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Conserved domains on  [gi|2099416996|gb|UBH25385|]
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pyridoxal 5'-phosphate synthase glutaminase subunit PdxT [Micrococcus porci]

Protein Classification

PdxT family protein( domain architecture ID 10785267)

PdxT family protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PdxT COG0311
Pyridoxal 5'-phosphate synthase subunit PdxT (glutamine amidotransferase) [Coenzyme transport ...
 6-212 4.15e-84

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: 247.67  E-value: 4.15e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099416996   6 KTVGVFALQGDVREHVHVLEALGARTRPVRRPADLAGLDGIVLPGEESSVMDRLARIMGLRDPLAEAVRAGLPVYGTCAG 85
Cdd:COG0311     1 MKIGVLALQGDVREHIRALERLGAEVVEVRRPEDLEGLDGLIIPGGESTTIGKLLRRFGLLEPLRERIAAGLPVFGTCAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099416996  86 MILLAAGIENpaPGQGSLGVLDVTVRRNAFGSQADSLEADLQVPAVSADPMHAVLIRAPAvvrvgegvevlasvpaarav 165
Cdd:COG0311    81 LILLAKEIED--PDQPTLGLLDITVRRNAFGRQVDSFEADLDIPGLGDGPFPAVFIRAPY-------------------- 138

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2099416996 166 aasssTAETDDG----APAADLPVAVRAGNVSATSFHPEVTGDWSFHRAFL 212
Cdd:COG0311   139 -----IEEVGPGvevlATVDGRIVAVRQGNILATSFHPELTDDLRVHEYFL 184
 
Name Accession Description Interval E-value
PdxT COG0311
Pyridoxal 5'-phosphate synthase subunit PdxT (glutamine amidotransferase) [Coenzyme transport ...
 6-212 4.15e-84

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: 247.67  E-value: 4.15e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099416996   6 KTVGVFALQGDVREHVHVLEALGARTRPVRRPADLAGLDGIVLPGEESSVMDRLARIMGLRDPLAEAVRAGLPVYGTCAG 85
Cdd:COG0311     1 MKIGVLALQGDVREHIRALERLGAEVVEVRRPEDLEGLDGLIIPGGESTTIGKLLRRFGLLEPLRERIAAGLPVFGTCAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099416996  86 MILLAAGIENpaPGQGSLGVLDVTVRRNAFGSQADSLEADLQVPAVSADPMHAVLIRAPAvvrvgegvevlasvpaarav 165
Cdd:COG0311    81 LILLAKEIED--PDQPTLGLLDITVRRNAFGRQVDSFEADLDIPGLGDGPFPAVFIRAPY-------------------- 138

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2099416996 166 aasssTAETDDG----APAADLPVAVRAGNVSATSFHPEVTGDWSFHRAFL 212
Cdd:COG0311   139 -----IEEVGPGvevlATVDGRIVAVRQGNILATSFHPELTDDLRVHEYFL 184
PRK13525 PRK13525
pyridoxal 5'-phosphate synthase glutaminase subunit PdxT;
6-212 1.44e-83

pyridoxal 5'-phosphate synthase glutaminase subunit PdxT;


Pssm-ID: 237411 [Multi-domain]  Cd Length: 189  Bit Score: 246.22  E-value: 1.44e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099416996   6 KTVGVFALQGDVREHVHVLEALGARTRPVRRPADLAGLDGIVLPGEESSVMDRLARIMGLRDPLAEAVRAGLPVYGTCAG 85
Cdd:PRK13525    2 MKIGVLALQGAVREHLAALEALGAEAVEVRRPEDLDEIDGLILPGGESTTMGKLLRDFGLLEPLREFIASGLPVFGTCAG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099416996  86 MILLAAGIENpaPGQGSLGVLDVTVRRNAFGSQADSLEADLQVPAVsADPMHAVLIRAPavvrvgegvevlasvpaarav 165
Cdd:PRK13525   82 MILLAKEIEG--YEQEHLGLLDITVRRNAFGRQVDSFEAELDIKGL-GEPFPAVFIRAP--------------------- 137

