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Conserved domains on  [gi|500857555|ref|WP_012009059|]
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pyridoxal 5'-phosphate synthase glutaminase subunit PdxT [Bacillus pumilus]

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
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;
1-188 1.56e-121

pyridoxal 5'-phosphate synthase glutaminase subunit PdxT;


:

Pssm-ID: 237411 [Multi-domain]  Cd Length: 189  Bit Score: 341.37  E-value: 1.56e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857555   1 MLTIGVLGLQGAVREHIQSIEACGAEGKIIKRAEELVSVDGLIIPGGESTTMRRLMDTYQFIEPIKAFAAKGKPIFGTCA 80
Cdd:PRK13525   1 MMKIGVLALQGAVREHLAALEALGAEAVEVRRPEDLDEIDGLILPGGESTTMGKLLRDFGLLEPLREFIASGLPVFGTCA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857555  81 GLIMLAKHIEDRDNAHLGLLNVSVARNSFGRQVDSFEADLEVKGLDAPFTGVFIRAPHIISADESVEVMAEYDGRIVMAK 160
Cdd:PRK13525  81 GMILLAKEIEGYEQEHLGLLDITVRRNAFGRQVDSFEAELDIKGLGEPFPAVFIRAPYIEEVGPGVEVLATVGGRIVAVR 160
                        170       180
                 ....*....|....*....|....*...
gi 500857555 161 ENNILGCSFHPELTDDHRLTQLFVEMVK 188
Cdd:PRK13525 161 QGNILATSFHPELTDDTRVHRYFLEMVK 188
 
Name Accession Description Interval E-value
PRK13525 PRK13525
pyridoxal 5'-phosphate synthase glutaminase subunit PdxT;
1-188 1.56e-121

pyridoxal 5'-phosphate synthase glutaminase subunit PdxT;


Pssm-ID: 237411 [Multi-domain]  Cd Length: 189  Bit Score: 341.37  E-value: 1.56e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857555   1 MLTIGVLGLQGAVREHIQSIEACGAEGKIIKRAEELVSVDGLIIPGGESTTMRRLMDTYQFIEPIKAFAAKGKPIFGTCA 80
Cdd:PRK13525   1 MMKIGVLALQGAVREHLAALEALGAEAVEVRRPEDLDEIDGLILPGGESTTMGKLLRDFGLLEPLREFIASGLPVFGTCA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857555  81 GLIMLAKHIEDRDNAHLGLLNVSVARNSFGRQVDSFEADLEVKGLDAPFTGVFIRAPHIISADESVEVMAEYDGRIVMAK 160
Cdd:PRK13525  81 GMILLAKEIEGYEQEHLGLLDITVRRNAFGRQVDSFEAELDIKGLGEPFPAVFIRAPYIEEVGPGVEVLATVGGRIVAVR 160
                        170       180
                 ....*....|....*....|....*...
gi 500857555 161 ENNILGCSFHPELTDDHRLTQLFVEMVK 188
Cdd:PRK13525 161 QGNILATSFHPELTDDTRVHRYFLEMVK 188
PdxT COG0311
Pyridoxal 5'-phosphate synthase subunit PdxT (glutamine amidotransferase) [Coenzyme transport ...
2-191 9.93e-116

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: 326.64  E-value: 9.93e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857555   2 LTIGVLGLQGAVREHIQSIEACGAEGKIIKRAEELVSVDGLIIPGGESTTMRRLMDTYQFIEPIKAFAAKGKPIFGTCAG 81
Cdd:COG0311    1 MKIGVLALQGDVREHIRALERLGAEVVEVRRPEDLEGLDGLIIPGGESTTIGKLLRRFGLLEPLRERIAAGLPVFGTCAG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857555  82 LIMLAKHIEDRDNAHLGLLNVSVARNSFGRQVDSFEADLEVKGL-DAPFTGVFIRAPHIISADESVEVMAEYDGRIVMAK 160
Cdd:COG0311   81 LILLAKEIEDPDQPTLGLLDITVRRNAFGRQVDSFEADLDIPGLgDGPFPAVFIRAPYIEEVGPGVEVLATVDGRIVAVR 160
                        170       180       190
                 ....*....|....*....|....*....|.
gi 500857555 161 ENNILGCSFHPELTDDHRLTQLFVEMVKTYK 191
Cdd:COG0311  161 QGNILATSFHPELTDDLRVHEYFLEMVRGAK 191
GATase1_PB cd01749
Glutamine Amidotransferase (GATase_I) involved in pyridoxine biosynthesis; Glutamine ...
4-184 1.28e-101

