVTIGAGAIIGAGAVV---TK------------DVPDGSVVV 194
LbH_THP_succinylT_putative cd04649
Putative 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (THP ...
 102-215 8.02e-09

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: 53.19  E-value: 8.02e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042197645 102 GVRVVPPAVARKGSYIAKGAILMP-SYVNIGAYVDEGTMVDtwATVGSCAQIGKNVHLSGGVGIGGVLEPLQANPTIIED 180
Cdd:cd04649     1 GVRIADADRVRLGAYLAEGTTVMHeGFVNFNAGTLGNCMVE--GRISSGVIVGKGSDVGGGASIMGTLSGGGNNVISIGK 78

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1042197645 181 NCFIGARSEIveGVIVEEGSVISMGVYIGQSTKIL 215
Cdd:cd04649    79 RCLLGANSGI--GISLGDNCIVEAGLYVTAGTKVT 111
Hexapep_2 pfam14602
Hexapeptide repeat of succinyl-transferase;
176-210 2.96e-07

Hexapeptide repeat of succinyl-transferase;


Pssm-ID: 434064 [Multi-domain]  Cd Length: 33  Bit Score: 45.89  E-value: 2.96e-07
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1042197645 176 TIIEDNCFIGARSEIveGVIVEEGSVISMGVYIGQ 210
Cdd:pfam14602   1 VIIGDNCLIGANSGI--GVSLGDNCVVGAGVVITA 33
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 152-205 4.93e-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: 47.07  E-value: 4.93e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1042197645 152 IGKNVHLSGGVGI-----------GGVLEPLQANPTIIEDNCFIGARSEIVEGVIVEEGSVISMG 205
Cdd:cd04647    24 IGDNVLIGPNVTIydhnhdiddpeRPIEQGVTSAPIVIGDDVWIGANVVILPGVTIGDGAVVGAG 88
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 146-234 6.74e-07

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: 46.66  E-value: 6.74e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042197645 146 VGSCAQIGKNVHLSGGVGIGGVLEPLQANPTIIEDNCFIGARSEIVEGVIVEEGSVISMGVYIGQStkildretgeisyg 225
Cdd:cd03354    25 IGETAVIGDNCTIYQGVTLGGKGKGGGKRHPTIGDNVVIGAGAKILGNITIGDNVKIGANAVVTKD-------------- 90


                  ....*....
gi 1042197645 226 rIPAGSVVV 234
Cdd:cd03354    91 -VPANSTVV 98
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 130-234 6.05e-06

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: 45.46  E-value: 6.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042197645 130 IGAYV--DEGTMVdtwaTVGSCAQIGKNVHLSGGVGIGGV-LEPLQANPTiIEDNCFIGARSEIVEGVIVEEGSVISMGV 206
Cdd:COG1045    74 IGRGFfiDHGTGV----VIGETAVIGDNVTIYQGVTLGGTgKEKGKRHPT-IGDNVVIGAGAKILGPITIGDNAKIGANS 148

                          90       100
                  ....*....|....*....|....*...
gi 1042197645 207 YIGQStkildretgeisygrIPAGSVVV 234
Cdd:COG1045   149 VVLKD---------------VPPGSTVV 161
LbH_Dynactin_5 cd03359
Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that ...
 115-202 6.52e-06

Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that stimulates dynein-mediated vesicle transport. Dynactin is a heterocomplex of at least eight subunits, including a 150,000-MW protein called Glued, the actin-capping protein Arp1, and dynamatin. In vitro binding experiments show that dynactin enhances dynein-dependent motility, possibly through interaction with microtubules and vesicles. Subunit p25 is part of the pointed-end subcomplex in dynactin that also includes p26, p27, and Arp11. This subcomplex interacts with membranous cargoes. p25 and p27 contain imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), indicating a left-handed parallel beta helix (LbH) structural domain. Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity.