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2099416996 166 aassSTAETDDG----APAADLPVAVRAGNVSATSFHPEVTGDWSFHRAFL 212
Cdd:PRK13525  138 ----YIEEVGPGvevlATVGGRIVAVRQGNILATSFHPELTDDTRVHRYFL 184
GATase1_PB cd01749
Glutamine Amidotransferase (GATase_I) involved in pyridoxine biosynthesis; Glutamine ...
 8-212 3.22e-80

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: 237.42  E-value: 3.22e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099416996   8 VGVFALQGDVREHVHVLEALGARTRPVRRPADLAGLDGIVLPGEESSVMDRLARIMGLRDPLAEAVRAGLPVYGTCAGMI 87
Cdd:cd01749     1 IGVLALQGDFREHIRALERLGVEVIEVRTPEDLEGIDGLIIPGGESTTIGKLLRRTGLLDPLREFIRAGKPVFGTCAGLI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099416996  88 LLAAGIENPaPGQGSLGVLDVTVRRNAFGSQADSLEADLQVPAVSADPMHAVLIRAPAVVRVGEGVEVLasvpaaravaa 167
Cdd:cd01749    81 LLAKEVEDQ-GGQPLLGLLDITVRRNAFGRQVDSFEADLDIPGLGLGPFPAVFIRAPVIEEVGPGVEVL----------- 148

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2099416996 168 ssstaetddgAPAADLPVAVRAGNVSATSFHPEVTGDWSFHRAFL 212
Cdd:cd01749   149 ----------AEYDGKIVAVRQGNVLATSFHPELTDDTRIHEYFL 183
PLP_synth_Pdx2 TIGR03800
pyridoxal 5'-phosphate synthase, glutaminase subunit Pdx2; Pyridoxal 5'-phosphate (PLP) is ...
 8-213 2.18e-63

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: 194.96  E-value: 2.18e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099416996   8 VGVFALQGDVREHVHVLEALGARTRPVRRPADLAGLDGIVLPGEESSVMDRLARIMGLRDPLAEAVRAGLPVYGTCAGMI 87
Cdd:TIGR03800   2 IGVLALQGAVREHARALEALGVEGVEVKRPEQLDEIDGLIIPGGESTTISRLLDKYGMFEPLRNFILSGLPVFGTCAGLI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099416996  88 LLAAGIENPAPGQgsLGVLDVTVRRNAFGSQADSLEADLQVPAVSADPMHAVLIRAPAVVRVGEGVEVLasvpaaravaa 167
Cdd:TIGR03800  82 MLAKEIIGQKEGQ--LGLLDMTVERNAYGRQVDSFEAEVDIKGVGDDPITGVFIRAPKIVSVGNGVEIL----------- 148

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2099416996 168 ssstaetddgAPAADLPVAVRAGNVSATSFHPEVTGDWSFHRAFLA 213
Cdd:TIGR03800 149 ----------AKVGNRIVAVRQGNILVSSFHPELTDDHRVHEYFLE 184
SNO pfam01174
SNO glutamine amidotransferase family; This family and its amidotransferase domain was first ...
 10-212 1.71e-43

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: 144.21  E-value: 1.71e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099416996  10 VFALQGDVREHVHVLEALGARTRPVRRPADLAGLDGIVLPGEESSVMDRLARIMGLRDPLAEAVRAG-LPVYGTCAGMIL 88
Cdd:pfam01174   1 VLALQGAVEEHEEAIKKCGAENKTVKRPEDLAQCDALIIPGGESTAMSLLAKRYGFYEPLYEFVHNPnKPIWGTCAGLIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099416996  89 LAAGIENPApgQGSLGVLDVTVRRNAFGSQADSLEADLQVPAVsADPMHAVLIRAPavvrvgegvevlasvpaaravaAS 168
Cdd:pfam01174  81 LSKQLGNEL--VKTLGLLKVTVKRNAFGRQVDSFEKECDFKNL-IPKFPGVFIRAP----------------------VI 135

