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Conserved domains on  [gi|446613093|ref|WP_000690439|]
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MULTISPECIES: pyridoxal 5'-phosphate synthase glutaminase subunit PdxT [Bacteria]

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;
1-184 2.97e-114

pyridoxal 5'-phosphate synthase glutaminase subunit PdxT;


:

Pssm-ID: 237411 [Multi-domain]  Cd Length: 189  Bit Score: 322.49  E-value: 2.97e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613093   1 MKIGVLALQGAVREHIRHIELSGHEGIAVKKVEQLEEIEGLILPGGESTTLRRLMNLYGFKEALQN---STLPMFGTCAG 77
Cdd:PRK13525   2 MKIGVLALQGAVREHLAALEALGAEAVEVRRPEDLDEIDGLILPGGESTTMGKLLRDFGLLEPLREfiaSGLPVFGTCAG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613093  78 LIVLAQDIVG-EEGYLNKLNITVQRNSFGRQVDSFETELDIKGIATDIEGVFIRAPHIEKVGQGVDILCKVNEKIVAVQQ 156
Cdd:PRK13525  82 MILLAKEIEGyEQEHLGLLDITVRRNAFGRQVDSFEAELDIKGLGEPFPAVFIRAPYIEEVGPGVEVLATVGGRIVAVRQ 161

                        170       180
                 ....*....|....*....|....*...
gi 446613093 157 GKYLGVSFHPELTDDYRVTDYFINHIVK 184
Cdd:PRK13525 162 GNILATSFHPELTDDTRVHRYFLEMVKE 189
 
Name Accession Description Interval E-value
PRK13525 PRK13525
pyridoxal 5'-phosphate synthase glutaminase subunit PdxT;
1-184 2.97e-114

pyridoxal 5'-phosphate synthase glutaminase subunit PdxT;


Pssm-ID: 237411 [Multi-domain]  Cd Length: 189  Bit Score: 322.49  E-value: 2.97e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613093   1 MKIGVLALQGAVREHIRHIELSGHEGIAVKKVEQLEEIEGLILPGGESTTLRRLMNLYGFKEALQN---STLPMFGTCAG 77
Cdd:PRK13525   2 MKIGVLALQGAVREHLAALEALGAEAVEVRRPEDLDEIDGLILPGGESTTMGKLLRDFGLLEPLREfiaSGLPVFGTCAG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613093  78 LIVLAQDIVG-EEGYLNKLNITVQRNSFGRQVDSFETELDIKGIATDIEGVFIRAPHIEKVGQGVDILCKVNEKIVAVQQ 156
Cdd:PRK13525  82 MILLAKEIEGyEQEHLGLLDITVRRNAFGRQVDSFEAELDIKGLGEPFPAVFIRAPYIEEVGPGVEVLATVGGRIVAVRQ 161

                        170       180
                 ....*....|....*....|....*...
gi 446613093 157 GKYLGVSFHPELTDDYRVTDYFINHIVK 184
Cdd:PRK13525 162 GNILATSFHPELTDDTRVHRYFLEMVKE 189
PdxT COG0311
Pyridoxal 5'-phosphate synthase subunit PdxT (glutamine amidotransferase) [Coenzyme transport ...
 1-186 7.22e-100

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: 286.19  E-value: 7.22e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613093   1 MKIGVLALQGAVREHIRHIELSGHEGIAVKKVEQLEEIEGLILPGGESTTLRRLMNLYGFKEALQN---STLPMFGTCAG 77
Cdd:COG0311    1 MKIGVLALQGDVREHIRALERLGAEVVEVRRPEDLEGLDGLIIPGGESTTIGKLLRRFGLLEPLREriaAGLPVFGTCAG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613093  78 LIVLAQDIVGEEG-YLNKLNITVQRNSFGRQVDSFETELDIKGIATD-IEGVFIRAPHIEKVGQGVDILCKVNEKIVAVQ 155
Cdd:COG0311   81 LILLAKEIEDPDQpTLGLLDITVRRNAFGRQVDSFEADLDIPGLGDGpFPAVFIRAPYIEEVGPGVEVLATVDGRIVAVR 160