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: 290.58  E-value: 1.28e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857555   4 IGVLGLQGAVREHIQSIEACGAEGKIIKRAEELVSVDGLIIPGGESTTMRRLMDTYQFIEPIKAFAAKGKPIFGTCAGLI 83
Cdd:cd01749    1 IGVLALQGDFREHIRALERLGVEVIEVRTPEDLEGIDGLIIPGGESTTIGKLLRRTGLLDPLREFIRAGKPVFGTCAGLI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857555  84 MLAKHIED-RDNAHLGLLNVSVARNSFGRQVDSFEADLEVKGLD-APFTGVFIRAPHIISADESVEVMAEYDGRIVMAKE 161
Cdd:cd01749   81 LLAKEVEDqGGQPLLGLLDITVRRNAFGRQVDSFEADLDIPGLGlGPFPAVFIRAPVIEEVGPGVEVLAEYDGKIVAVRQ 160
                        170       180
                 ....*....|....*....|...
gi 500857555 162 NNILGCSFHPELTDDHRLTQLFV 184
Cdd:cd01749  161 GNVLATSFHPELTDDTRIHEYFL 183
PLP_synth_Pdx2 TIGR03800
pyridoxal 5'-phosphate synthase, glutaminase subunit Pdx2; Pyridoxal 5'-phosphate (PLP) is ...
4-185 2.59e-96

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


Pssm-ID: 274792 [Multi-domain]  Cd Length: 184  Bit Score: 277.39  E-value: 2.59e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857555    4 IGVLGLQGAVREHIQSIEACGAEGKIIKRAEELVSVDGLIIPGGESTTMRRLMDTYQFIEPIKAFAAKGKPIFGTCAGLI 83
Cdd:TIGR03800   2 IGVLALQGAVREHARALEALGVEGVEVKRPEQLDEIDGLIIPGGESTTISRLLDKYGMFEPLRNFILSGLPVFGTCAGLI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857555   84 MLAKHIEDRDNAHLGLLNVSVARNSFGRQVDSFEADLEVKGL-DAPFTGVFIRAPHIISADESVEVMAEYDGRIVMAKEN 162
Cdd:TIGR03800  82 MLAKEIIGQKEGQLGLLDMTVERNAYGRQVDSFEAEVDIKGVgDDPITGVFIRAPKIVSVGNGVEILAKVGNRIVAVRQG 161
                         170       180
                  ....*....|....*....|...
gi 500857555  163 NILGCSFHPELTDDHRLTQLFVE 185
Cdd:TIGR03800 162 NILVSSFHPELTDDHRVHEYFLE 184
SNO pfam01174
SNO glutamine amidotransferase family; This family and its amidotransferase domain was first ...
6-187 2.53e-89

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: 259.77  E-value: 2.53e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857555    6 VLGLQGAVREHIQSIEACGAEGKIIKRAEELVSVDGLIIPGGESTTMRRLMDTYQFIEPIKAFAAKG-KPIFGTCAGLIM 84
Cdd:pfam01174   1 VLALQGAVEEHEEAIKKCGAENKTVKRPEDLAQCDALIIPGGESTAMSLLAKRYGFYEPLYEFVHNPnKPIWGTCAGLIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857555   85 LAKHIEDRDNAHLGLLNVSVARNSFGRQVDSFEADLEVKGLDAPFTGVFIRAPHI--ISADESVEVMAEYDGRIVMAKEN 162
Cdd:pfam01174  81 LSKQLGNELVKTLGLLKVTVKRNAFGRQVDSFEKECDFKNLIPKFPGVFIRAPVIeeILDPEVVVVLYELDGKIVVAKQG 160
                         170       180
                  ....*....|....*....|....*.
gi 500857555  163 NILGCSFHPELT-DDHRLTQLFVEMV 187
Cdd:pfam01174 161 NILATSFHPELAeDDYRVHDWFVENF 186
 
Name Accession Description Interval E-value
PRK13525 PRK13525
pyridoxal 5'-phosphate synthase glutaminase subunit PdxT;
1-188 1.56e-121

pyridoxal 5'-phosphate synthase glutaminase subunit PdxT;


Pssm-ID: 237411 [Multi-domain]  Cd Length: 189  Bit Score: 341.37  E-value: 1.56e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857555   1 MLTIGVLGLQGAVREHIQSIEACGAEGKIIKRAEELVSVDGLIIPGGESTTMRRLMDTYQFIEPIKAFAAKGKPIFGTCA 80
Cdd:PRK13525   1 MMKIGVLALQGAVREHLAALEALGAEAVEVRRPEDLDEIDGLILPGGESTTMGKLLRDFGLLEPLREFIASGLPVFGTCA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857555  81 GLIMLAKHIEDRDNAHLGLLNVSVARNSFGRQVDSFEADLEVKGLDAPFTGVFIRAPHIISADESVEVMAEYDGRIVMAK 160
Cdd:PRK13525  81 GMILLAKEIEGYEQEHLGLLDITVRRNAFGRQVDSFEAELDIKGLGEPFPAVFIRAPYIEEVGPGVEVLATVGGRIVAVR 160
                        170       180
                 ....*....|....*....|....*...
gi 500857555 161 ENNILGCSFHPELTDDHRLTQLFVEMVK 188
Cdd:PRK13525 161 QGNILATSFHPELTDDTRVHRYFLEMVK 188
PdxT COG0311
Pyridoxal 5'-phosphate synthase subunit PdxT (glutamine amidotransferase) [Coenzyme transport ...
2-191 9.93e-116