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2099416996 169 SSTAETDDGAPAADLP---VAVRAGNVSATSFHPEVT-GDWSFHRAFL 212
Cdd:pfam01174 136 EEILDPEVVVVLYELDgkiVVAKQGNILATSFHPELAeDDYRVHDWFV 183
 
Name Accession Description Interval E-value
PdxT COG0311
Pyridoxal 5'-phosphate synthase subunit PdxT (glutamine amidotransferase) [Coenzyme transport ...
 6-212 4.15e-84

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: 247.67  E-value: 4.15e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099416996   6 KTVGVFALQGDVREHVHVLEALGARTRPVRRPADLAGLDGIVLPGEESSVMDRLARIMGLRDPLAEAVRAGLPVYGTCAG 85
Cdd:COG0311     1 MKIGVLALQGDVREHIRALERLGAEVVEVRRPEDLEGLDGLIIPGGESTTIGKLLRRFGLLEPLRERIAAGLPVFGTCAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099416996  86 MILLAAGIENpaPGQGSLGVLDVTVRRNAFGSQADSLEADLQVPAVSADPMHAVLIRAPAvvrvgegvevlasvpaarav 165
Cdd:COG0311    81 LILLAKEIED--PDQPTLGLLDITVRRNAFGRQVDSFEADLDIPGLGDGPFPAVFIRAPY-------------------- 138

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2099416996 166 aasssTAETDDG----APAADLPVAVRAGNVSATSFHPEVTGDWSFHRAFL 212
Cdd:COG0311   139 -----IEEVGPGvevlATVDGRIVAVRQGNILATSFHPELTDDLRVHEYFL 184
PRK13525 PRK13525
pyridoxal 5'-phosphate synthase glutaminase subunit PdxT;
6-212 1.44e-83

pyridoxal 5'-phosphate synthase glutaminase subunit PdxT;


Pssm-ID: 237411 [Multi-domain]  Cd Length: 189  Bit Score: 246.22  E-value: 1.44e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099416996   6 KTVGVFALQGDVREHVHVLEALGARTRPVRRPADLAGLDGIVLPGEESSVMDRLARIMGLRDPLAEAVRAGLPVYGTCAG 85
Cdd:PRK13525    2 MKIGVLALQGAVREHLAALEALGAEAVEVRRPEDLDEIDGLILPGGESTTMGKLLRDFGLLEPLREFIASGLPVFGTCAG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099416996  86 MILLAAGIENpaPGQGSLGVLDVTVRRNAFGSQADSLEADLQVPAVsADPMHAVLIRAPavvrvgegvevlasvpaarav 165
Cdd:PRK13525   82 MILLAKEIEG--YEQEHLGLLDITVRRNAFGRQVDSFEAELDIKGL-GEPFPAVFIRAP--------------------- 137

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2099416996 166 aassSTAETDDG----APAADLPVAVRAGNVSATSFHPEVTGDWSFHRAFL 212
Cdd:PRK13525  138 ----YIEEVGPGvevlATVGGRIVAVRQGNILATSFHPELTDDTRVHRYFL 184
GATase1_PB cd01749
Glutamine Amidotransferase (GATase_I) involved in pyridoxine biosynthesis; Glutamine ...
 8-212 3.22e-80

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: 237.42  E-value: 3.22e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099416996   8 VGVFALQGDVREHVHVLEALGARTRPVRRPADLAGLDGIVLPGEESSVMDRLARIMGLRDPLAEAVRAGLPVYGTCAGMI 87
Cdd:cd01749     1 IGVLALQGDFREHIRALERLGVEVIEVRTPEDLEGIDGLIIPGGESTTIGKLLRRTGLLDPLREFIRAGKPVFGTCAGLI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099416996  88 LLAAGIENPaPGQGSLGVLDVTVRRNAFGSQADSLEADLQVPAVSADPMHAVLIRAPAVVRVGEGVEVLasvpaaravaa 167
Cdd:cd01749    81 LLAKEVEDQ-GGQPLLGLLDITVRRNAFGRQVDSFEADLDIPGLGLGPFPAVFIRAPVIEEVGPGVEVL----------- 148