Pssm-ID: 100049 [Multi-domain]  Cd Length: 161  Bit Score: 45.28  E-value: 6.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042197645 115 SYIAKGAILMPSY-----------VNIGAYV--DEGTMVdtwatvgSCAQIGKNVHlsggvgiggvleplqanptiIEDN 181
Cdd:cd03359    49 CILSEGCVIRPPFkkfskgvaffpLHIGDYVfiGENCVV-------NAAQIGSYVH--------------------IGKN 101

                          90       100
                  ....*....|....*....|.
gi 1042197645 182 CFIGARSEIVEGVIVEEGSVI 202
Cdd:cd03359   102 CVIGRRCIIKDCVKILDGTVV 122
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 98-202 2.70e-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: 2.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042197645  98 FAKAGVRVVPPAVARKG----SYIAKGAILMPSyVNIGAYvdegtmvdtwATVGSCAQIGKNVHLSGGVgiggvleplqa 173
Cdd:COG1044    82 FAKLLQLFYPPPAPAPGihpsAVIDPSAKIGEG-VSIGPF----------AVIGAGVVIGDGVVIGPGV----------- 139

                          90       100
                  ....*....|....*....|....*....
gi 1042197645 174 nptIIEDNCFIGARSEIVEGVIVEEGSVI 202
Cdd:COG1044   140 ---VIGDGVVIGDDCVLHPNVTIYERCVI 165
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 98-210 4.42e-05

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 43.97  E-value: 4.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042197645  98 FAKAGVRVVPPAVARKGSYIAKGAILMPSyvnigAYVDEGTMVDTWATVGSCAQIGKNVHLSGGVGIG-GVleplqanpt 176
Cdd:PRK00892   84 FARLAQLFDPPATPSPAAGIHPSAVIDPS-----AKIGEGVSIGPNAVIGAGVVIGDGVVIGAGAVIGdGV--------- 149

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1042197645 177 IIEDNCFIGARSEIVEGVIVEEGSVISMGVYIGQ 210
Cdd:PRK00892  150 KIGADCRLHANVTIYHAVRIGNRVIIHSGAVIGS 183
LbH_eIF2B_epsilon cd05787
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 131-210 7.60e-05

eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a eukaryotic translation initiator, a guanine nucleotide exchange factor (GEF) composed of five different subunits (alpha, beta, gamma, delta and epsilon). eIF2B is important for regenerating GTP-bound eIF2 during the initiation process. This event is obligatory for eIF2 to bind initiator methionyl-tRNA, forming the ternary initiation complex. The eIF-2B epsilon subunit contains an N-terminal domain that resembles a dinucleotide-binding Rossmann fold, a central LbH domain containing 4 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), and a C-terminal domain of unknown function that is present in eIF-4 gamma, eIF-5, and eIF-2B epsilon. The epsilon and gamma subunits form the catalytic subcomplex of eIF-2B, which binds eIF2 and catalyzes guanine nucleotide exchange.


Pssm-ID: 100061 [Multi-domain]  Cd Length: 79  Bit Score: 40.25  E-value: 7.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042197645 131 GAYVDEGTMVdTWATVGSCAQIGKNVHLSGGVGIGGVleplqanptIIEDNC-----FIGARSEIVEGVIVEEGSVISMG 205
Cdd:cd05787     5 GTSIGEGTTI-KNSVIGRNCKIGKNVVIDNSYIWDDV---------TIEDGCtihhsIVADGAVIGKGCTIPPGSLISFG 74


                  ....*
gi 1042197645 206 VYIGQ 210
Cdd:cd05787    75 VVIGD 79
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 103-208 9.66e-05

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 43.21  E-value: 9.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042197645 103 VRVVPPAVARKGSYIAKGailmpsyVNIGAYV-------DEGTMVDTWATVGScAQIGKNVHLSGGVgIGGVLEPLQANP 175
Cdd:PRK14357  313 VSVGPFSRLREGTVLKKS-------VKIGNFVeikkstiGENTKAQHLTYLGD-ATVGKNVNIGAGT-ITCNYDGKKKNP 383

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1042197645 176 TIIEDNCFIGARSEIVEGVIVEEGSVISMGVYI 208
Cdd:PRK14357  384 TFIEDGAFIGSNSSLVAPVRIGKGALIGAGSVI 416
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 102-205 4.04e-04

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 41.36  E-value: 4.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042197645 102 GVRVVPPAVARKGSYIAKGailmpsyVNIG-------AYVDEGTMVDTWATVGScAQIGKNVHLSGG---VGIGGVlepl 171
Cdd:PRK14354  322 NVTVGPFAHLRPGSVIGEE-------VKIGnfveikkSTIGEGTKVSHLTYIGD-AEVGENVNIGCGtitVNYDGK---- 389

