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Conserved domains on  [gi|504427681|ref|WP_014614783|]
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pyridoxal 5'-phosphate synthase glutaminase subunit PdxT [Staphylococcus pseudintermedius]

Protein Classification

pyridoxal 5'-phosphate synthase glutaminase subunit PdxT( domain architecture ID 10014274)

pyridoxal 5'-phosphate synthase glutaminase subunit PdxT catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the biosynthesis of pyridoxal 5'-phosphate

CATH:  3.40.50.880
EC:  4.3.3.6|3.5.1.2
Gene Ontology:  GO:0004359|GO:0036381|GO:0042823|GO:0006543
PubMed:  10387030
SCOP:  3001405

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK13525 PRK13525
pyridoxal 5'-phosphate synthase glutaminase subunit PdxT;
1-182 1.36e-112

pyridoxal 5'-phosphate synthase glutaminase subunit PdxT;


:

Pssm-ID: 237411 [Multi-domain]  Cd Length: 189  Bit Score: 318.26  E-value: 1.36e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427681   1 MKIGVLALQGAVREHIRHIELAGHEGVAIKKVEQLEEIDGLIIPGGESTTLRRLMNLYGFKEALR---ASQLPMFGTCAG 77
Cdd:PRK13525   2 MKIGVLALQGAVREHLAALEALGAEAVEVRRPEDLDEIDGLILPGGESTTMGKLLRDFGLLEPLRefiASGLPVFGTCAG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427681  78 LIVLAKDIVG-EEGYLQKLDITVERNSFGRQVDSFESELHIKGIDQPIEGVFIRAPHIQSTEAAVDVLGTIDDKIIAVQQ 156
Cdd:PRK13525  82 MILLAKEIEGyEQEHLGLLDITVRRNAFGRQVDSFEAELDIKGLGEPFPAVFIRAPYIEEVGPGVEVLATVGGRIVAVRQ 161

                        170       180
                 ....*....|....*....|....*.
gi 504427681 157 GRYLGVSFHPELTDDYRMTQYFIEHV 182
Cdd:PRK13525 162 GNILATSFHPELTDDTRVHRYFLEMV 187
 
Name Accession Description Interval E-value
PRK13525 PRK13525
pyridoxal 5'-phosphate synthase glutaminase subunit PdxT;
1-182 1.36e-112

pyridoxal 5'-phosphate synthase glutaminase subunit PdxT;


Pssm-ID: 237411 [Multi-domain]  Cd Length: 189  Bit Score: 318.26  E-value: 1.36e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427681   1 MKIGVLALQGAVREHIRHIELAGHEGVAIKKVEQLEEIDGLIIPGGESTTLRRLMNLYGFKEALR---ASQLPMFGTCAG 77
Cdd:PRK13525   2 MKIGVLALQGAVREHLAALEALGAEAVEVRRPEDLDEIDGLILPGGESTTMGKLLRDFGLLEPLRefiASGLPVFGTCAG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427681  78 LIVLAKDIVG-EEGYLQKLDITVERNSFGRQVDSFESELHIKGIDQPIEGVFIRAPHIQSTEAAVDVLGTIDDKIIAVQQ 156
Cdd:PRK13525  82 MILLAKEIEGyEQEHLGLLDITVRRNAFGRQVDSFEAELDIKGLGEPFPAVFIRAPYIEEVGPGVEVLATVGGRIVAVRQ 161

                        170       180
                 ....*....|....*....|....*.
gi 504427681 157 GRYLGVSFHPELTDDYRMTQYFIEHV 182
Cdd:PRK13525 162 GNILATSFHPELTDDTRVHRYFLEMV 187
PdxT COG0311
Pyridoxal 5'-phosphate synthase subunit PdxT (glutamine amidotransferase) [Coenzyme transport ...
 1-182 1.03e-99

Pyridoxal 5'-phosphate synthase subunit PdxT (glutamine amidotransferase) [Coenzyme transport and metabolism]; Pyridoxal 5'-phosphate synthase subunit PdxT (glutamine amidotransferase) is part of the Pathway/BioSystem: Pyridoxal phosphate biosynthesis