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2099416996 168 ssstaetddgAPAADLPVAVRAGNVSATSFHPEVTGDWSFHRAFL 212
Cdd:cd01749   149 ----------AEYDGKIVAVRQGNVLATSFHPELTDDTRIHEYFL 183
PLP_synth_Pdx2 TIGR03800
pyridoxal 5'-phosphate synthase, glutaminase subunit Pdx2; Pyridoxal 5'-phosphate (PLP) is ...
 8-213 2.18e-63

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: 194.96  E-value: 2.18e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099416996   8 VGVFALQGDVREHVHVLEALGARTRPVRRPADLAGLDGIVLPGEESSVMDRLARIMGLRDPLAEAVRAGLPVYGTCAGMI 87
Cdd:TIGR03800   2 IGVLALQGAVREHARALEALGVEGVEVKRPEQLDEIDGLIIPGGESTTISRLLDKYGMFEPLRNFILSGLPVFGTCAGLI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099416996  88 LLAAGIENPAPGQgsLGVLDVTVRRNAFGSQADSLEADLQVPAVSADPMHAVLIRAPAVVRVGEGVEVLasvpaaravaa 167
Cdd:TIGR03800  82 MLAKEIIGQKEGQ--LGLLDMTVERNAYGRQVDSFEAEVDIKGVGDDPITGVFIRAPKIVSVGNGVEIL----------- 148

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2099416996 168 ssstaetddgAPAADLPVAVRAGNVSATSFHPEVTGDWSFHRAFLA 213
Cdd:TIGR03800 149 ----------AKVGNRIVAVRQGNILVSSFHPELTDDHRVHEYFLE 184
PRK13527 PRK13527
glutamine amidotransferase subunit PdxT; Provisional
 7-212 1.83e-59

glutamine amidotransferase subunit PdxT; Provisional


Pssm-ID: 237412 [Multi-domain]  Cd Length: 200  Bit Score: 185.48  E-value: 1.83e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099416996   7 TVGVFALQGDVREHVHVLEALGAR------TRPVRRPADLAGLDGIVLPGEESSVMDRLARIMGLRDPLAEAVRAGLPVY 80
Cdd:PRK13527    2 KIGVLALQGDVEEHIDALKRALDElgidgeVVEVRRPGDLPDCDALIIPGGESTTIGRLMKREGILDEIKEKIEEGLPIL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099416996  81 GTCAGMILLAAGIENP---APGQGSLGVLDVTVRRNAFGSQADSLEADLQVpAVSADPMHAVLIRAPAVVRVGEGVEVLa 157
Cdd:PRK13527   82 GTCAGLILLAKEVGDDrvtKTEQPLLGLMDVTVKRNAFGRQRDSFEAEIDL-SGLDGPFHAVFIRAPAITKVGGDVEVL- 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2099416996 158 svpaaravaassstaetddgAPAADLPVAVRAGNVSATSFHPEVTGDWSFHRAFL 212
Cdd:PRK13527  160 --------------------AKLDDRIVAVEQGNVLATAFHPELTDDTRIHEYFL 194
PLN02832 PLN02832
glutamine amidotransferase subunit of pyridoxal 5'-phosphate synthase complex
 7-212 1.12e-51

glutamine amidotransferase subunit of pyridoxal 5'-phosphate synthase complex


Pssm-ID: 215446 [Multi-domain]  Cd Length: 248  Bit Score: 167.19  E-value: 1.12e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099416996   7 TVGVFALQGDVREHVHVLEALGARTRPVRRPADLAGLDGIVLPGEESSVMDRLARIMGLRDPLAEAVRAGLPVYGTCAGM 86
Cdd:PLN02832    3 AIGVLALQGSFNEHIAALRRLGVEAVEVRKPEQLEGVSGLIIPGGESTTMAKLAERHNLFPALREFVKSGKPVWGTCAGL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099416996  87 ILLAAGIENPAP-GQGSLGVLDVTVRRNAFGSQADSLEADLQVPAVSAD-----PMHAVLIRAPAVVRVGEGVEVLasVP 160
Cdd:PLN02832   83 IFLAERAVGQKEgGQELLGGLDCTVHRNFFGSQINSFETELPVPELAASeggpeTFRAVFIRAPAILSVGPGVEVL--AE 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2099416996 161 AARAVAASSSTAETDDGaPAADLPVAVRAGNVSATSFHPEVTGDWSFHRAFL 212
Cdd:PLN02832  161 YPLPSEKALYSSSTDAE-GRDKVIVAVKQGNLLATAFHPELTADTRWHSYFV 211
SNO pfam01174
SNO glutamine amidotransferase family; This family and its amidotransferase domain was first ...
 10-212 1.71e-43