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1042197645 172 QANPTIIEDNCFIGARSEIVEGVIVEEGSVISMG 205
Cdd:PRK14354  390 NKFKTIIGDNAFIGCNSNLVAPVTVGDNAYIAAG 423
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 177-214 9.85e-04

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 40.12  E-value: 9.85e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1042197645 177 IIEDNCFIGARSEIVEGVIVEEGSVISMGVYIGQSTKI 214
Cdd:PRK00892  114 KIGEGVSIGPNAVIGAGVVIGDGVVIGAGAVIGDGVKI 151
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 100-237 9.90e-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: 39.31  E-value: 9.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042197645 100 KAGVRVVPPAVARKGSYIAKGAILMPSyVNIGAYV--DEGTMVDTWATVGSCAQIGKNVHLSGGVGIG----------GV 167
Cdd:cd03352     5 GENVSIGPNAVIGEGVVIGDGVVIGPG-VVIGDGVviGDDCVIHPNVTIYEGCIIGDRVIIHSGAVIGsdgfgfapdgGG 83

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1042197645 168 LEPL-QANPTIIEDNCFIGARSEIVEGV----IVEEGSVISMGVYIGQSTKIldretGEISygrIPAGSVVVSGS 237
Cdd:cd03352    84 WVKIpQLGGVIIGDDVEIGANTTIDRGAlgdtVIGDGTKIDNLVQIAHNVRI-----GENC---LIAAQVGIAGS 150
PRK10502 PRK10502
putative acyl transferase; Provisional
 114-205 1.05e-03

putative acyl transferase; Provisional


Pssm-ID: 236703 [Multi-domain]  Cd Length: 182  Bit Score: 39.16  E-value: 1.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042197645 114 GSYIAKGAILMPS-------YVNIGAY--VDEGTMVDTWATVgscaQIGKNVHLSGGV----GIGGVLEP---LQANPTI 177
Cdd:PRK10502   51 GAKIGKGVVIRPSvritypwKLTIGDYawIGDDVWLYNLGEI----TIGAHCVISQKSylctGSHDYSDPhfdLNTAPIV 126

                          90       100
                  ....*....|....*....|....*...
gi 1042197645 178 IEDNCFIGARSEIVEGVIVEEGSVISMG 205
Cdd:PRK10502  127 IGEGCWLAADVFVAPGVTIGSGAVVGAR 154
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 136-202 1.74e-03

N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix (LbH) acetyltransferase domain: GlmU is also known as UDP-N-acetylglucosamine pyrophosphorylase. It is a bifunctional bacterial enzyme that catalyzes two consecutive steps in the formation of UDP-N-acetylglucosamine (UDP-GlcNAc), an important precursor in bacterial cell wall formation. The two enzymatic activities, uridyltransferase and acetyltransferase, are carried out by two independent domains. The C-terminal LbH domain possesses the acetyltransferase activity. It catalyzes the CoA-dependent acetylation of GlcN-1-phosphate to GlcNAc-1-phosphate. The LbH domain contains 10 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X. The acetyltransferase active site is located at the interface between two subunits of the active LbH trimer.


Pssm-ID: 100044 [Multi-domain]  Cd Length: 193  Bit Score: 38.56  E-value: 1.74e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042197645 136 EGTMVDTWATVGSCAQIGKNVHLSGGVGIGG--VLEP-LQANPTIIEDNCFIGARSeIVEGVIVEEGSVI 202
Cdd:cd03353     8 ETTYIDGDVEIGVDVVIDPGVILEGKTVIGEdcVIGPnCVIKDSTIGDGVVIKASS-VIEGAVIGNGATV 76
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 144-214 1.91e-03

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: 38.54  E-value: 1.91e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1042197645 144 ATVGSCAQIGKNVHLSGGVGIG-GVLepLQANpTIIEDNCFIGARSEIVEGVIVEEGSVISMGVYIGQSTKI 214
Cdd:cd03352     2 AKIGENVSIGPNAVIGEGVVIGdGVV--IGPG-VVIGDGVVIGDDCVIHPNVTIYEGCIIGDRVIIHSGAVI 70
PLN02296 PLN02296
carbonate dehydratase
 146-229 2.36e-03

carbonate dehydratase


Pssm-ID: 215167 [Multi-domain]  Cd Length: 269  Bit Score: 38.57  E-value: 2.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042197645 146 VGSCAQIGKN--VHLsGGVGIGGVLEP--LQANPTI----------IEDNCFIGARSEIVEGVIVEEGSVISMGVYIGQS 211
Cdd:PLN02296   94 VGSGTNIQDNslVHV-AKTNLSGKVLPtiIGDNVTIghsavlhgctVEDEAFVGMGATLLDGVVVEKHAMVAAGALVRQN 172

