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Conserved domains on  [gi|489319454|ref|WP_003226797|]
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MULTISPECIES: pyridoxal 5'-phosphate synthase glutaminase subunit PdxT [Bacillus]

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;
1-189 1.22e-127

pyridoxal 5'-phosphate synthase glutaminase subunit PdxT;


:

Pssm-ID: 237411 [Multi-domain]  Cd Length: 189  Bit Score: 356.78  E-value: 1.22e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489319454   1 MLTIGVLGLQGAVREHIHAIEACGAAGLVVKRPEQLNEVDGLILPGGESTTMRRLIDTYQFMEPLREFAAQGKPMFGTCA 80
Cdd:PRK13525   1 MMKIGVLALQGAVREHLAALEALGAEAVEVRRPEDLDEIDGLILPGGESTTMGKLLRDFGLLEPLREFIASGLPVFGTCA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489319454  81 GLIILAKEIAGSDNPHLGLLNVVVERNSFGRQVDSFEADLTIKGLDEPFTGVFIRAPHILEAGENVEVLSEHNGRIVAAK 160
Cdd:PRK13525  81 GMILLAKEIEGYEQEHLGLLDITVRRNAFGRQVDSFEAELDIKGLGEPFPAVFIRAPYIEEVGPGVEVLATVGGRIVAVR 160

                        170       180
                 ....*....|....*....|....*....
gi 489319454 161 QGQFLGCSFHPELTEDHRVTQLFVEMVEE 189
Cdd:PRK13525 161 QGNILATSFHPELTDDTRVHRYFLEMVKE 189
 
Name Accession Description Interval E-value
PRK13525 PRK13525
pyridoxal 5'-phosphate synthase glutaminase subunit PdxT;
1-189 1.22e-127

pyridoxal 5'-phosphate synthase glutaminase subunit PdxT;


Pssm-ID: 237411 [Multi-domain]  Cd Length: 189  Bit Score: 356.78  E-value: 1.22e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489319454   1 MLTIGVLGLQGAVREHIHAIEACGAAGLVVKRPEQLNEVDGLILPGGESTTMRRLIDTYQFMEPLREFAAQGKPMFGTCA 80
Cdd:PRK13525   1 MMKIGVLALQGAVREHLAALEALGAEAVEVRRPEDLDEIDGLILPGGESTTMGKLLRDFGLLEPLREFIASGLPVFGTCA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489319454  81 GLIILAKEIAGSDNPHLGLLNVVVERNSFGRQVDSFEADLTIKGLDEPFTGVFIRAPHILEAGENVEVLSEHNGRIVAAK 160
Cdd:PRK13525  81 GMILLAKEIEGYEQEHLGLLDITVRRNAFGRQVDSFEAELDIKGLGEPFPAVFIRAPYIEEVGPGVEVLATVGGRIVAVR 160

                        170       180
                 ....*....|....*....|....*....
gi 489319454 161 QGQFLGCSFHPELTEDHRVTQLFVEMVEE 189
Cdd:PRK13525 161 QGNILATSFHPELTDDTRVHRYFLEMVKE 189
PdxT COG0311
Pyridoxal 5'-phosphate synthase subunit PdxT (glutamine amidotransferase) [Coenzyme transport ...
 2-191 3.17e-119

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: 335.49  E-value: 3.17e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489319454   2 LTIGVLGLQGAVREHIHAIEACGAAGLVVKRPEQLNEVDGLILPGGESTTMRRLIDTYQFMEPLREFAAQGKPMFGTCAG 81
Cdd:COG0311    1 MKIGVLALQGDVREHIRALERLGAEVVEVRRPEDLEGLDGLIIPGGESTTIGKLLRRFGLLEPLRERIAAGLPVFGTCAG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489319454  82 LIILAKEIAGSDNPHLGLLNVVVERNSFGRQVDSFEADLTIKGL-DEPFTGVFIRAPHILEAGENVEVLSEHNGRIVAAK 160
Cdd:COG0311   81 LILLAKEIEDPDQPTLGLLDITVRRNAFGRQVDSFEADLDIPGLgDGPFPAVFIRAPYIEEVGPGVEVLATVDGRIVAVR 160

                        170       180       190
                 ....*....|....*....|....*....|.
gi 489319454 161 QGQFLGCSFHPELTEDHRVTQLFVEMVEEYK 191
Cdd:COG0311  161 QGNILATSFHPELTDDLRVHEYFLEMVRGAK 191
SNO pfam01174
SNO glutamine amidotransferase family; This family and its amidotransferase domain was first ...
 6-189 2.85e-106

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: 302.91  E-value: 2.85e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489319454    6 VLGLQGAVREHIHAIEACGAAGLVVKRPEQLNEVDGLILPGGESTTMRRLIDTYQFMEPLREFAAQG-KPMFGTCAGLII 84
Cdd:pfam01174   1 VLALQGAVEEHEEAIKKCGAENKTVKRPEDLAQCDALIIPGGESTAMSLLAKRYGFYEPLYEFVHNPnKPIWGTCAGLIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489319454   85 LAKEIAGSDNPHLGLLNVVVERNSFGRQVDSFEADLTIKGLDEPFTGVFIRAPHILEAG--ENVEVLSEHNGRIVAAKQG 162
Cdd:pfam01174  81 LSKQLGNELVKTLGLLKVTVKRNAFGRQVDSFEKECDFKNLIPKFPGVFIRAPVIEEILdpEVVVVLYELDGKIVVAKQG 160