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: 326.64  E-value: 9.93e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857555   2 LTIGVLGLQGAVREHIQSIEACGAEGKIIKRAEELVSVDGLIIPGGESTTMRRLMDTYQFIEPIKAFAAKGKPIFGTCAG 81
Cdd:COG0311    1 MKIGVLALQGDVREHIRALERLGAEVVEVRRPEDLEGLDGLIIPGGESTTIGKLLRRFGLLEPLRERIAAGLPVFGTCAG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857555  82 LIMLAKHIEDRDNAHLGLLNVSVARNSFGRQVDSFEADLEVKGL-DAPFTGVFIRAPHIISADESVEVMAEYDGRIVMAK 160
Cdd:COG0311   81 LILLAKEIEDPDQPTLGLLDITVRRNAFGRQVDSFEADLDIPGLgDGPFPAVFIRAPYIEEVGPGVEVLATVDGRIVAVR 160
                        170       180       190
                 ....*....|....*....|....*....|.
gi 500857555 161 ENNILGCSFHPELTDDHRLTQLFVEMVKTYK 191
Cdd:COG0311  161 QGNILATSFHPELTDDLRVHEYFLEMVRGAK 191
GATase1_PB cd01749
Glutamine Amidotransferase (GATase_I) involved in pyridoxine biosynthesis; Glutamine ...
4-184 1.28e-101

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: 290.58  E-value: 1.28e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857555   4 IGVLGLQGAVREHIQSIEACGAEGKIIKRAEELVSVDGLIIPGGESTTMRRLMDTYQFIEPIKAFAAKGKPIFGTCAGLI 83
Cdd:cd01749    1 IGVLALQGDFREHIRALERLGVEVIEVRTPEDLEGIDGLIIPGGESTTIGKLLRRTGLLDPLREFIRAGKPVFGTCAGLI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857555  84 MLAKHIED-RDNAHLGLLNVSVARNSFGRQVDSFEADLEVKGLD-APFTGVFIRAPHIISADESVEVMAEYDGRIVMAKE 161
Cdd:cd01749   81 LLAKEVEDqGGQPLLGLLDITVRRNAFGRQVDSFEADLDIPGLGlGPFPAVFIRAPVIEEVGPGVEVLAEYDGKIVAVRQ 160
                        170       180
                 ....*....|....*....|...
gi 500857555 162 NNILGCSFHPELTDDHRLTQLFV 184
Cdd:cd01749  161 GNVLATSFHPELTDDTRIHEYFL 183
PLP_synth_Pdx2 TIGR03800
pyridoxal 5'-phosphate synthase, glutaminase subunit Pdx2; Pyridoxal 5'-phosphate (PLP) is ...
4-185 2.59e-96

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


Pssm-ID: 274792 [Multi-domain]  Cd Length: 184  Bit Score: 277.39  E-value: 2.59e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857555    4 IGVLGLQGAVREHIQSIEACGAEGKIIKRAEELVSVDGLIIPGGESTTMRRLMDTYQFIEPIKAFAAKGKPIFGTCAGLI 83
Cdd:TIGR03800   2 IGVLALQGAVREHARALEALGVEGVEVKRPEQLDEIDGLIIPGGESTTISRLLDKYGMFEPLRNFILSGLPVFGTCAGLI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857555   84 MLAKHIEDRDNAHLGLLNVSVARNSFGRQVDSFEADLEVKGL-DAPFTGVFIRAPHIISADESVEVMAEYDGRIVMAKEN 162
Cdd:TIGR03800  82 MLAKEIIGQKEGQLGLLDMTVERNAYGRQVDSFEAEVDIKGVgDDPITGVFIRAPKIVSVGNGVEILAKVGNRIVAVRQG 161
                         170       180
                  ....*....|....*....|...
gi 500857555  163 NILGCSFHPELTDDHRLTQLFVE 185
Cdd:TIGR03800 162 NILVSSFHPELTDDHRVHEYFLE 184
PRK13527 PRK13527
glutamine amidotransferase subunit PdxT; Provisional
2-188 2.16e-90

glutamine amidotransferase subunit PdxT; Provisional


Pssm-ID: 237412 [Multi-domain]  Cd Length: 200  Bit Score: 262.90  E-value: 2.16e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857555   2 LTIGVLGLQGAVREHIQSIEAC------GAEGKIIKRAEELVSVDGLIIPGGESTTMRRLMDTYQFIEPIKAFAAKGKPI 75
Cdd:PRK13527   1 MKIGVLALQGDVEEHIDALKRAldelgiDGEVVEVRRPGDLPDCDALIIPGGESTTIGRLMKREGILDEIKEKIEEGLPI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857555  76 FGTCAGLIMLAKHIEDR-----DNAHLGLLNVSVARNSFGRQVDSFEADLEVKGLDAPFTGVFIRAPHIISADESVEVMA 150
Cdd:PRK13527  81 LGTCAGLILLAKEVGDDrvtktEQPLLGLMDVTVKRNAFGRQRDSFEAEIDLSGLDGPFHAVFIRAPAITKVGGDVEVLA 160
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 500857555 151 EYDGRIVMAKENNILGCSFHPELTDDHRLTQLFVEMVK 188
Cdd:PRK13527 161 KLDDRIVAVEQGNVLATAFHPELTDDTRIHEYFLKKVK 198
SNO pfam01174
SNO glutamine amidotransferase family; This family and its amidotransferase domain was first ...
6-187 2.53e-89