                          90
                  ....*....|....*...
gi 1042197645 212 TKIldrETGEIsYGRIPA 229
Cdd:PLN02296  173 TRI---PSGEV-WAGNPA 186
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 144-217 2.51e-03

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 38.58  E-value: 2.51e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1042197645 144 ATVGSCAQIGKNVHLSGGVGIG-GVleplqanptIIEDNCFIGARSEIVEGVIVEEGSVISMGVYIGQSTKILDR 217
Cdd:PRK00892  107 AVIDPSAKIGEGVSIGPNAVIGaGV---------VIGDGVVIGAGAVIGDGVKIGADCRLHANVTIYHAVRIGNR 172
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 100-205 2.75e-03

N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix (LbH) acetyltransferase domain: GlmU is also known as UDP-N-acetylglucosamine pyrophosphorylase. It is a bifunctional bacterial enzyme that catalyzes two consecutive steps in the formation of UDP-N-acetylglucosamine (UDP-GlcNAc), an important precursor in bacterial cell wall formation. The two enzymatic activities, uridyltransferase and acetyltransferase, are carried out by two independent domains. The C-terminal LbH domain possesses the acetyltransferase activity. It catalyzes the CoA-dependent acetylation of GlcN-1-phosphate to GlcNAc-1-phosphate. The LbH domain contains 10 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X. The acetyltransferase active site is located at the interface between two subunits of the active LbH trimer.


Pssm-ID: 100044 [Multi-domain]  Cd Length: 193  Bit Score: 37.78  E-value: 2.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042197645 100 KAGVRVVPPAVARKGSYIAKGailmpsyVNIGAYV-------DEGTMVDTWATVGScAQIGKNVHlsggVGIG------- 165
Cdd:cd03353    71 GNGATVGPFAHLRPGTVLGEG-------VHIGNFVeikkstiGEGSKANHLSYLGD-AEIGEGVN----IGAGtitcnyd 138

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1042197645 166 GVleplQANPTIIEDNCFIGARSEIVEGVIVEEGSVISMG 205
Cdd:cd03353   139 GV----NKHRTVIGDNVFIGSNSQLVAPVTIGDGATIAAG 174
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
175-202 2.83e-03

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 34.62  E-value: 2.83e-03
                          10        20
                  ....*....|....*....|....*...
gi 1042197645 175 PTIIEDNCFIGARSEIVEGVIVEEGSVI 202
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVII 28
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 144-245 4.70e-03

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: 37.69  E-value: 4.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042197645 144 ATVGSCAQIGKNVHLSGGVGIG-GVleplqanptIIEDNCFIGARSEIVEGVIVEEGSVISMGVYIGQSTKILDRetgei 222
Cdd:COG1044   103 AVIDPSAKIGEGVSIGPFAVIGaGV---------VIGDGVVIGPGVVIGDGVVIGDDCVLHPNVTIYERCVIGDR----- 168

                          90       100
                  ....*....|....*....|....*.
gi 1042197645 223 syGRIPAGSVVVS---GSLPSKDGSH 245
Cdd:COG1044   169 --VIIHSGAVIGAdgfGFAPDEDGGW 192
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 130-234 4.79e-03

Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function prediction only];


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 36.93  E-value: 4.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042197645 130 IGAY--VDEGTMVDTwaTVGSCAQIGKNVHLSGGVGIGGVleplqanptIIEDNCFIGARSEIVEGVIVEEGSVISMGVY 207
Cdd:COG0663    52 IGEGsnIQDGVVLHV--DPGYPLTIGDDVTIGHGAILHGC---------TIGDNVLIGMGAIVLDGAVIGDGSIVGAGAL 120

                          90       100
                  ....*....|....*....|....*..
gi 1042197645 208 IGQSTkildretgeisygRIPAGSVVV 234
Cdd:COG0663   121 VTEGK-------------VVPPGSLVV 134
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 150-217 4.82e-03

