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Conserved domains on  [gi|769949417|ref|WP_045082685|]
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imidazole glycerol phosphate synthase subunit HisH [Photobacterium angustum]

Protein Classification

imidazole glycerol phosphate synthase subunit HisH( domain architecture ID 10014130)

imidazole glycerol phosphate synthase subunit HisH catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the synthesis of IGP and AICAR

CATH:  3.40.50.880
EC:  4.3.2.10|3.5.1.2
Gene Ontology:  GO:0004359|GO:0000107|GO:0016829
PubMed:  10387030
SCOP:  3001405

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
hisH PRK13170
imidazole glycerol phosphate synthase subunit HisH; Provisional
 8-215 6.43e-135

imidazole glycerol phosphate synthase subunit HisH; Provisional


:

Pssm-ID: 183877 [Multi-domain]  Cd Length: 196  Bit Score: 376.12  E-value: 6.43e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769949417   8 QRVVIIDTGCANVSSVRFAIERLGYQVEVSKDPEVVLAADKLFLPGVGTASEAMQNLQQRDLVSLVKQVTKPLLGICLGM 87
Cdd:PRK13170   1 MNVVIIDTGCANLSSVKFAIERLGYEPVVSRDPDVILAADKLFLPGVGTAQAAMDQLRERELIDLIKACTQPVLGICLGM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769949417  88 QLLGKESQEHGQngseiIPCLDLCDASVEKIQAEGLPLPHMGWNTITPEDNHPLFKGIPAGSYFYFVHSYAMPVFDHteq 167
Cdd:PRK13170  81 QLLGERSEESGG-----VDCLGIIDGPVKKMTDFGLPLPHMGWNQVTPQAGHPLFQGIEDGSYFYFVHSYAMPVNEY--- 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 769949417 168 qggkTIASAQYGQSFTAAVQSGNYYGVQFHPERSSKAGAKLIQNFLEL 215
Cdd:PRK13170 153 ----TIAQCNYGEPFSAAIQKDNFFGVQFHPERSGAAGAQLLKNFLEM 196
 
Name Accession Description Interval E-value
hisH PRK13170
imidazole glycerol phosphate synthase subunit HisH; Provisional
 8-215 6.43e-135

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 183877 [Multi-domain]  Cd Length: 196  Bit Score: 376.12  E-value: 6.43e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769949417   8 QRVVIIDTGCANVSSVRFAIERLGYQVEVSKDPEVVLAADKLFLPGVGTASEAMQNLQQRDLVSLVKQVTKPLLGICLGM 87
Cdd:PRK13170   1 MNVVIIDTGCANLSSVKFAIERLGYEPVVSRDPDVILAADKLFLPGVGTAQAAMDQLRERELIDLIKACTQPVLGICLGM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769949417  88 QLLGKESQEHGQngseiIPCLDLCDASVEKIQAEGLPLPHMGWNTITPEDNHPLFKGIPAGSYFYFVHSYAMPVFDHteq 167
Cdd:PRK13170  81 QLLGERSEESGG-----VDCLGIIDGPVKKMTDFGLPLPHMGWNQVTPQAGHPLFQGIEDGSYFYFVHSYAMPVNEY--- 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 769949417 168 qggkTIASAQYGQSFTAAVQSGNYYGVQFHPERSSKAGAKLIQNFLEL 215
Cdd:PRK13170 153 ----TIAQCNYGEPFSAAIQKDNFFGVQFHPERSGAAGAQLLKNFLEM 196
HisH COG0118
Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH [Amino acid ...
 8-210 2.10e-105

Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH [Amino acid transport and metabolism]; Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH is part of the Pathway/BioSystem: Histidine biosynthesis