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: 144.21  E-value: 1.71e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099416996  10 VFALQGDVREHVHVLEALGARTRPVRRPADLAGLDGIVLPGEESSVMDRLARIMGLRDPLAEAVRAG-LPVYGTCAGMIL 88
Cdd:pfam01174   1 VLALQGAVEEHEEAIKKCGAENKTVKRPEDLAQCDALIIPGGESTAMSLLAKRYGFYEPLYEFVHNPnKPIWGTCAGLIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099416996  89 LAAGIENPApgQGSLGVLDVTVRRNAFGSQADSLEADLQVPAVsADPMHAVLIRAPavvrvgegvevlasvpaaravaAS 168
Cdd:pfam01174  81 LSKQLGNEL--VKTLGLLKVTVKRNAFGRQVDSFEKECDFKNL-IPKFPGVFIRAP----------------------VI 135

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2099416996 169 SSTAETDDGAPAADLP---VAVRAGNVSATSFHPEVT-GDWSFHRAFL 212
Cdd:pfam01174 136 EEILDPEVVVVLYELDgkiVVAKQGNILATSFHPELAeDDYRVHDWFV 183
PRK13526 PRK13526
glutamine amidotransferase subunit PdxT; Provisional
 7-213 5.88e-31

glutamine amidotransferase subunit PdxT; Provisional


Pssm-ID: 184113 [Multi-domain]  Cd Length: 179  Bit Score: 111.97  E-value: 5.88e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099416996   7 TVGVFALQGDVREHVHVLEALGARTRPVRRPADLAGLDGIVLPGEESSVMDRLARIMGLRDPLAEAVRAGlPVYGTCAGM 86
Cdd:PRK13526    4 KVGVLAIQGGYQKHADMFKSLGVEVKLVKFNNDFDSIDRLVIPGGESTTLLNLLNKHQIFDKLYNFCSSK-PVFGTCAGS 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099416996  87 ILLAAGienpapgQGSLGVLDVTVRRNAFGSQADSLEADLqvpAVSADPMHAVLIRAPAVVRVGEGVEVLasvpaarava 166
Cdd:PRK13526   83 IILSKG-------EGYLNLLDLEVQRNAYGRQVDSFVADI---SFNDKNITGVFIRAPKFIVVGNQVDIL---------- 142

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2099416996 167 assstaetddgAPAADLPVAVRAGNVSATSFHPEVTGDWSFHRAFLA 213
Cdd:PRK13526  143 -----------SKYQNSPVLLRQANILVSSFHPELTQDPTVHEYFLA 178
hisH PRK13181
imidazole glycerol phosphate synthase subunit HisH; Provisional
 15-112 1.32e-12

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 183878 [Multi-domain]  Cd Length: 199  Bit Score: 63.73  E-value: 1.32e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099416996  15 GDVREHVHVLEALGARTRPVRRPADLAGLDGIVLPG--EESSVMDRLaRIMGLRDPLAEAVRAGLPVYGTCAGMILLAAG 92
Cdd:PRK13181   10 GNLRSVANALKRLGVEAVVSSDPEEIAGADKVILPGvgAFGQAMRSL-RESGLDEALKEHVEKKQPVLGICLGMQLLFES 88

                          90       100
                  ....*....|....*....|.
gi 2099416996  93 IENPA-PGqgsLGVLDVTVRR 112
Cdd:PRK13181   89 SEEGNvKG---LGLIPGDVKR 106
GATase1_CobQ cd01750
Type 1 glutamine amidotransferase (GATase1) domain found in Cobyric Acid Synthase (CobQ); Type ...
 21-114 1.38e-08