                         170       180
                  ....*....|....*....|....*...
gi 489319454  163 QFLGCSFHPELTED-HRVTQLFVEMVEE 189
Cdd:pfam01174 161 NILATSFHPELAEDdYRVHDWFVENFVK 188
GATase1_PB cd01749
Glutamine Amidotransferase (GATase_I) involved in pyridoxine biosynthesis; Glutamine ...
 4-184 1.05e-105

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: 300.98  E-value: 1.05e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489319454   4 IGVLGLQGAVREHIHAIEACGAAGLVVKRPEQLNEVDGLILPGGESTTMRRLIDTYQFMEPLREFAAQGKPMFGTCAGLI 83
Cdd:cd01749    1 IGVLALQGDFREHIRALERLGVEVIEVRTPEDLEGIDGLIIPGGESTTIGKLLRRTGLLDPLREFIRAGKPVFGTCAGLI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489319454  84 ILAKEIAGSDN-PHLGLLNVVVERNSFGRQVDSFEADLTIKGLD-EPFTGVFIRAPHILEAGENVEVLSEHNGRIVAAKQ 161
Cdd:cd01749   81 LLAKEVEDQGGqPLLGLLDITVRRNAFGRQVDSFEADLDIPGLGlGPFPAVFIRAPVIEEVGPGVEVLAEYDGKIVAVRQ 160

                        170       180
                 ....*....|....*....|...
gi 489319454 162 GQFLGCSFHPELTEDHRVTQLFV 184
Cdd:cd01749  161 GNVLATSFHPELTDDTRIHEYFL 183
PLP_synth_Pdx2 TIGR03800
pyridoxal 5'-phosphate synthase, glutaminase subunit Pdx2; Pyridoxal 5'-phosphate (PLP) is ...
 4-185 3.12e-103

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: 295.11  E-value: 3.12e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489319454    4 IGVLGLQGAVREHIHAIEACGAAGLVVKRPEQLNEVDGLILPGGESTTMRRLIDTYQFMEPLREFAAQGKPMFGTCAGLI 83
Cdd:TIGR03800   2 IGVLALQGAVREHARALEALGVEGVEVKRPEQLDEIDGLIIPGGESTTISRLLDKYGMFEPLRNFILSGLPVFGTCAGLI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489319454   84 ILAKEIAGSDNPHLGLLNVVVERNSFGRQVDSFEADLTIKGLDE-PFTGVFIRAPHILEAGENVEVLSEHNGRIVAAKQG 162
Cdd:TIGR03800  82 MLAKEIIGQKEGQLGLLDMTVERNAYGRQVDSFEAEVDIKGVGDdPITGVFIRAPKIVSVGNGVEILAKVGNRIVAVRQG 161

                         170       180
                  ....*....|....*....|...
gi 489319454  163 QFLGCSFHPELTEDHRVTQLFVE 185
Cdd:TIGR03800 162 NILVSSFHPELTDDHRVHEYFLE 184
 
Name Accession Description Interval E-value
PRK13525 PRK13525
pyridoxal 5'-phosphate synthase glutaminase subunit PdxT;
1-189 1.22e-127

pyridoxal 5'-phosphate synthase glutaminase subunit PdxT;


Pssm-ID: 237411 [Multi-domain]  Cd Length: 189  Bit Score: 356.78  E-value: 1.22e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489319454   1 MLTIGVLGLQGAVREHIHAIEACGAAGLVVKRPEQLNEVDGLILPGGESTTMRRLIDTYQFMEPLREFAAQGKPMFGTCA 80
Cdd:PRK13525   1 MMKIGVLALQGAVREHLAALEALGAEAVEVRRPEDLDEIDGLILPGGESTTMGKLLRDFGLLEPLREFIASGLPVFGTCA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489319454  81 GLIILAKEIAGSDNPHLGLLNVVVERNSFGRQVDSFEADLTIKGLDEPFTGVFIRAPHILEAGENVEVLSEHNGRIVAAK 160
Cdd:PRK13525  81 GMILLAKEIEGYEQEHLGLLDITVRRNAFGRQVDSFEAELDIKGLGEPFPAVFIRAPYIEEVGPGVEVLATVGGRIVAVR 160

                        170       180
                 ....*....|....*....|....*....
gi 489319454 161 QGQFLGCSFHPELTEDHRVTQLFVEMVEE 189
Cdd:PRK13525 161 QGNILATSFHPELTDDTRVHRYFLEMVKE 189
PdxT COG0311
Pyridoxal 5'-phosphate synthase subunit PdxT (glutamine amidotransferase) [Coenzyme transport ...
 2-191 3.17e-119

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: 335.49  E-value: 3.17e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489319454   2 LTIGVLGLQGAVREHIHAIEACGAAGLVVKRPEQLNEVDGLILPGGESTTMRRLIDTYQFMEPLREFAAQGKPMFGTCAG 81
Cdd:COG0311    1 MKIGVLALQGDVREHIRALERLGAEVVEVRRPEDLEGLDGLIIPGGESTTIGKLLRRFGLLEPLRERIAAGLPVFGTCAG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489319454  82 LIILAKEIAGSDNPHLGLLNVVVERNSFGRQVDSFEADLTIKGL-DEPFTGVFIRAPHILEAGENVEVLSEHNGRIVAAK 160
Cdd:COG0311   81 LILLAKEIEDPDQPTLGLLDITVRRNAFGRQVDSFEADLDIPGLgDGPFPAVFIRAPYIEEVGPGVEVLATVDGRIVAVR 160