Pssm-ID: 440080 [Multi-domain]  Cd Length: 191  Bit Score: 285.80  E-value: 1.03e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427681   1 MKIGVLALQGAVREHIRHIELAGHEGVAIKKVEQLEEIDGLIIPGGESTTLRRLMNLYGFKEALR---ASQLPMFGTCAG 77
Cdd:COG0311    1 MKIGVLALQGDVREHIRALERLGAEVVEVRRPEDLEGLDGLIIPGGESTTIGKLLRRFGLLEPLReriAAGLPVFGTCAG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427681  78 LIVLAKDIVGEEG-YLQKLDITVERNSFGRQVDSFESELHIKGI-DQPIEGVFIRAPHIQSTEAAVDVLGTIDDKIIAVQ 155
Cdd:COG0311   81 LILLAKEIEDPDQpTLGLLDITVRRNAFGRQVDSFEADLDIPGLgDGPFPAVFIRAPYIEEVGPGVEVLATVDGRIVAVR 160

                        170       180
                 ....*....|....*....|....*..
gi 504427681 156 QGRYLGVSFHPELTDDYRMTQYFIEHV 182
Cdd:COG0311  161 QGNILATSFHPELTDDLRVHEYFLEMV 187
PLP_synth_Pdx2 TIGR03800
pyridoxal 5'-phosphate synthase, glutaminase subunit Pdx2; Pyridoxal 5'-phosphate (PLP) is ...
 2-180 1.87e-96

pyridoxal 5'-phosphate synthase, glutaminase subunit Pdx2; Pyridoxal 5'-phosphate (PLP) is synthesized by the PdxA/PdxJ pathway in some species (mostly within the gamma subdivision of the proteobacteria) and by the Pdx1/Pdx2 pathway in most other organisms. This family describes Pdx2, the glutaminase subunit of the PLP synthase. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridoxine]


Pssm-ID: 274792 [Multi-domain]  Cd Length: 184  Bit Score: 277.39  E-value: 1.87e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427681    2 KIGVLALQGAVREHIRHIELAGHEGVAIKKVEQLEEIDGLIIPGGESTTLRRLMNLYGFKEALRA---SQLPMFGTCAGL 78
Cdd:TIGR03800   1 KIGVLALQGAVREHARALEALGVEGVEVKRPEQLDEIDGLIIPGGESTTISRLLDKYGMFEPLRNfilSGLPVFGTCAGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427681   79 IVLAKDIVG-EEGYLQKLDITVERNSFGRQVDSFESELHIKGI-DQPIEGVFIRAPHIQSTEAAVDVLGTIDDKIIAVQQ 156
Cdd:TIGR03800  81 IMLAKEIIGqKEGQLGLLDMTVERNAYGRQVDSFEAEVDIKGVgDDPITGVFIRAPKIVSVGNGVEILAKVGNRIVAVRQ 160

                         170       180
                  ....*....|....*....|....
gi 504427681  157 GRYLGVSFHPELTDDYRMTQYFIE 180
Cdd:TIGR03800 161 GNILVSSFHPELTDDHRVHEYFLE 184
GATase1_PB cd01749
Glutamine Amidotransferase (GATase_I) involved in pyridoxine biosynthesis; Glutamine ...
 3-179 1.66e-93

Glutamine Amidotransferase (GATase_I) involved in pyridoxine biosynthesis; Glutamine Amidotransferase (GATase_I) involved in pyridoxine biosynthesis. Glutamine amidotransferase (GATase) activity involves the removal of the ammonia group from a glutamate molecule and its subsequent transfer to a specific substrate, thus creating a new carbon-nitrogen group on the substrate. This group contains proteins like Bacillus subtilus YaaE and Plasmodium falciparum Pdx2 which are members of the triad glutamine aminotransferase family and function in a pathway for the biosynthesis of vitamin B6.