                        170       180       190
                 ....*....|....*....|....*....|.
gi 446613093 156 QGKYLGVSFHPELTDDYRVTDYFINHIVKKA 186
Cdd:COG0311  161 QGNILATSFHPELTDDLRVHEYFLEMVRGAK 191
PLP_synth_Pdx2 TIGR03800
pyridoxal 5'-phosphate synthase, glutaminase subunit Pdx2; Pyridoxal 5'-phosphate (PLP) is ...
 2-180 2.02e-98

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: 282.40  E-value: 2.02e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613093    2 KIGVLALQGAVREHIRHIELSGHEGIAVKKVEQLEEIEGLILPGGESTTLRRLMNLYGFKEALQN---STLPMFGTCAGL 78
Cdd:TIGR03800   1 KIGVLALQGAVREHARALEALGVEGVEVKRPEQLDEIDGLIIPGGESTTISRLLDKYGMFEPLRNfilSGLPVFGTCAGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613093   79 IVLAQDIVG-EEGYLNKLNITVQRNSFGRQVDSFETELDIKGIATD-IEGVFIRAPHIEKVGQGVDILCKVNEKIVAVQQ 156
Cdd:TIGR03800  81 IMLAKEIIGqKEGQLGLLDMTVERNAYGRQVDSFEAEVDIKGVGDDpITGVFIRAPKIVSVGNGVEILAKVGNRIVAVRQ 160

                         170       180
                  ....*....|....*....|....
gi 446613093  157 GKYLGVSFHPELTDDYRVTDYFIN 180
Cdd:TIGR03800 161 GNILVSSFHPELTDDHRVHEYFLE 184
GATase1_PB cd01749
Glutamine Amidotransferase (GATase_I) involved in pyridoxine biosynthesis; Glutamine ...
 3-179 2.23e-95

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: 274.40  E-value: 2.23e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613093   3 IGVLALQGAVREHIRHIELSGHEGIAVKKVEQLEEIEGLILPGGESTTLRRLMNLYGFKEALQN---STLPMFGTCAGLI 79
Cdd:cd01749    1 IGVLALQGDFREHIRALERLGVEVIEVRTPEDLEGIDGLIIPGGESTTIGKLLRRTGLLDPLREfirAGKPVFGTCAGLI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613093  80 VLAQDIVGEEG--YLNKLNITVQRNSFGRQVDSFETELDIKGIA-TDIEGVFIRAPHIEKVGQGVDILCKVNEKIVAVQQ 156
Cdd:cd01749   81 LLAKEVEDQGGqpLLGLLDITVRRNAFGRQVDSFEADLDIPGLGlGPFPAVFIRAPVIEEVGPGVEVLAEYDGKIVAVRQ 160

                        170       180
                 ....*....|....*....|...
gi 446613093 157 GKYLGVSFHPELTDDYRVTDYFI 179
Cdd:cd01749  161 GNVLATSFHPELTDDTRIHEYFL 183
SNO pfam01174
SNO glutamine amidotransferase family; This family and its amidotransferase domain was first ...
 5-184 2.32e-74

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: 221.63  E-value: 2.32e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613093    5 VLALQGAVREHIRHIELSGHEGIAVKKVEQLEEIEGLILPGGESTTLRRLMNLYGFKEAL----QNSTLPMFGTCAGLIV 80
Cdd:pfam01174   1 VLALQGAVEEHEEAIKKCGAENKTVKRPEDLAQCDALIIPGGESTAMSLLAKRYGFYEPLyefvHNPNKPIWGTCAGLIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613093   81 LAQDIVGEE-GYLNKLNITVQRNSFGRQVDSFETELDIKGIATDIEGVFIRAPHIEKVG--QGVDILCKVNEKIVAVQQG 157
Cdd:pfam01174  81 LSKQLGNELvKTLGLLKVTVKRNAFGRQVDSFEKECDFKNLIPKFPGVFIRAPVIEEILdpEVVVVLYELDGKIVVAKQG 160

                         170       180
                  ....*....|....*....|....*...
gi 446613093  158 KYLGVSFHPELT-DDYRVTDYFINHIVK 184
Cdd:pfam01174 161 NILATSFHPELAeDDYRVHDWFVENFVK 188
 