                        170       180       190
                 ....*....|....*....|....*....|.
gi 489319454 161 QGQFLGCSFHPELTEDHRVTQLFVEMVEEYK 191
Cdd:COG0311  161 QGNILATSFHPELTDDLRVHEYFLEMVRGAK 191
SNO pfam01174
SNO glutamine amidotransferase family; This family and its amidotransferase domain was first ...
 6-189 2.85e-106

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: 302.91  E-value: 2.85e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489319454    6 VLGLQGAVREHIHAIEACGAAGLVVKRPEQLNEVDGLILPGGESTTMRRLIDTYQFMEPLREFAAQG-KPMFGTCAGLII 84
Cdd:pfam01174   1 VLALQGAVEEHEEAIKKCGAENKTVKRPEDLAQCDALIIPGGESTAMSLLAKRYGFYEPLYEFVHNPnKPIWGTCAGLIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489319454   85 LAKEIAGSDNPHLGLLNVVVERNSFGRQVDSFEADLTIKGLDEPFTGVFIRAPHILEAG--ENVEVLSEHNGRIVAAKQG 162
Cdd:pfam01174  81 LSKQLGNELVKTLGLLKVTVKRNAFGRQVDSFEKECDFKNLIPKFPGVFIRAPVIEEILdpEVVVVLYELDGKIVVAKQG 160

                         170       180
                  ....*....|....*....|....*...
gi 489319454  163 QFLGCSFHPELTED-HRVTQLFVEMVEE 189
Cdd:pfam01174 161 NILATSFHPELAEDdYRVHDWFVENFVK 188
GATase1_PB cd01749
Glutamine Amidotransferase (GATase_I) involved in pyridoxine biosynthesis; Glutamine ...
 4-184 1.05e-105

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: 300.98  E-value: 1.05e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489319454   4 IGVLGLQGAVREHIHAIEACGAAGLVVKRPEQLNEVDGLILPGGESTTMRRLIDTYQFMEPLREFAAQGKPMFGTCAGLI 83
Cdd:cd01749    1 IGVLALQGDFREHIRALERLGVEVIEVRTPEDLEGIDGLIIPGGESTTIGKLLRRTGLLDPLREFIRAGKPVFGTCAGLI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489319454  84 ILAKEIAGSDN-PHLGLLNVVVERNSFGRQVDSFEADLTIKGLD-EPFTGVFIRAPHILEAGENVEVLSEHNGRIVAAKQ 161
Cdd:cd01749   81 LLAKEVEDQGGqPLLGLLDITVRRNAFGRQVDSFEADLDIPGLGlGPFPAVFIRAPVIEEVGPGVEVLAEYDGKIVAVRQ 160

                        170       180
                 ....*....|....*....|...
gi 489319454 162 GQFLGCSFHPELTEDHRVTQLFV 184
Cdd:cd01749  161 GNVLATSFHPELTDDTRIHEYFL 183
PLP_synth_Pdx2 TIGR03800
pyridoxal 5'-phosphate synthase, glutaminase subunit Pdx2; Pyridoxal 5'-phosphate (PLP) is ...
 4-185 3.12e-103

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: 295.11  E-value: 3.12e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489319454    4 IGVLGLQGAVREHIHAIEACGAAGLVVKRPEQLNEVDGLILPGGESTTMRRLIDTYQFMEPLREFAAQGKPMFGTCAGLI 83
Cdd:TIGR03800   2 IGVLALQGAVREHARALEALGVEGVEVKRPEQLDEIDGLIIPGGESTTISRLLDKYGMFEPLRNFILSGLPVFGTCAGLI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489319454   84 ILAKEIAGSDNPHLGLLNVVVERNSFGRQVDSFEADLTIKGLDE-PFTGVFIRAPHILEAGENVEVLSEHNGRIVAAKQG 162
Cdd:TIGR03800  82 MLAKEIIGQKEGQLGLLDMTVERNAYGRQVDSFEAEVDIKGVGDdPITGVFIRAPKIVSVGNGVEILAKVGNRIVAVRQG 161

                         170       180
                  ....*....|....*....|...
gi 489319454  163 QFLGCSFHPELTEDHRVTQLFVE 185
Cdd:TIGR03800 162 NILVSSFHPELTDDHRVHEYFLE 184
PRK13527 PRK13527
glutamine amidotransferase subunit PdxT; Provisional
 2-189 1.39e-90

glutamine amidotransferase subunit PdxT; Provisional


Pssm-ID: 237412 [Multi-domain]  Cd Length: 200  Bit Score: 263.67  E-value: 1.39e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489319454   2 LTIGVLGLQGAVREHIHAIE----ACGAAGLV--VKRPEQLNEVDGLILPGGESTTMRRLIDTYQFMEPLREFAAQGKPM 75
Cdd:PRK13527   1 MKIGVLALQGDVEEHIDALKraldELGIDGEVveVRRPGDLPDCDALIIPGGESTTIGRLMKREGILDEIKEKIEEGLPI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489319454  76 FGTCAGLIILAKE-----IAGSDNPHLGLLNVVVERNSFGRQVDSFEADLTIKGLDEPFTGVFIRAPHILEAGENVEVLS 150
Cdd:PRK13527  81 LGTCAGLILLAKEvgddrVTKTEQPLLGLMDVTVKRNAFGRQRDSFEAEIDLSGLDGPFHAVFIRAPAITKVGGDVEVLA 160