Pssm-ID: 153220 [Multi-domain]  Cd Length: 183  Bit Score: 269.78  E-value: 1.66e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427681   3 IGVLALQGAVREHIRHIELAGHEGVAIKKVEQLEEIDGLIIPGGESTTLRRLMNLYGFKEALR---ASQLPMFGTCAGLI 79
Cdd:cd01749    1 IGVLALQGDFREHIRALERLGVEVIEVRTPEDLEGIDGLIIPGGESTTIGKLLRRTGLLDPLRefiRAGKPVFGTCAGLI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427681  80 VLAKDIVGEEG--YLQKLDITVERNSFGRQVDSFESELHIKGIDQ-PIEGVFIRAPHIQSTEAAVDVLGTIDDKIIAVQQ 156
Cdd:cd01749   81 LLAKEVEDQGGqpLLGLLDITVRRNAFGRQVDSFEADLDIPGLGLgPFPAVFIRAPVIEEVGPGVEVLAEYDGKIVAVRQ 160

                        170       180
                 ....*....|....*....|...
gi 504427681 157 GRYLGVSFHPELTDDYRMTQYFI 179
Cdd:cd01749  161 GNVLATSFHPELTDDTRIHEYFL 183
SNO pfam01174
SNO glutamine amidotransferase family; This family and its amidotransferase domain was first ...
 5-182 2.60e-72

SNO glutamine amidotransferase family; This family and its amidotransferase domain was first described in. It is predicted that members of this family are involved in the pyridoxine biosynthetic pathway, based on the proximity and co-regulation of the corresponding genes and physical interaction between the members of pfam01174 and pfam01680.


Pssm-ID: 334414 [Multi-domain]  Cd Length: 188  Bit Score: 216.24  E-value: 2.60e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427681    5 VLALQGAVREHIRHIELAGHEGVAIKKVEQLEEIDGLIIPGGESTTLRRLMNLYGFKEALRA----SQLPMFGTCAGLIV 80
Cdd:pfam01174   1 VLALQGAVEEHEEAIKKCGAENKTVKRPEDLAQCDALIIPGGESTAMSLLAKRYGFYEPLYEfvhnPNKPIWGTCAGLIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427681   81 LAKDIVGEE-GYLQKLDITVERNSFGRQVDSFESELHIKGIDQPIEGVFIRAPHIQS--TEAAVDVLGTIDDKIIAVQQG 157
Cdd:pfam01174  81 LSKQLGNELvKTLGLLKVTVKRNAFGRQVDSFEKECDFKNLIPKFPGVFIRAPVIEEilDPEVVVVLYELDGKIVVAKQG 160

                         170       180
                  ....*....|....*....|....*.
gi 504427681  158 RYLGVSFHPELT-DDYRMTQYFIEHV 182
Cdd:pfam01174 161 NILATSFHPELAeDDYRVHDWFVENF 186
 
Name Accession Description Interval E-value
PRK13525 PRK13525
pyridoxal 5'-phosphate synthase glutaminase subunit PdxT;
1-182 1.36e-112

pyridoxal 5'-phosphate synthase glutaminase subunit PdxT;


Pssm-ID: 237411 [Multi-domain]  Cd Length: 189  Bit Score: 318.26  E-value: 1.36e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427681   1 MKIGVLALQGAVREHIRHIELAGHEGVAIKKVEQLEEIDGLIIPGGESTTLRRLMNLYGFKEALR---ASQLPMFGTCAG 77
Cdd:PRK13525   2 MKIGVLALQGAVREHLAALEALGAEAVEVRRPEDLDEIDGLILPGGESTTMGKLLRDFGLLEPLRefiASGLPVFGTCAG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427681  78 LIVLAKDIVG-EEGYLQKLDITVERNSFGRQVDSFESELHIKGIDQPIEGVFIRAPHIQSTEAAVDVLGTIDDKIIAVQQ 156
Cdd:PRK13525  82 MILLAKEIEGyEQEHLGLLDITVRRNAFGRQVDSFEAELDIKGLGEPFPAVFIRAPYIEEVGPGVEVLATVGGRIVAVRQ 161

                        170       180
                 ....*....|....*....|....*.
gi 504427681 157 GRYLGVSFHPELTDDYRMTQYFIEHV 182
Cdd:PRK13525 162 GNILATSFHPELTDDTRVHRYFLEMV 187
PdxT COG0311
Pyridoxal 5'-phosphate synthase subunit PdxT (glutamine amidotransferase) [Coenzyme transport ...
 1-182 1.03e-99

Pyridoxal 5'-phosphate synthase subunit PdxT (glutamine amidotransferase) [Coenzyme transport and metabolism]; Pyridoxal 5'-phosphate synthase subunit PdxT (glutamine amidotransferase) is part of the Pathway/BioSystem: Pyridoxal phosphate biosynthesis