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: 52.63  E-value: 1.38e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099416996  21 VHVLEAL----GARTRPVRRPADLAGLDGIVLPGEESSVMDRLA-RIMGLRDPLAEAVRAGLPVYGTCAGMILL------ 89
Cdd:cd01750    12 FTDLDPLarepGVDVRYVEVPEGLGDADLIILPGSKDTIQDLAWlRKRGLAEAIKNYARAGGPVLGICGGYQMLgkyivd 91

                          90       100
                  ....*....|....*....|....*
gi 2099416996  90 AAGIENPAPGQGsLGVLDVTVRRNA 114
Cdd:cd01750    92 PEGVEGPGEIEG-LGLLDVETEFGP 115
hisH PRK13143
imidazole glycerol phosphate synthase subunit HisH; Provisional
 24-112 1.84e-08

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237289 [Multi-domain]  Cd Length: 200  Bit Score: 52.56  E-value: 1.84e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099416996  24 LEALGARTRPVRRPADLAGLDGIVLP--GEESSVMDRLARimgLRDPLAEAVRAGLPVYGTCAGM-ILLAAGIENPApGQ 100
Cdd:PRK13143   20 LERAGAEVVITSDPEEILDADGIVLPgvGAFGAAMENLSP---LRDVILEAARSGKPFLGICLGMqLLFESSEEGGG-VR 95

                          90
                  ....*....|..
gi 2099416996 101 GsLGVLDVTVRR 112
Cdd:PRK13143   96 G-LGLFPGRVVR 106
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 8-97 1.59e-07

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: 48.36  E-value: 1.59e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099416996   8 VGVFALQG----DVREHVHVLEALGARTR-------PVRRPADLAGLDGIVLPGEESSVMDrLARIMGLRDPLAEAVRAG 76
Cdd:cd01653     1 VAVLLFPGfeelELASPLDALREAGAEVDvvspdggPVESDVDLDDYDGLILPGGPGTPDD-LARDEALLALLREAAAAG 79

                          90       100
                  ....*....|....*....|.
gi 2099416996  77 LPVYGTCAGMILLAAGIENPA 97
Cdd:cd01653    80 KPILGICLGAQLLVLGVQFHP 100
GATase1_CobB cd03130
Type 1 glutamine amidotransferase (GATase1) domain found in Cobyrinic Acid a,c-Diamide ...
 18-111 4.12e-07

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: 48.36  E-value: 4.12e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099416996  18 REHVHVLEALGARTRPVR--RPADLAGLDGIVLPG---EEssVMDRLARIMGLRDPLAEAVRAGLPVYGTCAGMILLAAG 92
Cdd:cd03130    14 PENLELLEAAGAELVPFSplKDEELPDADGLYLGGgypEL--FAEELSANQSMRESIRAFAESGGPIYAECGGLMYLGES 91

                          90       100
                  ....*....|....*....|
gi 2099416996  93 IENPAPGQGS-LGVLDVTVR 111
Cdd:cd03130    92 LDDEEGQSYPmAGVLPGDAR 111
GATase_3 pfam07685
CobB/CobQ-like glutamine amidotransferase domain;
44-111 5.59e-07

CobB/CobQ-like glutamine amidotransferase domain;


Pssm-ID: 429595 [Multi-domain]  Cd Length: 189  Bit Score: 48.01  E-value: 5.59e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2099416996  44 DGIVLPGEESSVMD-RLARIMGLRDPLAEAVRAGLPVYGTCAGMILLAAGIENPA----PGqgsLGVLDVTVR 111
Cdd:pfam07685  44 DLIILPGGKPTIQDlALLRNSGMDEAIKEAAEDGGPVLGICGGYQMLGETIEDPEgvriEG---LGLLDIETV 113
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 15-89 2.02e-06