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: 259.77  E-value: 2.53e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857555    6 VLGLQGAVREHIQSIEACGAEGKIIKRAEELVSVDGLIIPGGESTTMRRLMDTYQFIEPIKAFAAKG-KPIFGTCAGLIM 84
Cdd:pfam01174   1 VLALQGAVEEHEEAIKKCGAENKTVKRPEDLAQCDALIIPGGESTAMSLLAKRYGFYEPLYEFVHNPnKPIWGTCAGLIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857555   85 LAKHIEDRDNAHLGLLNVSVARNSFGRQVDSFEADLEVKGLDAPFTGVFIRAPHI--ISADESVEVMAEYDGRIVMAKEN 162
Cdd:pfam01174  81 LSKQLGNELVKTLGLLKVTVKRNAFGRQVDSFEKECDFKNLIPKFPGVFIRAPVIeeILDPEVVVVLYELDGKIVVAKQG 160
                         170       180
                  ....*....|....*....|....*.
gi 500857555  163 NILGCSFHPELT-DDHRLTQLFVEMV 187
Cdd:pfam01174 161 NILATSFHPELAeDDYRVHDWFVENF 186
PLN02832 PLN02832
glutamine amidotransferase subunit of pyridoxal 5'-phosphate synthase complex
1-196 2.53e-70

glutamine amidotransferase subunit of pyridoxal 5'-phosphate synthase complex


Pssm-ID: 215446 [Multi-domain]  Cd Length: 248  Bit Score: 213.80  E-value: 2.53e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857555   1 MLTIGVLGLQGAVREHIQSIEACGAEGKIIKRAEELVSVDGLIIPGGESTTMRRLMDTYQFIEPIKAFAAKGKPIFGTCA 80
Cdd:PLN02832   1 MMAIGVLALQGSFNEHIAALRRLGVEAVEVRKPEQLEGVSGLIIPGGESTTMAKLAERHNLFPALREFVKSGKPVWGTCA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857555  81 GLIMLAKHIE---DRDNAHLGLLNVSVARNSFGRQVDSFEADLEVK------GLDAPFTGVFIRAPHIISADESVEVMAE 151
Cdd:PLN02832  81 GLIFLAERAVgqkEGGQELLGGLDCTVHRNFFGSQINSFETELPVPelaaseGGPETFRAVFIRAPAILSVGPGVEVLAE 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 500857555 152 Y------------------DGRIVMAKENNILGCSFHPELTDDHRLTQLFVEMVKTYKTKLAV 196
Cdd:PLN02832 161 YplpsekalyssstdaegrDKVIVAVKQGNLLATAFHPELTADTRWHSYFVKMVSESEEYASS 223
PRK13526 PRK13526
glutamine amidotransferase subunit PdxT; Provisional
3-186 8.00e-50

glutamine amidotransferase subunit PdxT; Provisional


Pssm-ID: 184113 [Multi-domain]  Cd Length: 179  Bit Score: 159.35  E-value: 8.00e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857555   3 TIGVLGLQGAVREHIQSIEACGAEGKIIKRAEELVSVDGLIIPGGESTTMRRLMDTYQFIEPIKAFAAKgKPIFGTCAGL 82
Cdd:PRK13526   4 KVGVLAIQGGYQKHADMFKSLGVEVKLVKFNNDFDSIDRLVIPGGESTTLLNLLNKHQIFDKLYNFCSS-KPVFGTCAGS 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857555  83 IMLAKhiedrDNAHLGLLNVSVARNSFGRQVDSFEADLEVkgLDAPFTGVFIRAPHIISADESVEVMAEYDGRIVMAKEN 162
Cdd:PRK13526  83 IILSK-----GEGYLNLLDLEVQRNAYGRQVDSFVADISF--NDKNITGVFIRAPKFIVVGNQVDILSKYQNSPVLLRQA 155
                        170       180
                 ....*....|....*....|....
gi 500857555 163 NILGCSFHPELTDDHRLTQLFVEM 186
Cdd:PRK13526 156 NILVSSFHPELTQDPTVHEYFLAM 179
GATase1_IGP_Synthase cd01748
Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate ...
20-172 3.74e-13

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: 64.83  E-value: 3.74e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857555  20 IEACGAEGKIIKRAEELVSVDGLIIPG-GE-STTMRRLMDTyQFIEPIKAFAAKGKPIFGTCAGLIMLAKHIEDRDNAH- 96
Cdd:cd01748   18 LERLGAEVIITSDPEEILSADKLILPGvGAfGDAMANLRER-GLIEALKEAIASGKPFLGICLGMQLLFESSEEGGGTKg 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857555  97 LGLLNVSVARnsfgrqvdsFEAD------------LEVKGLDAPFTGV-------FIRAPHIISADESVEVM-AEYDGRI 156
Cdd:cd01748   97 LGLIPGKVVR---------FPASeglkvphmgwnqLEITKESPLFKGIpdgsyfyFVHSYYAPPDDPDYILAtTDYGGKF 167
                        170
                 ....*....|....*..
gi 500857555 157 VMAKE-NNILGCSFHPE 172
Cdd:cd01748  168 PAAVEkDNIFGTQFHPE 184
GATase1_CobB cd03130
Type 1 glutamine amidotransferase (GATase1) domain found in Cobyrinic Acid a,c-Diamide ...
14-104 3.03e-12