Name Accession Description Interval E-value
PRK13525 PRK13525
pyridoxal 5'-phosphate synthase glutaminase subunit PdxT;
1-184 2.97e-114

pyridoxal 5'-phosphate synthase glutaminase subunit PdxT;


Pssm-ID: 237411 [Multi-domain]  Cd Length: 189  Bit Score: 322.49  E-value: 2.97e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613093   1 MKIGVLALQGAVREHIRHIELSGHEGIAVKKVEQLEEIEGLILPGGESTTLRRLMNLYGFKEALQN---STLPMFGTCAG 77
Cdd:PRK13525   2 MKIGVLALQGAVREHLAALEALGAEAVEVRRPEDLDEIDGLILPGGESTTMGKLLRDFGLLEPLREfiaSGLPVFGTCAG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613093  78 LIVLAQDIVG-EEGYLNKLNITVQRNSFGRQVDSFETELDIKGIATDIEGVFIRAPHIEKVGQGVDILCKVNEKIVAVQQ 156
Cdd:PRK13525  82 MILLAKEIEGyEQEHLGLLDITVRRNAFGRQVDSFEAELDIKGLGEPFPAVFIRAPYIEEVGPGVEVLATVGGRIVAVRQ 161

                        170       180
                 ....*....|....*....|....*...
gi 446613093 157 GKYLGVSFHPELTDDYRVTDYFINHIVK 184
Cdd:PRK13525 162 GNILATSFHPELTDDTRVHRYFLEMVKE 189
PdxT COG0311
Pyridoxal 5'-phosphate synthase subunit PdxT (glutamine amidotransferase) [Coenzyme transport ...
 1-186 7.22e-100

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: 286.19  E-value: 7.22e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613093   1 MKIGVLALQGAVREHIRHIELSGHEGIAVKKVEQLEEIEGLILPGGESTTLRRLMNLYGFKEALQN---STLPMFGTCAG 77
Cdd:COG0311    1 MKIGVLALQGDVREHIRALERLGAEVVEVRRPEDLEGLDGLIIPGGESTTIGKLLRRFGLLEPLREriaAGLPVFGTCAG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613093  78 LIVLAQDIVGEEG-YLNKLNITVQRNSFGRQVDSFETELDIKGIATD-IEGVFIRAPHIEKVGQGVDILCKVNEKIVAVQ 155
Cdd:COG0311   81 LILLAKEIEDPDQpTLGLLDITVRRNAFGRQVDSFEADLDIPGLGDGpFPAVFIRAPYIEEVGPGVEVLATVDGRIVAVR 160

                        170       180       190
                 ....*....|....*....|....*....|.
gi 446613093 156 QGKYLGVSFHPELTDDYRVTDYFINHIVKKA 186
Cdd:COG0311  161 QGNILATSFHPELTDDLRVHEYFLEMVRGAK 191
PLP_synth_Pdx2 TIGR03800
pyridoxal 5'-phosphate synthase, glutaminase subunit Pdx2; Pyridoxal 5'-phosphate (PLP) is ...
 2-180 2.02e-98

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: 282.40  E-value: 2.02e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613093    2 KIGVLALQGAVREHIRHIELSGHEGIAVKKVEQLEEIEGLILPGGESTTLRRLMNLYGFKEALQN---STLPMFGTCAGL 78
Cdd:TIGR03800   1 KIGVLALQGAVREHARALEALGVEGVEVKRPEQLDEIDGLIIPGGESTTISRLLDKYGMFEPLRNfilSGLPVFGTCAGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613093   79 IVLAQDIVG-EEGYLNKLNITVQRNSFGRQVDSFETELDIKGIATD-IEGVFIRAPHIEKVGQGVDILCKVNEKIVAVQQ 156
Cdd:TIGR03800  81 IMLAKEIIGqKEGQLGLLDMTVERNAYGRQVDSFEAEVDIKGVGDDpITGVFIRAPKIVSVGNGVEILAKVGNRIVAVRQ 160