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: 44.50  E-value: 2.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099416996  15 GDVREHVHVLEALGARTR-------PVRRPADLAGLDGIVLPGEESSVMDrLARIMGLRDPLAEAVRAGLPVYGTCAGMI 87
Cdd:cd03128    12 LELASPLDALREAGAEVDvvspdggPVESDVDLDDYDGLILPGGPGTPDD-LAWDEALLALLREAAAAGKPVLGICLGAQ 90


                  ..
gi 2099416996  88 LL 89
Cdd:cd03128    91 LL 92
CobB COG1797
Cobyrinic acid a,c-diamide synthase [Coenzyme transport and metabolism]; Cobyrinic acid a, ...
 18-116 2.75e-06

Cobyrinic acid a,c-diamide synthase [Coenzyme transport and metabolism]; Cobyrinic acid a,c-diamide synthase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 441402 [Multi-domain]  Cd Length: 459  Bit Score: 47.03  E-value: 2.75e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099416996  18 REHVHVLEALGARTRPVR--RPADL-AGLDGIVLPG---EESsvMDRLARIMGLRDPLAEAVRAGLPVYGTCAGMILLAA 91
Cdd:COG1797   264 PENLELLEAAGAELVFFSplRDEALpEDVDGLYLGGgfpELF--AEELSANRSMRESIREAAEAGMPIYAECGGLMYLCR 341

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2099416996  92 GIENpAPGQGS--LGVLDVTV----RRNAFG 116
Cdd:COG1797   342 SITD-FEGKGYpmVGVLPGDAvmtkRLQGLG 371
PRK01077 PRK01077
cobyrinate a,c-diamide synthase;
19-116 1.03e-05

cobyrinate a,c-diamide synthase;


Pssm-ID: 234896 [Multi-domain]  Cd Length: 451  Bit Score: 45.51  E-value: 1.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099416996  19 EHVHVLEALGARTRPVRRPAD--LAGLDGIVLPG---EESSvmDRLARIMGLRDPLAEAVRAGLPVYGTCAGMILLAAGI 93
Cdd:PRK01077  262 ENLELLRAAGAELVFFSPLADeaLPDCDGLYLGGgypELFA--AELAANTSMRASIRAAAAAGKPIYAECGGLMYLGESL 339

                          90       100
                  ....*....|....*....|....*....
gi 2099416996  94 ENpAPGQGS--LGVLDVTV----RRNAFG 116
Cdd:PRK01077  340 ED-ADGERHpmVGLLPGEAsmtkRLQALG 367
hisH CHL00188
imidazole glycerol phosphate synthase subunit hisH; Provisional
 34-112 6.36e-04

imidazole glycerol phosphate synthase subunit hisH; Provisional


Pssm-ID: 214389 [Multi-domain]  Cd Length: 210  Bit Score: 39.48  E-value: 6.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099416996  34 VRRPADLAGLDGIVLPGEES--SVMDRLARiMGLRDPLAEAVRAGLPVYGTCAGM-ILLAAGIENPAPGqgsLGVLDVTV 110
Cdd:CHL00188   31 INSESELAQVHALVLPGVGSfdLAMKKLEK-KGLITPIKKWIAEGNPFIGICLGLhLLFETSEEGKEEG---LGIYKGQV 106


                  ..
gi 2099416996 111 RR 112
Cdd:CHL00188  107 KR 108
PRK03619 PRK03619
phosphoribosylformylglycinamidine synthase subunit PurQ;
18-92 8.74e-04

phosphoribosylformylglycinamidine synthase subunit PurQ;


Pssm-ID: 235140 [Multi-domain]  Cd Length: 219  Bit Score: 38.94  E-value: 8.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099416996  18 REHVHVLEA-LGARTRPV-RRPADLAGLDGIVLPGEES-------SVMDRLARIMglrDPLAEAVRAGLPVYGTCAGM-I 87
Cdd:PRK03619   15 RDMARALRDlLGAEPEYVwHKETDLDGVDAVVLPGGFSygdylrcGAIAAFSPIM---KAVKEFAEKGKPVLGICNGFqI 91


                  ....*
gi 2099416996  88 LLAAG 92
Cdd:PRK03619   92 LTEAG 96
 
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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