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 489319454 151 EHNGRIVAAKQGQFLGCSFHPELTEDHRVTQLFVEMVEE 189
Cdd:PRK13527 161 KLDDRIVAVEQGNVLATAFHPELTDDTRIHEYFLKKVKG 199
PLN02832 PLN02832
glutamine amidotransferase subunit of pyridoxal 5'-phosphate synthase complex
 1-194 1.41e-73

glutamine amidotransferase subunit of pyridoxal 5'-phosphate synthase complex


Pssm-ID: 215446 [Multi-domain]  Cd Length: 248  Bit Score: 222.28  E-value: 1.41e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489319454   1 MLTIGVLGLQGAVREHIHAIEACGAAGLVVKRPEQLNEVDGLILPGGESTTMRRLIDTYQFMEPLREFAAQGKPMFGTCA 80
Cdd:PLN02832   1 MMAIGVLALQGSFNEHIAALRRLGVEAVEVRKPEQLEGVSGLIIPGGESTTMAKLAERHNLFPALREFVKSGKPVWGTCA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489319454  81 GLIILA-KEIAGSDNPH--LGLLNVVVERNSFGRQVDSFEADLTIK------GLDEPFTGVFIRAPHILEAGENVEVLSE 151
Cdd:PLN02832  81 GLIFLAeRAVGQKEGGQelLGGLDCTVHRNFFGSQINSFETELPVPelaaseGGPETFRAVFIRAPAILSVGPGVEVLAE 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489319454 152 H------------------NGRIVAAKQGQFLGCSFHPELTEDHRVTQLFVEMVEEYKQKA 194
Cdd:PLN02832 161 YplpsekalyssstdaegrDKVIVAVKQGNLLATAFHPELTADTRWHSYFVKMVSESEEYA 221
PRK13526 PRK13526
glutamine amidotransferase subunit PdxT; Provisional
 3-186 1.56e-50

glutamine amidotransferase subunit PdxT; Provisional


Pssm-ID: 184113 [Multi-domain]  Cd Length: 179  Bit Score: 161.27  E-value: 1.56e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489319454   3 TIGVLGLQGAVREHIHAIEACGAAGLVVKRPEQLNEVDGLILPGGESTTMRRLIDTYQFMEPLREFAAQgKPMFGTCAGL 82
Cdd:PRK13526   4 KVGVLAIQGGYQKHADMFKSLGVEVKLVKFNNDFDSIDRLVIPGGESTTLLNLLNKHQIFDKLYNFCSS-KPVFGTCAGS 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489319454  83 IILAKeiaGSDnpHLGLLNVVVERNSFGRQVDSFEADLTIkgLDEPFTGVFIRAPHILEAGENVEVLSEHNGRIVAAKQG 162
Cdd:PRK13526  83 IILSK---GEG--YLNLLDLEVQRNAYGRQVDSFVADISF--NDKNITGVFIRAPKFIVVGNQVDILSKYQNSPVLLRQA 155

                        170       180
                 ....*....|....*....|....
gi 489319454 163 QFLGCSFHPELTEDHRVTQLFVEM 186
Cdd:PRK13526 156 NILVSSFHPELTQDPTVHEYFLAM 179
GATase1_IGP_Synthase cd01748
Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate ...
 19-172 2.38e-11

Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate synthase (IGPS); Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate synthase (IGPS). IGPS incorporates ammonia derived from glutamine into N1-[(5'-phosphoribulosyl)-formimino]-5-aminoimidazole-4-carboxamide ribonucleotide (PRFAR) to form 5'-(5-aminoimidazole-4-carboxamide) ribonucleotide (AICAR) and imidazole glycerol phosphate (IGP). The glutamine amidotransferase domain generates the ammonia nucleophile which is channeled from the glutaminase active site to the PRFAR active site. IGPS belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site.


Pssm-ID: 153219 [Multi-domain]  Cd Length: 198  Bit Score: 59.82  E-value: 2.38e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489319454  19 AIEACGAAGLVVKRPEQLNEVDGLILPG-GE-STTMRRLIDTyQFMEPLREFAAQGKPMFGTCAGLIILAKEiaGSDNPH 96
Cdd:cd01748   17 ALERLGAEVIITSDPEEILSADKLILPGvGAfGDAMANLRER-GLIEALKEAIASGKPFLGICLGMQLLFES--SEEGGG 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489319454  97 ---LGLLNVVVER--NSFGR--------QVDSFEADLTIKGLDEPFTGVFIrapH----ILEAGENVEVLSEHNGRIVAA 159
Cdd:cd01748   94 tkgLGLIPGKVVRfpASEGLkvphmgwnQLEITKESPLFKGIPDGSYFYFV---HsyyaPPDDPDYILATTDYGGKFPAA 170

                        170
                 ....*....|....
gi 489319454 160 -KQGQFLGCSFHPE 172
Cdd:cd01748  171 vEKDNIFGTQFHPE 184
GATase1_CobB cd03130
Type 1 glutamine amidotransferase (GATase1) domain found in Cobyrinic Acid a,c-Diamide ...
 14-105 1.10e-10

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: 57.99  E-value: 1.10e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489319454  14 REHIHAIEACGAAglVVK----RPEQLNEVDGLILPGG--EsTTMRRLIDTYQFMEPLREFAAQGKPMFGTCAGLIILAK 87
Cdd:cd03130   14 PENLELLEAAGAE--LVPfsplKDEELPDADGLYLGGGypE-LFAEELSANQSMRESIRAFAESGGPIYAECGGLMYLGE 90

                         90       100
                 ....*....|....*....|.
gi 489319454  88 EIAGSDN---PHLGLLNVVVE 105
Cdd:cd03130   91 SLDDEEGqsyPMAGVLPGDAR 111
GATase_3 pfam07685
CobB/CobQ-like glutamine amidotransferase domain;
37-105 1.64e-09

CobB/CobQ-like glutamine amidotransferase domain;