Pssm-ID: 440080 [Multi-domain]  Cd Length: 191  Bit Score: 285.80  E-value: 1.03e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427681   1 MKIGVLALQGAVREHIRHIELAGHEGVAIKKVEQLEEIDGLIIPGGESTTLRRLMNLYGFKEALR---ASQLPMFGTCAG 77
Cdd:COG0311    1 MKIGVLALQGDVREHIRALERLGAEVVEVRRPEDLEGLDGLIIPGGESTTIGKLLRRFGLLEPLReriAAGLPVFGTCAG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427681  78 LIVLAKDIVGEEG-YLQKLDITVERNSFGRQVDSFESELHIKGI-DQPIEGVFIRAPHIQSTEAAVDVLGTIDDKIIAVQ 155
Cdd:COG0311   81 LILLAKEIEDPDQpTLGLLDITVRRNAFGRQVDSFEADLDIPGLgDGPFPAVFIRAPYIEEVGPGVEVLATVDGRIVAVR 160

                        170       180
                 ....*....|....*....|....*..
gi 504427681 156 QGRYLGVSFHPELTDDYRMTQYFIEHV 182
Cdd:COG0311  161 QGNILATSFHPELTDDLRVHEYFLEMV 187
PLP_synth_Pdx2 TIGR03800
pyridoxal 5'-phosphate synthase, glutaminase subunit Pdx2; Pyridoxal 5'-phosphate (PLP) is ...
 2-180 1.87e-96

pyridoxal 5'-phosphate synthase, glutaminase subunit Pdx2; Pyridoxal 5'-phosphate (PLP) is synthesized by the PdxA/PdxJ pathway in some species (mostly within the gamma subdivision of the proteobacteria) and by the Pdx1/Pdx2 pathway in most other organisms. This family describes Pdx2, the glutaminase subunit of the PLP synthase. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridoxine]


Pssm-ID: 274792 [Multi-domain]  Cd Length: 184  Bit Score: 277.39  E-value: 1.87e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427681    2 KIGVLALQGAVREHIRHIELAGHEGVAIKKVEQLEEIDGLIIPGGESTTLRRLMNLYGFKEALRA---SQLPMFGTCAGL 78
Cdd:TIGR03800   1 KIGVLALQGAVREHARALEALGVEGVEVKRPEQLDEIDGLIIPGGESTTISRLLDKYGMFEPLRNfilSGLPVFGTCAGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427681   79 IVLAKDIVG-EEGYLQKLDITVERNSFGRQVDSFESELHIKGI-DQPIEGVFIRAPHIQSTEAAVDVLGTIDDKIIAVQQ 156
Cdd:TIGR03800  81 IMLAKEIIGqKEGQLGLLDMTVERNAYGRQVDSFEAEVDIKGVgDDPITGVFIRAPKIVSVGNGVEILAKVGNRIVAVRQ 160

                         170       180
                  ....*....|....*....|....
gi 504427681  157 GRYLGVSFHPELTDDYRMTQYFIE 180
Cdd:TIGR03800 161 GNILVSSFHPELTDDHRVHEYFLE 184
GATase1_PB cd01749
Glutamine Amidotransferase (GATase_I) involved in pyridoxine biosynthesis; Glutamine ...
 3-179 1.66e-93

Glutamine Amidotransferase (GATase_I) involved in pyridoxine biosynthesis; Glutamine Amidotransferase (GATase_I) involved in pyridoxine biosynthesis. Glutamine amidotransferase (GATase) activity involves the removal of the ammonia group from a glutamate molecule and its subsequent transfer to a specific substrate, thus creating a new carbon-nitrogen group on the substrate. This group contains proteins like Bacillus subtilus YaaE and Plasmodium falciparum Pdx2 which are members of the triad glutamine aminotransferase family and function in a pathway for the biosynthesis of vitamin B6.