Pssm-ID: 439888 [Multi-domain]  Cd Length: 196  Bit Score: 301.57  E-value: 2.10e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769949417   8 QRVVIIDTGCANVSSVRFAIERLGYQVEVSKDPEVVLAADKLFLPGVGTASEAMQNLQQRDLVSLVKQV---TKPLLGIC 84
Cdd:COG0118    1 MMIAIIDYGMGNLRSVAKALERLGAEVVVTSDPDEIRAADRLVLPGVGAFGDAMENLRERGLDEAIREAvagGKPVLGIC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769949417  85 LGMQLLGKESQEHGQngseiIPCLDLCDASVEKIQAEGLPLPHMGWNTITPEDNHPLFKGIPAGSYFYFVHSYAMPVFDH 164
Cdd:COG0118   81 LGMQLLFERSEENGD-----TEGLGLIPGEVVRFPASDLKVPHMGWNTVEIAKDHPLFAGIPDGEYFYFVHSYYVPPDDP 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 769949417 165 TEqqggkTIASAQYGQSFTAAVQSGNYYGVQFHPERSSKAGAKLIQ 210
Cdd:COG0118  156 ED-----VVATTDYGVPFTAAVERGNVFGTQFHPEKSGAAGLRLLK 196
GATase1_IGP_Synthase cd01748
Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate ...
 10-213 2.07e-96

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: 279.00  E-value: 2.07e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769949417  10 VVIIDTGCANVSSVRFAIERLGYQVEVSKDPEVVLAADKLFLPGVGTASEAMQNLQQRDLVSLVKQVT---KPLLGICLG 86
Cdd:cd01748    1 IAIIDYGMGNLRSVANALERLGAEVIITSDPEEILSADKLILPGVGAFGDAMANLRERGLIEALKEAIasgKPFLGICLG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769949417  87 MQLLGKESQEHGQngseiIPCLDLCDASVEKIQA-EGLPLPHMGWNTITPEDNHPLFKGIPAGSYFYFVHSYAMPVFDHT 165
Cdd:cd01748   81 MQLLFESSEEGGG-----TKGLGLIPGKVVRFPAsEGLKVPHMGWNQLEITKESPLFKGIPDGSYFYFVHSYYAPPDDPD 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 769949417 166 EqqggkTIASAQYGQSFTAAVQSGNYYGVQFHPERSSKAGAKLIQNFL 213
Cdd:cd01748  156 Y-----ILATTDYGGKFPAAVEKDNIFGTQFHPEKSGKAGLKLLKNFL 198
IMP_synth_hisH TIGR01855
imidazole glycerol phosphate synthase, glutamine amidotransferase subunit; This model ...
 10-215 5.21e-88

imidazole glycerol phosphate synthase, glutamine amidotransferase subunit; This model represents the glutamine amidotransferase subunit (or domain, in eukaryotic systems) of imidazole glycerol phosphate synthase. This subunit catalyzes step 5 of histidine biosynthesis from PRPP. The other subunit, the cyclase, catalyzes step 6. [Amino acid biosynthesis, Histidine family]


Pssm-ID: 273836 [Multi-domain]  Cd Length: 196  Bit Score: 257.64  E-value: 5.21e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769949417   10 VVIIDTGCANVSSVRFAIERLGYQVEVSKDPEVVLAADKLFLPGVGTASEAMQNLQQRDLVSLVKQV---TKPLLGICLG 86
Cdd:TIGR01855   1 IVIIDYGVGNLGSVKRALKRVGAEPVVVKDSKEAELADKLILPGVGAFGAAMARLRENGLDLFVELVvrlGKPVLGICLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769949417   87 MQLLGKESQEHGQngseiIPCLDLCDASVEKIQAEglPLPHMGWNTITPEDNHPLFKGIPAGSYFYFVHSYAMPVFDHTe 166
Cdd:TIGR01855  81 MQLLFERSEEGGG-----VPGLGLIKGNVVKLEAR--KVPHMGWNEVHPVKESPLLNGIDEGAYFYFVHSYYAVCEEEA- 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 769949417  167 qqggkTIASAQYGQSFTAAVQSGNYYGVQFHPERSSKAGAKLIQNFLEL 215
Cdd:TIGR01855 153 -----VLAYADYGEKFPAAVQKGNIFGTQFHPEKSGKTGLKLLENFLEL 196
GATase pfam00117
Glutamine amidotransferase class-I;
11-213 1.09e-20