Pssm-ID: 429595 [Multi-domain]  Cd Length: 189  Bit Score: 54.94  E-value: 1.64e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489319454   37 NEVDGLILPGGESTT-MRRLIDTYQFMEPLREFAAQGKPMFGTCAGLIILAKEIAGSDN---PHLGLLNVVVE 105
Cdd:pfam07685  41 PDADLIILPGGKPTIqDLALLRNSGMDEAIKEAAEDGGPVLGICGGYQMLGETIEDPEGvriEGLGLLDIETV 113
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 12-85 1.07e-08

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: 50.66  E-value: 1.07e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489319454  12 AVREHIHAIEACGAAGLVVKRPEQLNEVDGLILPGGESTTMRRLIDTyQFMEPLREFAAQGKPMFGTCAGLIIL 85
Cdd:cd03128   20 ALREAGAEVDVVSPDGGPVESDVDLDDYDGLILPGGPGTPDDLAWDE-ALLALLREAAAAGKPVLGICLGAQLL 92
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 12-85 1.16e-08

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: 51.06  E-value: 1.16e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489319454  12 AVREHIHAIEACGAAGLVVKRPEQLNEVDGLILPGGESTTMRRLIDtYQFMEPLREFAAQGKPMFGTCAGLIIL 85
Cdd:cd01653   20 ALREAGAEVDVVSPDGGPVESDVDLDDYDGLILPGGPGTPDDLARD-EALLALLREAAAAGKPILGICLGAQLL 92
GATase1_CobQ cd01750
Type 1 glutamine amidotransferase (GATase1) domain found in Cobyric Acid Synthase (CobQ); Type ...
 29-124 1.55e-07

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: 49.55  E-value: 1.55e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489319454  29 VVKRPEQLNEVDGLILPGGESTTmRRLI--DTYQFMEPLREFAAQGKPMFGTCAGLIILAKEI-------AGSDNPHLGL 99
Cdd:cd01750   28 YVEVPEGLGDADLIILPGSKDTI-QDLAwlRKRGLAEAIKNYARAGGPVLGICGGYQMLGKYIvdpegveGPGEIEGLGL 106

                         90       100       110
                 ....*....|....*....|....*....|..
gi 489319454 100 LNVV-------VERNSFGRqVDSFEADLTIKG 124
Cdd:cd01750  107 LDVEtefgpekTTRRVTGR-LDEEGEGGEVTG 137
PLN02617 PLN02617
imidazole glycerol phosphate synthase hisHF
 11-172 3.27e-07

imidazole glycerol phosphate synthase hisHF


Pssm-ID: 178226 [Multi-domain]  Cd Length: 538  Bit Score: 49.71  E-value: 3.27e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489319454  11 GAVREHIHAIEACGAAGLVVKRPEQLNEVDGLILPGGES--TTMRRLIDTyQFMEPLREFAAQGKPMFGTCAGLIIL--- 85
Cdd:PLN02617  17 GNVRSVRNAIRHLGFTIKDVQTPEDILNADRLIFPGVGAfgSAMDVLNNR-GMAEALREYIQNDRPFLGICLGLQLLfes 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489319454  86 AKEIAGSDNphLGLLNVVVER--NSFGRQVDSFEADLTIKGLDEP-FTGV------FIRAPHILEAGENVE-VLS--EHN 153
Cdd:PLN02617  96 SEENGPVEG--LGVIPGVVGRfdSSNGLRVPHIGWNALQITKDSElLDGVggrhvyFVHSYRATPSDENKDwVLAtcNYG 173

                        170       180
                 ....*....|....*....|
gi 489319454 154 GRIVAAKQ-GQFLGCSFHPE 172
Cdd:PLN02617 174 GEFIASVRkGNVHAVQFHPE 193
GATase1_1 cd01741
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 33-172 5.14e-07

Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group contains a subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain. GATase activity catalyses the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. Glutamine amidotransferases (GATase) includes the triad family of amidotransferases which have a conserved Cys-His-Glu catalytic triad in the glutaminase active site. In this subgroup this triad is conserved. GATase activity can be found in a range of biosynthetic enzymes, including: 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. Glutamine amidotransferase (GATase) domains can occur either as single polypeptides, as in glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase.


Pssm-ID: 153212 [Multi-domain]  Cd Length: 188  Bit Score: 48.01  E-value: 5.14e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489319454  33 PEQLNEVDGLILPGGESTTMrrlIDTYQFMEPLREF----AAQGKPMFGTCAGLIILAKeiagsdnpHLGllnVVVERNS 108
Cdd:cd01741   41 LPDLDDYDGLVILGGPMSVD---EDDYPWLKKLKELirqaLAAGKPVLGICLGHQLLAR--------ALG---GKVGRNP 106

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489319454 109 FGRQVDSFEADLTIKGLDEPFTGVFIRAPHILEA-GENVEVL---------SEHNGRIVAAKQGQFLGCSFHPE 172
Cdd:cd01741  107 KGWEIGWFPVTLTEAGKADPLFAGLPDEFPVFHWhGDTVVELppgavllasSEACPNQAFRYGDRALGLQFHPE 180
hisH PRK13181
imidazole glycerol phosphate synthase subunit HisH; Provisional
 19-106 2.68e-06

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 183878 [Multi-domain]  Cd Length: 199  Bit Score: 46.01  E-value: 2.68e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489319454  19 AIEACGAAGLVVKRPEQLNEVDGLILPG-GE-STTMRRLIDTyQFMEPLREFAAQGKPMFGTCAGLIILAKEIAGSDNPH 96
Cdd:PRK13181  18 ALKRLGVEAVVSSDPEEIAGADKVILPGvGAfGQAMRSLRES-GLDEALKEHVEKKQPVLGICLGMQLLFESSEEGNVKG 96