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: 62.61  E-value: 3.03e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857555  14 REHIQSIEACGAEgkIIK----RAEELVSVDGLIIPGG--EsTTMRRLMDTYQFIEPIKAFAAKGKPIFGTCAGLIMLAK 87
Cdd:cd03130   14 PENLELLEAAGAE--LVPfsplKDEELPDADGLYLGGGypE-LFAEELSANQSMRESIRAFAESGGPIYAECGGLMYLGE 90
                         90       100
                 ....*....|....*....|
gi 500857555  88 HIEDRDNAH---LGLLNVSV 104
Cdd:cd03130   91 SLDDEEGQSypmAGVLPGDA 110
hisH CHL00188
imidazole glycerol phosphate synthase subunit hisH; Provisional
18-172 1.38e-10

imidazole glycerol phosphate synthase subunit hisH; Provisional


Pssm-ID: 214389 [Multi-domain]  Cd Length: 210  Bit Score: 57.97  E-value: 1.38e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857555  18 QSIEACGAEGKIIKRAEELVSVDGLIIPGGES--TTMRRLmDTYQFIEPIKAFAAKGKPIFGTCAGLIMLAKHIEDRDNA 95
Cdd:CHL00188  19 RAIQQAGQQPCIINSESELAQVHALVLPGVGSfdLAMKKL-EKKGLITPIKKWIAEGNPFIGICLGLHLLFETSEEGKEE 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857555  96 HLGLLNVSVAR--------------NSFgrQVDSFEA-DLEV---KGLDAPFTGVFIRAPHIISADESVEVMAEYDGRIV 157
Cdd:CHL00188  98 GLGIYKGQVKRlkhspvkviphmgwNRL--ECQNSECqNSEWvnwKAWPLNPWAYFVHSYGVMPKSQACATTTTFYGKQQ 175
                        170
                 ....*....|....*...
gi 500857555 158 MA---KENNILGCSFHPE 172
Cdd:CHL00188 176 MVaaiEYDNIFAMQFHPE 193
GATase_3 pfam07685
CobB/CobQ-like glutamine amidotransferase domain;
38-105 3.20e-10

CobB/CobQ-like glutamine amidotransferase domain;


Pssm-ID: 429595 [Multi-domain]  Cd Length: 189  Bit Score: 56.86  E-value: 3.20e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 500857555   38 SVDGLIIPGGESTT-MRRLMDTYQFIEPIKAFAAKGKPIFGTCAGLIMLAKHIEDRDN---AHLGLLNVSVA 105
Cdd:pfam07685  42 DADLIILPGGKPTIqDLALLRNSGMDEAIKEAAEDGGPVLGICGGYQMLGETIEDPEGvriEGLGLLDIETV 113
hisH PRK13181
imidazole glycerol phosphate synthase subunit HisH; Provisional
17-172 3.96e-10

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 183878 [Multi-domain]  Cd Length: 199  Bit Score: 56.80  E-value: 3.96e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857555  17 IQSI----EACGAEGKIIKRAEELVSVDGLIIPG-GE-STTMRRLMDTyQFIEPIKAFAAKGKPIFGTCAGLIMLAKHIE 90
Cdd:PRK13181  12 LRSVanalKRLGVEAVVSSDPEEIAGADKVILPGvGAfGQAMRSLRES-GLDEALKEHVEKKQPVLGICLGMQLLFESSE 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857555  91 DRDNAHLGLLNVSVAR-------------NSFGRQVDSfeaDLeVKGLDAPFTGVFIRAPHIISADESVEVM-AEYDGRI 156
Cdd:PRK13181  91 EGNVKGLGLIPGDVKRfrseplkvpqmgwNSVKPLKES---PL-FKGIEEGSYFYFVHSYYVPCEDPEDVLAtTEYGVPF 166
                        170
                 ....*....|....*..
gi 500857555 157 VMAKE-NNILGCSFHPE 172
Cdd:PRK13181 167 CSAVAkDNIYAVQFHPE 183
GATase1_CobQ cd01750
Type 1 glutamine amidotransferase (GATase1) domain found in Cobyric Acid Synthase (CobQ); Type ...
24-170 2.17e-09

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: 54.56  E-value: 2.17e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857555  24 GAEGKIIKRAEELVSVDGLIIPGGESTTMR-RLMDTYQFIEPIKAFAAKGKPIFGTCAGLIMLAKHIEDRDNAH------ 96
Cdd:cd01750   23 GVDVRYVEVPEGLGDADLIILPGSKDTIQDlAWLRKRGLAEAIKNYARAGGPVLGICGGYQMLGKYIVDPEGVEgpgeie 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857555  97 -LGLLNVS-------VARNSFGRqVDSFEADLEVKGldapF---TGVFIRAPH--IISADESVEVMAEYDGRIvmaKENN 163
Cdd:cd01750  103 gLGLLDVEtefgpekTTRRVTGR-LDEEGEGGEVTG----YeihSGRTTLGDGarPLGKGYGNNGEDGTDGAV---SGDN 174