                         170       180
                  ....*....|....*....|....
gi 446613093  157 GKYLGVSFHPELTDDYRVTDYFIN 180
Cdd:TIGR03800 161 GNILVSSFHPELTDDHRVHEYFLE 184
GATase1_PB cd01749
Glutamine Amidotransferase (GATase_I) involved in pyridoxine biosynthesis; Glutamine ...
 3-179 2.23e-95

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: 274.40  E-value: 2.23e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613093   3 IGVLALQGAVREHIRHIELSGHEGIAVKKVEQLEEIEGLILPGGESTTLRRLMNLYGFKEALQN---STLPMFGTCAGLI 79
Cdd:cd01749    1 IGVLALQGDFREHIRALERLGVEVIEVRTPEDLEGIDGLIIPGGESTTIGKLLRRTGLLDPLREfirAGKPVFGTCAGLI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613093  80 VLAQDIVGEEG--YLNKLNITVQRNSFGRQVDSFETELDIKGIA-TDIEGVFIRAPHIEKVGQGVDILCKVNEKIVAVQQ 156
Cdd:cd01749   81 LLAKEVEDQGGqpLLGLLDITVRRNAFGRQVDSFEADLDIPGLGlGPFPAVFIRAPVIEEVGPGVEVLAEYDGKIVAVRQ 160

                        170       180
                 ....*....|....*....|...
gi 446613093 157 GKYLGVSFHPELTDDYRVTDYFI 179
Cdd:cd01749  161 GNVLATSFHPELTDDTRIHEYFL 183
PRK13527 PRK13527
glutamine amidotransferase subunit PdxT; Provisional
 1-185 1.47e-78

glutamine amidotransferase subunit PdxT; Provisional


Pssm-ID: 237412 [Multi-domain]  Cd Length: 200  Bit Score: 232.47  E-value: 1.47e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613093   1 MKIGVLALQGAVREHIRHIELS------GHEGIAVKKVEQLEEIEGLILPGGESTTLRRLMNLYGFKEALQN---STLPM 71
Cdd:PRK13527   1 MKIGVLALQGDVEEHIDALKRAldelgiDGEVVEVRRPGDLPDCDALIIPGGESTTIGRLMKREGILDEIKEkieEGLPI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613093  72 FGTCAGLIVLAQDI----VGEEG--YLNKLNITVQRNSFGRQVDSFETELDIKGIATDIEGVFIRAPHIEKVGQGVDILC 145
Cdd:PRK13527  81 LGTCAGLILLAKEVgddrVTKTEqpLLGLMDVTVKRNAFGRQRDSFEAEIDLSGLDGPFHAVFIRAPAITKVGGDVEVLA 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 446613093 146 KVNEKIVAVQQGKYLGVSFHPELTDDYRVTDYFINHIVKK 185
Cdd:PRK13527 161 KLDDRIVAVEQGNVLATAFHPELTDDTRIHEYFLKKVKGK 200
SNO pfam01174
SNO glutamine amidotransferase family; This family and its amidotransferase domain was first ...
 5-184 2.32e-74

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: 221.63  E-value: 2.32e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613093    5 VLALQGAVREHIRHIELSGHEGIAVKKVEQLEEIEGLILPGGESTTLRRLMNLYGFKEAL----QNSTLPMFGTCAGLIV 80
Cdd:pfam01174   1 VLALQGAVEEHEEAIKKCGAENKTVKRPEDLAQCDALIIPGGESTAMSLLAKRYGFYEPLyefvHNPNKPIWGTCAGLIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613093   81 LAQDIVGEE-GYLNKLNITVQRNSFGRQVDSFETELDIKGIATDIEGVFIRAPHIEKVG--QGVDILCKVNEKIVAVQQG 157
Cdd:pfam01174  81 LSKQLGNELvKTLGLLKVTVKRNAFGRQVDSFEKECDFKNLIPKFPGVFIRAPVIEEILdpEVVVVLYELDGKIVVAKQG 160