                         90
                 ....*....|
gi 489319454  97 LGLLNVVVER 106
Cdd:PRK13181  97 LGLIPGDVKR 106
hisH PRK13143
imidazole glycerol phosphate synthase subunit HisH; Provisional
 19-106 2.83e-06

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237289 [Multi-domain]  Cd Length: 200  Bit Score: 46.01  E-value: 2.83e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489319454  19 AIEACGAAGLVVKRPEQLNEVDGLILPG-GE-STTMRRLIdtyQFMEPLREFAAQGKPMFGTCAGLIIL---AKEiaGSD 93
Cdd:PRK13143  19 ALERAGAEVVITSDPEEILDADGIVLPGvGAfGAAMENLS---PLRDVILEAARSGKPFLGICLGMQLLfesSEE--GGG 93

                         90
                 ....*....|...
gi 489319454  94 NPHLGLLNVVVER 106
Cdd:PRK13143  94 VRGLGLFPGRVVR 106
PRK01077 PRK01077
cobyrinate a,c-diamide synthase;
15-104 7.47e-06

cobyrinate a,c-diamide synthase;


Pssm-ID: 234896 [Multi-domain]  Cd Length: 451  Bit Score: 45.51  E-value: 7.47e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489319454  15 EHIHAIEACGAAgLVVKRP---EQLNEVDGLILPGG----------ESTTMRRLIdtyqfmeplREFAAQGKPMFGTCAG 81
Cdd:PRK01077 262 ENLELLRAAGAE-LVFFSPladEALPDCDGLYLGGGypelfaaelaANTSMRASI---------RAAAAAGKPIYAECGG 331

                         90       100
                 ....*....|....*....|....*.
gi 489319454  82 LIILAKEI---AGSDNPHLGLLNVVV 104
Cdd:PRK01077 332 LMYLGESLedaDGERHPMVGLLPGEA 357
GAT1_Peptidase_E_like cd03129
Type 1 glutamine amidotransferase (GATase1)-like domain found in peptidase E_like proteins; ...
 11-127 1.99e-05

Type 1 glutamine amidotransferase (GATase1)-like domain found in peptidase E_like proteins; Type 1 glutamine amidotransferase (GATase1)-like domain found in peptidase E_like proteins. This group contains proteins similar to the aspartyl dipeptidases Salmonella typhimurium peptidase E and Xenopus laevis peptidase E and, extracellular cyanophycinases from Pseudomonas anguilliseptica BI (CphE) and Synechocystis sp. PCC 6803 CphB. In bacteria peptidase E is believed to play a role in degrading peptides generated by intracellular protein breakdown or imported into the cell as nutrient sources. Peptidase E uniquely hydrolyses only Asp-X dipeptides (where X is any amino acid), and one tripeptide Asp-Gly-Gly. Cyanophycinases are intracellular exopeptidases which hydrolyze the polymer cyanophycin (multi L-arginyl-poly-L-aspartic acid) to the dipeptide beta-Asp-Arg. Peptidase E and cyanophycinases are thought to have a Ser-His-Glu catalytic triad which differs from the Cys-His-Glu catalytic triad typical of GATase1 domains by having a Ser in place of the reactive Cys at the nucleophile elbow. Xenopus peptidase E is developmentally regulated in response to thyroid hormone and, it is thought to play a role in apoptosis during tail reabsorption.


Pssm-ID: 153223 [Multi-domain]  Cd Length: 210  Bit Score: 43.45  E-value: 1.99e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489319454  11 GAVREHIHAIEACGAAGLVvkrpEQLNEVDGLILPGGESTTMRRLIDTYQFMEPLREFAAQGKPMFGTCAGLIILAKEIA 90
Cdd:cd03129   57 GVEVVHLLLIDTANDPDVV----ARLLEADGIFVGGGNQLRLLSVLRETPLLDAILKRVARGVVIGGTSAGAAVMGETGI 132

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 489319454  91 GSDN----------PHLGLLNVVV-----ERNSFGR---QVDSFEADLTIkGLDE 127
Cdd:cd03129  133 GTTPsepevtppmaPGLGLLPGIIdphfdSRGREGRlleLLAANPTPLGI-GIDE 186
hisH CHL00188
imidazole glycerol phosphate synthase subunit hisH; Provisional
 19-106 2.14e-05

imidazole glycerol phosphate synthase subunit hisH; Provisional


Pssm-ID: 214389 [Multi-domain]  Cd Length: 210  Bit Score: 43.34  E-value: 2.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489319454  19 AIEACGAAGLVVKRPEQLNEVDGLILPGGES--TTMRRLiDTYQFMEPLREFAAQGKPMFGTCAGLIILAKEIAGSDNPH 96
Cdd:CHL00188  20 AIQQAGQQPCIINSESELAQVHALVLPGVGSfdLAMKKL-EKKGLITPIKKWIAEGNPFIGICLGLHLLFETSEEGKEEG 98

                         90
                 ....*....|
gi 489319454  97 LGLLNVVVER 106
Cdd:CHL00188  99 LGIYKGQVKR 108
PRK06278 PRK06278
cobyrinic acid a,c-diamide synthase; Validated
 37-102 1.53e-04

cobyrinic acid a,c-diamide synthase; Validated


Pssm-ID: 180505 [Multi-domain]  Cd Length: 476  Bit Score: 41.56  E-value: 1.53e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489319454  37 NEVDGLILPGG---ESTTMrrlidTYQFMEPLREFaaqGKPMFGTCAGLIILAKEI---AGSDNP----HLGLLNV 102
Cdd:PRK06278  35 KDLDGLIIPGGslvESGSL-----TDELKKEILNF---DGYIIGICSGFQILSEKIdigRKSPVPiikeGLGLLDV 102
COG3442 COG3442
Glutamine amidotransferase related to the GATase domain of CobQ [General function prediction ...
 38-131 1.69e-04