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: 37.39  E-value: 4.82e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1042197645 150 AQIGKNVHLSGGVGIGgvleplqaNPTIIEDNCFIGARSEIVEGVIVEEGSVISMGVYIGQSTKILDR 217
Cdd:cd03352     2 AKIGENVSIGPNAVIG--------EGVVIGDGVVIGPGVVIGDGVVIGDDCVIHPNVTIYEGCIIGDR 61
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
 152-234 6.44e-03

Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT catalyze the CoA-dependent acetylation of the 6-hydroxyl group of their respective sugar substrates. MAT acetylates maltose and glucose exclusively at the C6 position of the nonreducing end glucosyl moiety. GAT specifically acetylates galactopyranosides. Furthermore, MAT shows higher affinity toward artificial substrates containing an alkyl or hydrophobic chain as well as a glucosyl unit. Active MAT and GAT are homotrimers, with each subunit consisting of an N-terminal alpha-helical region and a C-terminal left-handed parallel alpha-helix (LbH) subdomain with 6 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X).


Pssm-ID: 100047 [Multi-domain]  Cd Length: 169  Bit Score: 36.63  E-value: 6.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042197645 152 IGKNVHLSGGVGIGGVLEPL----------QANPTIIEDNCFIGARSEIVEGVIVEEGSVISMG--VyigqsTKilDret 219
Cdd:cd03357    85 IGDNVLIGPNVQIYTAGHPLdpeernrgleYAKPITIGDNVWIGGGVIILPGVTIGDNSVIGAGsvV-----TK--D--- 154

                          90
                  ....*....|....*
gi 1042197645 220 geisygrIPAGSVVV 234
Cdd:cd03357   155 -------IPANVVAA 162
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 178-234 7.23e-03

Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), Ferripyochelin Binding Protein (FBP), E. coli paaY protein, and similar proteins. CAs are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism, involving the nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three evolutionary distinct groups - alpha, beta and gamma carbonic anhydrases - which show no significant sequence identity or structural similarity. Gamma CAs are trimeric enzymes with left-handed parallel beta helix (LbH) structural domain.


Pssm-ID: 100051 [Multi-domain]  Cd Length: 153  Bit Score: 36.24  E-value: 7.23e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1042197645 178 IEDNCFIGARSEIVEGVIVEEGSVISMGVYIGQSTkildretgeisygRIPAGSVVV 234
Cdd:cd04645    80 IGDNCLIGMGAIILDGAVIGKGSIVAAGSLVPPGK-------------VIPPGSLVA 123
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 126-205 8.09e-03

WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of Xanthomonas campestris WcxM and proteins with similarity to the WcxM N-terminal domain. WcxM is thought to be bifunctional, catalyzing both the isomerization and transacetylation reactions of keto-hexoses. It contains an N-terminal LbH domain responsible for the transacetylation function and a C-terminal isomerase domain. The LbH domain contains imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), typical of enzymes with acyltransferase activity.


Pssm-ID: 100048 [Multi-domain]  Cd Length: 119  Bit Score: 35.55  E-value: 8.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042197645 126 SYVNIGAyvdeGTMVDTWATVGSCAQIGKNVHLSGGVGIG-------------------GVLEPLQANPTIIEDNCFIGA 186
Cdd:cd03358     3 DNCIIGT----NVFIENDVKIGDNVKIQSNVSIYEGVTIEddvfigpnvvftndlyprsKIYRKWELKGTTVKRGASIGA 78

                          90
                  ....*....|....*....
gi 1042197645 187 RSEIVEGVIVEEGSVISMG 205
Cdd:cd03358    79 NATILPGVTIGEYALVGAG 97
glmU PRK09451
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 101-228 8.31e-03

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;


Pssm-ID: 181867 [Multi-domain]  Cd Length: 456  Bit Score: 37.31  E-value: 8.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042197645 101 AGVRVVPPAVARKGSYIAKGAiLMPSYVNI-GAYVDEGTMVDTWATVGScAQIGKNVHLSGGV------GiggvleplqA 173
Cdd:PRK09451  322 AACTIGPFARLRPGAELAEGA-HVGNFVEMkKARLGKGSKAGHLTYLGD-AEIGDNVNIGAGTitcnydG---------A 390

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1042197645 174 NP--TIIEDNCFIGARSEIVEGVIVEEGSVISMGvyigqSTKILDRETGEISYGRIP 228
Cdd:PRK09451  391 NKfkTIIGDDVFVGSDTQLVAPVTVGKGATIGAG-----TTVTRDVAENELVISRVP 442
 
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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