Pssm-ID: 153220 [Multi-domain]  Cd Length: 183  Bit Score: 269.78  E-value: 1.66e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427681   3 IGVLALQGAVREHIRHIELAGHEGVAIKKVEQLEEIDGLIIPGGESTTLRRLMNLYGFKEALR---ASQLPMFGTCAGLI 79
Cdd:cd01749    1 IGVLALQGDFREHIRALERLGVEVIEVRTPEDLEGIDGLIIPGGESTTIGKLLRRTGLLDPLRefiRAGKPVFGTCAGLI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427681  80 VLAKDIVGEEG--YLQKLDITVERNSFGRQVDSFESELHIKGIDQ-PIEGVFIRAPHIQSTEAAVDVLGTIDDKIIAVQQ 156
Cdd:cd01749   81 LLAKEVEDQGGqpLLGLLDITVRRNAFGRQVDSFEADLDIPGLGLgPFPAVFIRAPVIEEVGPGVEVLAEYDGKIVAVRQ 160

                        170       180
                 ....*....|....*....|...
gi 504427681 157 GRYLGVSFHPELTDDYRMTQYFI 179
Cdd:cd01749  161 GNVLATSFHPELTDDTRIHEYFL 183
PRK13527 PRK13527
glutamine amidotransferase subunit PdxT; Provisional
 1-183 1.52e-82

glutamine amidotransferase subunit PdxT; Provisional


Pssm-ID: 237412 [Multi-domain]  Cd Length: 200  Bit Score: 242.48  E-value: 1.52e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427681   1 MKIGVLALQGAVREHIRHIELA------GHEGVAIKKVEQLEEIDGLIIPGGESTTLRRLMNLYGFKEALR---ASQLPM 71
Cdd:PRK13527   1 MKIGVLALQGDVEEHIDALKRAldelgiDGEVVEVRRPGDLPDCDALIIPGGESTTIGRLMKREGILDEIKekiEEGLPI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427681  72 FGTCAGLIVLAKDIVGE--EGYLQKL----DITVERNSFGRQVDSFESELHIKGIDQPIEGVFIRAPHIQSTEAAVDVLG 145
Cdd:PRK13527  81 LGTCAGLILLAKEVGDDrvTKTEQPLlglmDVTVKRNAFGRQRDSFEAEIDLSGLDGPFHAVFIRAPAITKVGGDVEVLA 160

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 504427681 146 TIDDKIIAVQQGRYLGVSFHPELTDDYRMTQYFIEHVM 183
Cdd:PRK13527 161 KLDDRIVAVEQGNVLATAFHPELTDDTRIHEYFLKKVK 198
SNO pfam01174
SNO glutamine amidotransferase family; This family and its amidotransferase domain was first ...
 5-182 2.60e-72

SNO glutamine amidotransferase family; This family and its amidotransferase domain was first described in. It is predicted that members of this family are involved in the pyridoxine biosynthetic pathway, based on the proximity and co-regulation of the corresponding genes and physical interaction between the members of pfam01174 and pfam01680.


Pssm-ID: 334414 [Multi-domain]  Cd Length: 188  Bit Score: 216.24  E-value: 2.60e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427681    5 VLALQGAVREHIRHIELAGHEGVAIKKVEQLEEIDGLIIPGGESTTLRRLMNLYGFKEALRA----SQLPMFGTCAGLIV 80
Cdd:pfam01174   1 VLALQGAVEEHEEAIKKCGAENKTVKRPEDLAQCDALIIPGGESTAMSLLAKRYGFYEPLYEfvhnPNKPIWGTCAGLIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427681   81 LAKDIVGEE-GYLQKLDITVERNSFGRQVDSFESELHIKGIDQPIEGVFIRAPHIQS--TEAAVDVLGTIDDKIIAVQQG 157
Cdd:pfam01174  81 LSKQLGNELvKTLGLLKVTVKRNAFGRQVDSFEKECDFKNLIPKFPGVFIRAPVIEEilDPEVVVVLYELDGKIVVAKQG 160

                         170       180
                  ....*....|....*....|....*.
gi 504427681  158 RYLGVSFHPELT-DDYRMTQYFIEHV 182
Cdd:pfam01174 161 NILATSFHPELAeDDYRVHDWFVENF 186
PLN02832 PLN02832
glutamine amidotransferase subunit of pyridoxal 5'-phosphate synthase complex
 1-180 2.71e-64