Glutamine amidotransferase related to the GATase domain of CobQ [General function prediction only];


Pssm-ID: 442666 [Multi-domain]  Cd Length: 241  Bit Score: 40.93  E-value: 1.69e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489319454  38 EVDGLILPGGESTTMRRLI-DTYQFMEPLREFAAQGKPMFGTCAGLIILAKEI---AGSDNPHLGLLNVVVERNSfGRQV 113
Cdd:COG3442   50 DVDIVFIGGGQDREQEIVAdDLLRIKDALRAAIEDGVPVLAICGGYQLLGHYYetaDGERIPGLGILDVYTVAGK-KRLI 128

                         90
                 ....*....|....*...
gi 489319454 114 DSFEADLTIKGLDEPFTG 131
Cdd:COG3442  129 GNVVVETELNGEFGTLVG 146
GATase1_PfpI_3 cd03140
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ...
 36-101 4.37e-04

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: 39.13  E-value: 4.37e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489319454  36 LNEVDGLILPGGESTTMRRLIDTYQFmepLREFAAQGKPMFGTCAGLIILAKEiagsdnphlGLLN 101
Cdd:cd03140   58 PEDYDLLILPGGDSWDNPEAPDLAGL---VRQALKQGKPVAAICGATLALARA---------GLLN 111
GATase pfam00117
Glutamine amidotransferase class-I;
17-184 4.54e-04

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 39.53  E-value: 4.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489319454   17 IHAIEACGAAGLVVKRPEQLNEV-----DGLILPGGESTtmRRLIDtyQFMEPLREFAAQGKPMFGTCAGLIILAKEIAG 91
Cdd:pfam00117  14 ARALRELGVEVTVVPNDTPAEEIleenpDGIILSGGPGS--PGAAG--GAIEAIREARELKIPILGICLGHQLLALAFGG 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489319454   92 -----SDNPHLGllnvvveRNSfgrQVDSFEADLTiKGLDEPFTgvfIRAPH-------ILEAGENVEVLSEHNGRIVAA 159
Cdd:pfam00117  90 kvvkaKKFGHHG-------KNS---PVGDDGCGLF-YGLPNVFI---VRRYHsyavdpdTLPDGLEVTATSENDGTIMGI 155

                         170       180       190
                  ....*....|....*....|....*....|
gi 489319454  160 --KQGQFLGCSFHPELT---EDHRVTQLFV 184
Cdd:pfam00117 156 rhKKLPIFGVQFHPESIltpHGPEILFNFF 185
GATase1_PfpI_like cd03134
A type 1 glutamine amidotransferase (GATase1)-like domain found in PfpI from Pyrococcus ...
 37-85 5.18e-04

A type 1 glutamine amidotransferase (GATase1)-like domain found in PfpI from Pyrococcus furiosus; A type 1 glutamine amidotransferase (GATase1)-like domain found in PfpI from Pyrococcus furiosus. This group includes proteins similar to PfpI from P. furiosus. and PH1704 from Pyrococcus horikoshii. These enzymes are ATP-independent intracellular proteases and 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. For PH1704, it is believed that this Cys together with a different His in one monomer and Glu (from an adjacent monomer) forms a different catalytic triad from the typical GATase1domain. PfpI is homooligomeric. Protease activity is only found for oligomeric forms of PH1704.


Pssm-ID: 153228 [Multi-domain]  Cd Length: 165  Bit Score: 39.06  E-value: 5.18e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 489319454  37 NEVDGLILPGGES-TTMRRLIDTYQFmepLREFAAQGKPMFGTCAGLIIL 85
Cdd:cd03134   61 DDYDALVIPGGTNpDKLRRDPDAVAF---VRAFAEAGKPVAAICHGPWVL 107
YajL COG0693
Protein/nucleotide deglycase, PfpI/YajL/DJ-1 family (repair of methylglyoxal-glycated proteins ...
 24-124 8.74e-04

Protein/nucleotide deglycase, PfpI/YajL/DJ-1 family (repair of methylglyoxal-glycated proteins and nucleic acids) [Defense mechanisms];


Pssm-ID: 440457 [Multi-domain]  Cd Length: 170  Bit Score: 38.55  E-value: 8.74e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489319454  24 GAAGLVVKRPEQLNEV-----DGLILPGGeSTTMRRLIDTYQFMEPLREFAAQGKPMFGTCAGLIILAkeiagsdnpHLG 98
Cdd:COG0693   45 SKHGITVTADKTLDDVdpddyDALVLPGG-HGAPDDLREDPDVVALVREFYEAGKPVAAICHGPAVLA---------AAG 114