                 ....*..
gi 500857555 164 ILGCSFH 170
Cdd:cd01750  175 VIGTYLH 181
PRK01077 PRK01077
cobyrinate a,c-diamide synthase;
15-104 3.03e-09

cobyrinate a,c-diamide synthase;


Pssm-ID: 234896 [Multi-domain]  Cd Length: 451  Bit Score: 55.52  E-value: 3.03e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857555  15 EHIQSIEACGAEgkiIK-----RAEELVSVDGLIIPGG----------ESTTMRrlmdtyqfiEPIKAFAAKGKPIFGTC 79
Cdd:PRK01077 262 ENLELLRAAGAE---LVffsplADEALPDCDGLYLGGGypelfaaelaANTSMR---------ASIRAAAAAGKPIYAEC 329
                         90       100
                 ....*....|....*....|....*...
gi 500857555  80 AGLIMLAKHIEDRDNAH---LGLLNVSV 104
Cdd:PRK01077 330 GGLMYLGESLEDADGERhpmVGLLPGEA 357
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
4-85 3.79e-09

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: 52.22  E-value: 3.79e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857555   4 IGVLGLQGA----VREHIQSIEACGAE-------GKIIKRAEELVSVDGLIIPGGESTTMRRLMDtYQFIEPIKAFAAKG 72
Cdd:cd01653    1 VAVLLFPGFeeleLASPLDALREAGAEvdvvspdGGPVESDVDLDDYDGLILPGGPGTPDDLARD-EALLALLREAAAAG 79
                         90
                 ....*....|...
gi 500857555  73 KPIFGTCAGLIML 85
Cdd:cd01653   80 KPILGICLGAQLL 92
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
12-85 5.09e-09

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: 51.43  E-value: 5.09e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 500857555  12 AVREHIQSIEACGAEGKIIKRAEELVSVDGLIIPGGESTTMRRLMDTyQFIEPIKAFAAKGKPIFGTCAGLIML 85
Cdd:cd03128   20 ALREAGAEVDVVSPDGGPVESDVDLDDYDGLILPGGPGTPDDLAWDE-ALLALLREAAAAGKPVLGICLGAQLL 92
hisH PRK13143
imidazole glycerol phosphate synthase subunit HisH; Provisional
19-172 5.53e-08

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237289 [Multi-domain]  Cd Length: 200  Bit Score: 50.64  E-value: 5.53e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857555  19 SIEACGAEGKIIKRAEELVSVDGLIIPG-GE-STTMRRLMdtyQFIEPIKAFAAKGKPIFGTCAGL-IMLAKHIEDRDNA 95
Cdd:PRK13143  19 ALERAGAEVVITSDPEEILDADGIVLPGvGAfGAAMENLS---PLRDVILEAARSGKPFLGICLGMqLLFESSEEGGGVR 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857555  96 HLGLLNvsvarnsfGRqVDSFEADLEVkgldaPFTG---VFIRAPHIIS------------------ADESVEVM-AEYD 153
Cdd:PRK13143  96 GLGLFP--------GR-VVRFPAGVKV-----PHMGwntVKVVKDCPLFegidgeyvyfvhsyyaypDDEDYVVAtTDYG 161
                        170       180
                 ....*....|....*....|
gi 500857555 154 GRIVMAKEN-NILGCSFHPE 172
Cdd:PRK13143 162 IEFPAAVCNdNVFGTQFHPE 181
PRK00784 PRK00784
cobyric acid synthase;
30-102 2.01e-06

cobyric acid synthase;


Pssm-ID: 234838 [Multi-domain]  Cd Length: 488  Bit Score: 47.00  E-value: 2.01e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857555  30 IKRAEELVSVDGLIIPGGESTT-----MRRL-MDtyqfiEPIKAFAAKGKPIFGTCAGLIMLAKHIEDRDN--------A 95
Cdd:PRK00784 282 VRPGEPLPDADLVILPGSKNTIadlawLRESgWD-----EAIRAHARRGGPVLGICGGYQMLGRRIADPDGvegapgsvE 356

                 ....*..
gi 500857555  96 HLGLLNV 102
Cdd:PRK00784 357 GLGLLDV 363
hisH PRK13152
imidazole glycerol phosphate synthase subunit HisH; Provisional
11-176 2.29e-06

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 171876 [Multi-domain]  Cd Length: 201  Bit Score: 45.99  E-value: 2.29e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857555  11 GAVREHIQSIEACGAEGKIIKRAEELVSVDGLIIPGGES--TTMRRLMDTYqFIEPIKAFA-AKGKPIFGTCAGL-IMLA 86
Cdd:PRK13152  10 GNLNSVAKAFEKIGAINFIAKNPKDLQKADKLLLPGVGSfkEAMKNLKELG-FIEALKEQVlVQKKPILGICLGMqLFLE 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857555  87 KHIEDRDNAHLGLLNVSVARnsfgrqvdsFEADLEVK-------------------GLDAPFTGVFIRAPHIISADESVE 147
Cdd:PRK13152  89 RGYEGGVCEGLGFIEGEVVK---------FEEDLNLKiphmgwneleilkqsplyqGIPEKSDFYFVHSFYVKCKDEFVS 159
                        170       180       190
                 ....*....|....*....|....*....|
gi 500857555 148 VMAEYDGRIVMA-KENNILGCSFHPELTDD 176
Cdd:PRK13152 160 AKAQYGHKFVASlQKDNIFATQFHPEKSQN 189
GATase1_1 cd01741
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
34-172 1.82e-05