glutamine amidotransferase subunit of pyridoxal 5'-phosphate synthase complex


Pssm-ID: 215446 [Multi-domain]  Cd Length: 248  Bit Score: 198.01  E-value: 2.71e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427681   1 MKIGVLALQGAVREHIRHIELAGHEGVAIKKVEQLEEIDGLIIPGGESTTLRRLMNLYGFKEALR---ASQLPMFGTCAG 77
Cdd:PLN02832   2 MAIGVLALQGSFNEHIAALRRLGVEAVEVRKPEQLEGVSGLIIPGGESTTMAKLAERHNLFPALRefvKSGKPVWGTCAG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427681  78 LIVLAKDIVG-EEG---YLQKLDITVERNSFGRQVDSFESELHIK------GIDQPIEGVFIRAPHIQSTEAAVDVLG-- 145
Cdd:PLN02832  82 LIFLAERAVGqKEGgqeLLGGLDCTVHRNFFGSQINSFETELPVPelaaseGGPETFRAVFIRAPAILSVGPGVEVLAey 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 504427681 146 ----------------TIDDKIIAVQQGRYLGVSFHPELTDDYRMTQYFIE 180
Cdd:PLN02832 162 plpsekalyssstdaeGRDKVIVAVKQGNLLATAFHPELTADTRWHSYFVK 212
PRK13526 PRK13526
glutamine amidotransferase subunit PdxT; Provisional
 1-179 8.02e-48

glutamine amidotransferase subunit PdxT; Provisional


Pssm-ID: 184113 [Multi-domain]  Cd Length: 179  Bit Score: 153.95  E-value: 8.02e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427681   1 MKIGVLALQGAVREHIRHIELAGHEGVAIKKVEQLEEIDGLIIPGGESTTLRRLMNLYGFKEALR--ASQLPMFGTCAGL 78
Cdd:PRK13526   3 QKVGVLAIQGGYQKHADMFKSLGVEVKLVKFNNDFDSIDRLVIPGGESTTLLNLLNKHQIFDKLYnfCSSKPVFGTCAGS 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427681  79 IVLAKDivgeEGYLQKLDITVERNSFGRQVDSFESELHIkgIDQPIEGVFIRAPHIQSTEAAVDVLGTIDDKIIAVQQGR 158
Cdd:PRK13526  83 IILSKG----EGYLNLLDLEVQRNAYGRQVDSFVADISF--NDKNITGVFIRAPKFIVVGNQVDILSKYQNSPVLLRQAN 156

                        170       180
                 ....*....|....*....|.
gi 504427681 159 YLGVSFHPELTDDYRMTQYFI 179
Cdd:PRK13526 157 ILVSSFHPELTQDPTVHEYFL 177
GATase1_CobB cd03130
Type 1 glutamine amidotransferase (GATase1) domain found in Cobyrinic Acid a,c-Diamide ...
 13-90 1.80e-06

Type 1 glutamine amidotransferase (GATase1) domain found in Cobyrinic Acid a,c-Diamide Synthase; Type 1 glutamine amidotransferase (GATase1) domain found in Cobyrinic Acid a,c-Diamide Synthase. CobB plays a role in cobalamin biosythesis catalyzing the conversion of cobyrinic acid to cobyrinic acid a,c-diamide. CobB belongs to the triad family of amidotransferases. Two of the three residues of the catalytic triad that are involved in glutamine binding, hydrolysis and transfer of the resulting ammonia to the acceptor substrate in other triad aminodotransferases are conserved in CobB.


Pssm-ID: 153224 [Multi-domain]  Cd Length: 198  Bit Score: 46.05  E-value: 1.80e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427681  13 REHIRHIELAGHEGVAIKKV--EQLEEIDGLIIPGG--EsTTLRRLMNLYGFKEALR---ASQLPMFGTCAGLIVLAKDI 85
Cdd:cd03130   14 PENLELLEAAGAELVPFSPLkdEELPDADGLYLGGGypE-LFAEELSANQSMRESIRafaESGGPIYAECGGLMYLGESL 92


                 ....*
gi 504427681  86 VGEEG 90
Cdd:cd03130   93 DDEEG 97
GATase_3 pfam07685
CobB/CobQ-like glutamine amidotransferase domain;
5-90 2.77e-05

CobB/CobQ-like glutamine amidotransferase domain;


Pssm-ID: 429595 [Multi-domain]  Cd Length: 189  Bit Score: 42.61  E-value: 2.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427681    5 VLALQGAVREHIrhielaghegVAIKKVEQLEEIDGLIIPGGESTT-LRRLMNLYGFKEALRA---SQLPMFGTCAGLIV 80
Cdd:pfam07685  20 PLRYEPAVRVRF----------VPLPDESLGPDADLIILPGGKPTIqDLALLRNSGMDEAIKEaaeDGGPVLGICGGYQM 89