                         90       100
                 ....*....|....*....|....*....
gi 489319454  99 LLNvvvernsfGRQV---DSFEADLTIKG 124
Cdd:COG0693  115 LLK--------GRKVtsfPNIEDDLKNAG 135
PfpI TIGR01382
intracellular protease, PfpI family; The member of this family from Pyrococcus horikoshii has ...
 18-91 8.83e-04

intracellular protease, PfpI family; The member of this family from Pyrococcus horikoshii has been solved to 2 Angstrom resolution. It is an ATP-independent intracellular protease that crystallizes as a hexameric ring. Cys-101 is proposed as the active site residue in a catalytic triad with the adjacent His-102 and a Glu residue from an adjacent monomer. A member of this family from Bacillus subtilis, GSP18, has been shown to be expressed in response to several forms of stress. A role in the degradation of small peptides has been suggested. A closely related family consists of the thiamine biosynthesis protein ThiJ and its homologs. [Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 273591 [Multi-domain]  Cd Length: 166  Bit Score: 38.17  E-value: 8.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489319454   18 HAIEACGAAGLVVKRPEQL------------NEVDGLILPGGESTTMRRLIDtyQFMEPLREFAAQGKPMFGTCAG--LI 83
Cdd:TIGR01382  28 EVDTVSKEAGTTVGKHGYSvtvdatidevnpEEYDALVIPGGRAPEYLRLNN--KAVRLVREFVEKGKPVAAICHGpqLL 105


                  ....*...
gi 489319454   84 ILAKEIAG 91
Cdd:TIGR01382 106 ISAGVLRG 113
GATase1_FGAR_AT cd01740
Type 1 glutamine amidotransferase (GATase1)-like domain found in Formylglycinamide ...
 14-158 1.10e-03

Type 1 glutamine amidotransferase (GATase1)-like domain found in Formylglycinamide ribonucleotide amidotransferase; Type 1 glutamine amidotransferase (GATase1)-like domain found in Formylglycinamide ribonucleotide amidotransferase (FGAR-AT). FGAR-AT catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to formylglycinamidine ribonucleotide (FGAM), ADP, Pi, and glutamate in the fourth step of the purine biosynthetic pathway. FGAR-AT is a glutamine amidotransferase. Glutamine amidotransferase activity catalyses the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. FGAR-AT belongs to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site


Pssm-ID: 153211 [Multi-domain]  Cd Length: 238  Bit Score: 38.75  E-value: 1.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489319454  14 REHIHAIEACGAAGLVV------KRPEQLNEVDGLILPGGES------------TTMRRlidtyqfMEPLREFAAQGKPM 75
Cdd:cd01740   13 RDMAYAFELAGFEAEDVwhndllAGRKDLDDYDGVVLPGGFSygdylragaiaaASPLL-------MEEVKEFAERGGLV 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489319454  76 FGTCAGLIILAKeiagsdnphLGLLNVVVERNSFGRQVDSFEAD---LTIKGLDEPFTGVFiraphilEAGENVEVLSEH 152
Cdd:cd01740   86 LGICNGFQILVE---------LGLLPGALIRNKGLKFICRWQNRfvtLRVENNDSPFTKGY-------MEGEVLRIPVAH 149


                 ....*..
gi 489319454 153 N-GRIVA 158
Cdd:cd01740  150 GeGRFYA 156
GATase1_PfpI_1 cd03169
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ...
 40-86 1.15e-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: 153243 [Multi-domain]  Cd Length: 180  Bit Score: 38.01  E-value: 1.15e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 489319454  40 DGLILPGGESTTMRRLIDtyQFMEPLREFAAQGKPMFGTCAGLIILA 86
Cdd:cd03169   78 DALVIPGGRAPEYLRLDE--KVLAIVRHFAEANKPVAAICHGPQILA 122
DJ-1_PfpI pfam01965
DJ-1/PfpI family; The family includes the protease PfpI. This domain is also found in ...
 40-87 6.03e-03

DJ-1/PfpI family; The family includes the protease PfpI. This domain is also found in transcriptional regulators.


Pssm-ID: 396514 [Multi-domain]  Cd Length: 165  Bit Score: 36.08  E-value: 6.03e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 489319454   40 DGLILPGGESTTmRRLIDTYQFMEPLREFAAQGKPMFGTCAGLIILAK 87
Cdd:pfam01965  63 DALVLPGGRAGP-ERLRDNEKLVEFVKDFYEKGKPVAAICHGPQVLAA 109
Peptidase_C26 pfam07722
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ...
 24-97 9.00e-03

Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze the cleavage of the gamma-glutamyl bond in poly-gamma-glutamyl substrates. They are structurally related to pfam00117, but contain extensions in four loops and at the C terminus.


Pssm-ID: 429620 [Multi-domain]  Cd Length: 219  Bit Score: 35.70  E-value: 9.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489319454   24 GAAGLVVKRP---------EQLNEVDGLILPGG--------------ESTTMRRLIDTYQFMEpLREFAAQGKPMFGTCA 80
Cdd:pfam07722  35 GAGGLPVLLPilgdpedaaAILDRLDGLLLTGGpnvdphfygeepseSGGPYDPARDAYELAL-IRAALARGKPILGICR 113

                          90
                  ....*....|....*..
gi 489319454   81 GLIILAKEIAGSDNPHL 97
Cdd:pfam07722 114 GFQLLNVALGGTLYQDI 130
Peptidase_S51 pfam03575
Peptidase family S51;
6-93 9.10e-03

Peptidase family S51;


Pssm-ID: 397574 [Multi-domain]  Cd Length: 206  Bit Score: 35.74  E-value: 9.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489319454    6 VLGLQGAVREHIHaieacgaaglVVKRPEQ-----LNEVDGLILPGGESTTMRRLIDTYQFMEPLREFAAQGKPMFGTCA 80
Cdd:pfam03575  55 ALEKLGCEVDGLH----------LSTDPLAeieekLLEADGIYVGGGNTFHLLKLLYETGLDKIIREAVQAGLPYIGWSA 124

                          90
                  ....*....|...
gi 489319454   81 GLIILAKEIAGSD 93
Cdd:pfam03575 125 GANVAGPSIITTS 137
 
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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