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: 43.39  E-value: 1.82e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857555  34 EELVSVDGLIIPGGESTTMRrlmDTYQFIEP----IKAFAAKGKPIFGTCAGLIMLAKhiedrdnaHLGllnVSVARNSF 109
Cdd:cd01741   42 PDLDDYDGLVILGGPMSVDE---DDYPWLKKlkelIRQALAAGKPVLGICLGHQLLAR--------ALG---GKVGRNPK 107
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 500857555 110 GRQVDSFEADLEVKGLDAPFTGVF---IRAPHI-----ISADESVEVMAEYDGRIVMA--KENNILGCSFHPE 172
Cdd:cd01741  108 GWEIGWFPVTLTEAGKADPLFAGLpdeFPVFHWhgdtvVELPPGAVLLASSEACPNQAfrYGDRALGLQFHPE 180
YajL COG0693
Protein/nucleotide deglycase, PfpI/YajL/DJ-1 family (repair of methylglyoxal-glycated proteins ...
40-157 1.96e-05

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: 43.17  E-value: 1.96e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857555  40 DGLIIPGGeSTTMRRLMDTYQFIEPIKAFAAKGKPIFGTCAGLIMLAKHiedrdnahlGLLNvsvarnsfGRQV---DSF 116
Cdd:COG0693   66 DALVLPGG-HGAPDDLREDPDVVALVREFYEAGKPVAAICHGPAVLAAA---------GLLK--------GRKVtsfPNI 127
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 500857555 117 EADLEVKGldapftGVFIraphiisaDESVEVmaeyDGRIV 157
Cdd:COG0693  128 EDDLKNAG------ATYV--------DEEVVV----DGNLI 150
GATase1_PfpI_like cd03134
A type 1 glutamine amidotransferase (GATase1)-like domain found in PfpI from Pyrococcus ...
40-85 8.81e-05

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: 40.99  E-value: 8.81e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 500857555  40 DGLIIPGGES-TTMRRLMDTYQFIepiKAFAAKGKPIFGTCAGLIML 85
Cdd:cd03134   64 DALVIPGGTNpDKLRRDPDAVAFV---RAFAEAGKPVAAICHGPWVL 107
PRK06278 PRK06278
cobyrinic acid a,c-diamide synthase; Validated
30-103 1.38e-04

cobyrinic acid a,c-diamide synthase; Validated


Pssm-ID: 180505 [Multi-domain]  Cd Length: 476  Bit Score: 41.56  E-value: 1.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857555  30 IKRAEELvsvDGLIIPGG---ESTTMrrlmdTYQFIEPIKAFaakGKPIFGTCAGLIMLAKHIEDRDNAH-------LGL 99
Cdd:PRK06278  31 IKEIKDL---DGLIIPGGslvESGSL-----TDELKKEILNF---DGYIIGICSGFQILSEKIDIGRKSPvpiikegLGL 99

                 ....
gi 500857555 100 LNVS 103
Cdd:PRK06278 100 LDVE 103
GATase1_PfpI_1 cd03169
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ...
40-86 2.13e-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: 153243 [Multi-domain]  Cd Length: 180  Bit Score: 40.32  E-value: 2.13e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 500857555  40 DGLIIPGGESTTMRRLMDtyQFIEPIKAFAAKGKPIFGTCAGLIMLA 86
Cdd:cd03169   78 DALVIPGGRAPEYLRLDE--KVLAIVRHFAEANKPVAAICHGPQILA 122
GATase1_PfpI_3 cd03140
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ...
35-101 2.41e-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: 39.90  E-value: 2.41e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 500857555  35 ELVSVDGLIIPGGESTTMRRLMDTYQFIEpikAFAAKGKPIFGTCAGLIMLAKHiedrdnahlGLLN 101
Cdd:cd03140   57 PPEDYDLLILPGGDSWDNPEAPDLAGLVR---QALKQGKPVAAICGATLALARA---------GLLN 111
PLN02617 PLN02617
imidazole glycerol phosphate synthase hisHF
11-172 2.52e-04

imidazole glycerol phosphate synthase hisHF


Pssm-ID: 178226 [Multi-domain]  Cd Length: 538  Bit Score: 40.85  E-value: 2.52e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857555  11 GAVREHIQSIEACGAEGKIIKRAEELVSVDGLIIPGGES--TTMRRLMDTyQFIEPIKAFAAKGKPIFGTCAGLIMLAKH 88
Cdd:PLN02617  17 GNVRSVRNAIRHLGFTIKDVQTPEDILNADRLIFPGVGAfgSAMDVLNNR-GMAEALREYIQNDRPFLGICLGLQLLFES 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857555  89 IEdrDNAH---LGLLNVSVAR--------------NSFGRQVDSFEADlEVKGLDAPFTGVFiRAPHIISADESVEVMAE 151
Cdd:PLN02617  96 SE--ENGPvegLGVIPGVVGRfdssnglrvphigwNALQITKDSELLD-GVGGRHVYFVHSY-RATPSDENKDWVLATCN 171
                        170       180
                 ....*....|....*....|..
gi 500857555 152 YDGRIVMA-KENNILGCSFHPE 172
Cdd:PLN02617 172 YGGEFIASvRKGNVHAVQFHPE 193
DJ-1_PfpI pfam01965
DJ-1/PfpI family; The family includes the protease PfpI. This domain is also found in ...
40-88 6.78e-04