                          90
                  ....*....|
gi 504427681   81 LAKDIVGEEG 90
Cdd:pfam07685  90 LGETIEDPEG 99
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 11-81 8.16e-05

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


Pssm-ID: 153222 [Multi-domain]  Cd Length: 92  Bit Score: 39.88  E-value: 8.16e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504427681  11 AVREHIRHIELAGHEGVAIKKVEQLEEIDGLIIPGGESTTlRRLMNLYGFKEALR---ASQLPMFGTCAGLIVL 81
Cdd:cd03128   20 ALREAGAEVDVVSPDGGPVESDVDLDDYDGLILPGGPGTP-DDLAWDEALLALLReaaAAGKPVLGICLGAQLL 92
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 11-81 8.94e-05

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


Pssm-ID: 153210 [Multi-domain]  Cd Length: 115  Bit Score: 40.27  E-value: 8.94e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504427681  11 AVREHIRHIELAGHEGVAIKKVEQLEEIDGLIIPGGESTTlRRLMNLYGFKEALR---ASQLPMFGTCAGLIVL 81
Cdd:cd01653   20 ALREAGAEVDVVSPDGGPVESDVDLDDYDGLILPGGPGTP-DDLARDEALLALLReaaAAGKPILGICLGAQLL 92
PRK01077 PRK01077
cobyrinate a,c-diamide synthase;
33-90 7.81e-04

cobyrinate a,c-diamide synthase;


Pssm-ID: 234896 [Multi-domain]  Cd Length: 451  Bit Score: 39.35  E-value: 7.81e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504427681  33 EQLEEIDGLIIPGG--EsttL--RRLMNLYGFKEALR---ASQLPMFGTCAGLIVLAKDIVGEEG 90
Cdd:PRK01077 283 EALPDCDGLYLGGGypE---LfaAELAANTSMRASIRaaaAAGKPIYAECGGLMYLGESLEDADG 344
GATase1_CobQ cd01750
Type 1 glutamine amidotransferase (GATase1) domain found in Cobyric Acid Synthase (CobQ); Type ...
 21-90 2.29e-03

Type 1 glutamine amidotransferase (GATase1) domain found in Cobyric Acid Synthase (CobQ); Type 1 glutamine amidotransferase (GATase1) domain found in Cobyric Acid Synthase (CobQ). CobQ plays a role in cobalamin biosythesis. CobQ catalyses amidations at positions B, D, E, and G on adenosylcobyrinic A,C-diamide in the biosynthesis of cobalamin. CobQ belongs to the triad family of amidotransferases. Two of the three residues of the catalytic triad that are involved in glutamine binding, hydrolysis and transfer of the resulting ammonia to the acceptor substrate in other triad aminodotransferases are conserved in CobQ.


Pssm-ID: 153221 [Multi-domain]  Cd Length: 194  Bit Score: 37.23  E-value: 2.29e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504427681  21 LAGHEGVAIKKV---EQLEEIDGLIIPGGESTTLR-RLMNLYGFKEAL---RASQLPMFGTCAGLIVLAKDIVGEEG 90
Cdd:cd01750   18 LAREPGVDVRYVevpEGLGDADLIILPGSKDTIQDlAWLRKRGLAEAIknyARAGGPVLGICGGYQMLGKYIVDPEG 94
GATase1_PfpI_3 cd03140
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ...
 35-98 8.98e-03

Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins similar to PfpI from Pyrococcus furiosus; Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins similar to PfpI from Pyrococcus furiosus. PfpI is an ATP-independent intracellular proteases which may hydrolyze small peptides to provide a nutritional source. Only Cys of the catalytic triad typical of GATase1 domains is conserved in this group. This Cys residue is found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow.


Pssm-ID: 153234 [Multi-domain]  Cd Length: 170  Bit Score: 35.27  E-value: 8.98e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504427681  35 LEEIDGLIIPGGESTTLRRLMNLYGFKEALRASQLPMFGTCAGLIVLAKdivgeEGYLQKLDIT 98
Cdd:cd03140   58 PEDYDLLILPGGDSWDNPEAPDLAGLVRQALKQGKPVAAICGATLALAR-----AGLLNNRKHT 116
 
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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