                         170       180
                  ....*....|....*....|....*...
gi 446613093  158 KYLGVSFHPELT-DDYRVTDYFINHIVK 184
Cdd:pfam01174 161 NILATSFHPELAeDDYRVHDWFVENFVK 188
PLN02832 PLN02832
glutamine amidotransferase subunit of pyridoxal 5'-phosphate synthase complex
 1-179 3.86e-62

glutamine amidotransferase subunit of pyridoxal 5'-phosphate synthase complex


Pssm-ID: 215446 [Multi-domain]  Cd Length: 248  Bit Score: 192.62  E-value: 3.86e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613093   1 MKIGVLALQGAVREHIRHIELSGHEGIAVKKVEQLEEIEGLILPGGESTTLRRLMNLYGFKEAL---QNSTLPMFGTCAG 77
Cdd:PLN02832   2 MAIGVLALQGSFNEHIAALRRLGVEAVEVRKPEQLEGVSGLIIPGGESTTMAKLAERHNLFPALrefVKSGKPVWGTCAG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613093  78 LIVLAQDIVG-EEG---YLNKLNITVQRNSFGRQVDSFETELDIK------GIATDIEGVFIRAPHIEKVGQGVDILCKV 147
Cdd:PLN02832  82 LIFLAERAVGqKEGgqeLLGGLDCTVHRNFFGSQINSFETELPVPelaaseGGPETFRAVFIRAPAILSVGPGVEVLAEY 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 446613093 148 ------------------NEKIVAVQQGKYLGVSFHPELTDDYRVTDYFI 179
Cdd:PLN02832 162 plpsekalyssstdaegrDKVIVAVKQGNLLATAFHPELTADTRWHSYFV 211
PRK13526 PRK13526
glutamine amidotransferase subunit PdxT; Provisional
 1-180 1.87e-50

glutamine amidotransferase subunit PdxT; Provisional


Pssm-ID: 184113 [Multi-domain]  Cd Length: 179  Bit Score: 160.50  E-value: 1.87e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613093   1 MKIGVLALQGAVREHIRHIELSGHEGIAVKKVEQLEEIEGLILPGGESTTLRRLMNLYGFKEALQN--STLPMFGTCAGL 78
Cdd:PRK13526   3 QKVGVLAIQGGYQKHADMFKSLGVEVKLVKFNNDFDSIDRLVIPGGESTTLLNLLNKHQIFDKLYNfcSSKPVFGTCAGS 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613093  79 IVLAQDivgeEGYLNKLNITVQRNSFGRQVDSFETELDIKGiaTDIEGVFIRAPHIEKVGQGVDILCKVNEKIVAVQQGK 158
Cdd:PRK13526  83 IILSKG----EGYLNLLDLEVQRNAYGRQVDSFVADISFND--KNITGVFIRAPKFIVVGNQVDILSKYQNSPVLLRQAN 156

                        170       180
                 ....*....|....*....|..
gi 446613093 159 YLGVSFHPELTDDYRVTDYFIN 180
Cdd:PRK13526 157 ILVSSFHPELTQDPTVHEYFLA 178
GATase_3 pfam07685
CobB/CobQ-like glutamine amidotransferase domain;
5-90 6.23e-04

CobB/CobQ-like glutamine amidotransferase domain;


Pssm-ID: 429595 [Multi-domain]  Cd Length: 189  Bit Score: 38.76  E-value: 6.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613093    5 VLALQGAVREHIrhielsghegIAVKKVEQLEEIEGLILPGGESTT-LRRLMNLYGFKEALQN---STLPMFGTCAGLIV 80
Cdd:pfam07685  20 PLRYEPAVRVRF----------VPLPDESLGPDADLIILPGGKPTIqDLALLRNSGMDEAIKEaaeDGGPVLGICGGYQM 89

                          90
                  ....*....|
gi 446613093   81 LAQDIVGEEG 90
Cdd:pfam07685  90 LGETIEDPEG 99
GATase1_CobB cd03130
Type 1 glutamine amidotransferase (GATase1) domain found in Cobyrinic Acid a,c-Diamide ...
 33-90 1.07e-03

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: 38.35  E-value: 1.07e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446613093  33 EQLEEIEGLILPGG--EsTTLRRLMNLYGFKEALQ---NSTLPMFGTCAGLIVLAQDIVGEEG 90
Cdd:cd03130   36 EELPDADGLYLGGGypE-LFAEELSANQSMRESIRafaESGGPIYAECGGLMYLGESLDDEEG 97
 
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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