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: 38.78  E-value: 6.78e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 500857555   40 DGLIIPGGESTTmRRLMDTYQFIEPIKAFAAKGKPIFGTCAGLIMLAKH 88
Cdd:pfam01965  63 DALVLPGGRAGP-ERLRDNEKLVEFVKDFYEKGKPVAAICHGPQVLAAA 110
GATase pfam00117
Glutamine amidotransferase class-I;
17-184 1.11e-03

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 38.37  E-value: 1.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857555   17 IQSIEACGAEGKIIK---RAEELVS--VDGLIIPGG-ESTTMRRLMdtyqfIEPIKAFAAKGKPIFGTCAGLIMLA---- 86
Cdd:pfam00117  14 ARALRELGVEVTVVPndtPAEEILEenPDGIILSGGpGSPGAAGGA-----IEAIREARELKIPILGICLGHQLLAlafg 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857555   87 ------KHIEDR--------DNAHL--GLLNVSVARNSFGrqvDSFEADLEVKGLDapFTGVfiraphiisADESVEVMA 150
Cdd:pfam00117  89 gkvvkaKKFGHHgknspvgdDGCGLfyGLPNVFIVRRYHS---YAVDPDTLPDGLE--VTAT---------SENDGTIMG 154
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 500857555  151 eydgriVMAKENNILGCSFHPELT---DDHRLTQLFV 184
Cdd:pfam00117 155 ------IRHKKLPIFGVQFHPESIltpHGPEILFNFF 185
PRK13566 PRK13566
anthranilate synthase component I;
65-172 1.74e-03

anthranilate synthase component I;


Pssm-ID: 237429 [Multi-domain]  Cd Length: 720  Bit Score: 38.36  E-value: 1.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857555  65 IKAFAAKGKPIFGTCAGLIMLAKHIedrdNAHLGLLNV------SVARNSFGRQVdsfeadleVKGLDAPFT-GVFirap 137
Cdd:PRK13566 591 IDAALARNLPIFGVCLGLQAIVEAF----GGELGQLAYpmhgkpSRIRVRGPGRL--------FSGLPEEFTvGRY---- 654
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 500857555 138 HIISAD-----ESVEVMAEYDGRIVMA---KENNILGCSFHPE 172
Cdd:PRK13566 655 HSLFADpetlpDELLVTAETEDGVIMAiehKTLPVAAVQFHPE 697
COG3442 COG3442
Glutamine amidotransferase related to the GATase domain of CobQ [General function prediction ...
38-103 4.18e-03

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


Pssm-ID: 442666 [Multi-domain]  Cd Length: 241  Bit Score: 36.69  E-value: 4.18e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857555  38 SVDGLIIPGGESTTMRRLMDTYQFI-EPIKAFAAKGKPIFGTCAGLIMLAKHIEDRDNAH---LGLLNVS 103
Cdd:COG3442   50 DVDIVFIGGGQDREQEIVADDLLRIkDALRAAIEDGVPVLAICGGYQLLGHYYETADGERipgLGILDVY 119
GATase1_DJ-1 cd03135
Type 1 glutamine amidotransferase (GATase1)-like domain found in Human DJ-1; Type 1 glutamine ...
40-88 5.31e-03

Type 1 glutamine amidotransferase (GATase1)-like domain found in Human DJ-1; Type 1 glutamine amidotransferase (GATase1)-like domain found in Human DJ-1. DJ-1 is involved in multiple physiological processes including cancer, Parkinson's disease and male fertility. It is unclear how DJ-1 functions in these. DJ-1 has been shown to possess chaperone activity. DJ-1 is preferentially expressed in the testis and moderately in other tissues; it is induced together with genes involved in oxidative stress response. The Drosophila homologue (DJ-1A) plays an essential role in oxidative stress response and neuronal maintenance. Inhibition of DJ-1A function through RNAi, results in the cellular accumulation of reactive oxygen species, organismal hypersensitivity to oxidative stress, and dysfunction and degeneration of dopaminergic and photoreceptor neurons. DJ-1 has lacks enzymatic activity and the catalytic triad of typical GATase1 domains, however it does contain the highly conserved cysteine located at the nucelophile elbow region typical of these domains. This cysteine been proposed to be a site of regulation of DJ-1 activity by oxidation. DJ-1 is a dimeric enzyme.


Pssm-ID: 153229 [Multi-domain]  Cd Length: 163  Bit Score: 35.99  E-value: 5.31e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 500857555  40 DGLIIPGGeSTTMRRLMDTYQFIEPIKAFAAKGKPIFGTCAGLIMLAKH 88
Cdd:cd03135   62 DAIVIPGG-LPGAQNLADNEKLIKLLKEFNAKGKLIAAICAAPAVLAKA 109
 
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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