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 85.37  E-value: 1.09e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769949417   11 VIIDTGCANVSSVRFAIERLGYQVEV----SKDPEVV-LAADKLFLPG----VGTASEAMQNLQQrdlvslVKQVTKPLL 81
Cdd:pfam00117   1 LLIDNGDSFTYNLARALRELGVEVTVvpndTPAEEILeENPDGIILSGgpgsPGAAGGAIEAIRE------ARELKIPIL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769949417   82 GICLGMQLLGkesQEHGqngseiipcldlcdASVEKIQAEglplPHMGWNTITPEDNHPLFKGIPAGSYFYFVHSYAmpV 161
Cdd:pfam00117  75 GICLGHQLLA---LAFG--------------GKVVKAKKF----GHHGKNSPVGDDGCGLFYGLPNVFIVRRYHSYA--V 131

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 769949417  162 FDHTEQQGGKTIASAQYGQSFTAAVQSGN-YYGVQFHPE-RSSKAGAKLIQNFL 213
Cdd:pfam00117 132 DPDTLPDGLEVTATSENDGTIMGIRHKKLpIFGVQFHPEsILTPHGPEILFNFF 185
 
Name Accession Description Interval E-value
hisH PRK13170
imidazole glycerol phosphate synthase subunit HisH; Provisional
 8-215 6.43e-135

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 183877 [Multi-domain]  Cd Length: 196  Bit Score: 376.12  E-value: 6.43e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769949417   8 QRVVIIDTGCANVSSVRFAIERLGYQVEVSKDPEVVLAADKLFLPGVGTASEAMQNLQQRDLVSLVKQVTKPLLGICLGM 87
Cdd:PRK13170   1 MNVVIIDTGCANLSSVKFAIERLGYEPVVSRDPDVILAADKLFLPGVGTAQAAMDQLRERELIDLIKACTQPVLGICLGM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769949417  88 QLLGKESQEHGQngseiIPCLDLCDASVEKIQAEGLPLPHMGWNTITPEDNHPLFKGIPAGSYFYFVHSYAMPVFDHteq 167
Cdd:PRK13170  81 QLLGERSEESGG-----VDCLGIIDGPVKKMTDFGLPLPHMGWNQVTPQAGHPLFQGIEDGSYFYFVHSYAMPVNEY--- 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 769949417 168 qggkTIASAQYGQSFTAAVQSGNYYGVQFHPERSSKAGAKLIQNFLEL 215
Cdd:PRK13170 153 ----TIAQCNYGEPFSAAIQKDNFFGVQFHPERSGAAGAQLLKNFLEM 196
HisH COG0118
Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH [Amino acid ...
 8-210 2.10e-105

Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH [Amino acid transport and metabolism]; Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH is part of the Pathway/BioSystem: Histidine biosynthesis


Pssm-ID: 439888 [Multi-domain]  Cd Length: 196  Bit Score: 301.57  E-value: 2.10e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769949417   8 QRVVIIDTGCANVSSVRFAIERLGYQVEVSKDPEVVLAADKLFLPGVGTASEAMQNLQQRDLVSLVKQV---TKPLLGIC 84
Cdd:COG0118    1 MMIAIIDYGMGNLRSVAKALERLGAEVVVTSDPDEIRAADRLVLPGVGAFGDAMENLRERGLDEAIREAvagGKPVLGIC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769949417  85 LGMQLLGKESQEHGQngseiIPCLDLCDASVEKIQAEGLPLPHMGWNTITPEDNHPLFKGIPAGSYFYFVHSYAMPVFDH 164
Cdd:COG0118   81 LGMQLLFERSEENGD-----TEGLGLIPGEVVRFPASDLKVPHMGWNTVEIAKDHPLFAGIPDGEYFYFVHSYYVPPDDP 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 769949417 165 TEqqggkTIASAQYGQSFTAAVQSGNYYGVQFHPERSSKAGAKLIQ 210
Cdd:COG0118  156 ED-----VVATTDYGVPFTAAVERGNVFGTQFHPEKSGAAGLRLLK 196
GATase1_IGP_Synthase cd01748
Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate ...
 10-213 2.07e-96

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: 279.00  E-value: 2.07e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769949417  10 VVIIDTGCANVSSVRFAIERLGYQVEVSKDPEVVLAADKLFLPGVGTASEAMQNLQQRDLVSLVKQVT---KPLLGICLG 86
Cdd:cd01748    1 IAIIDYGMGNLRSVANALERLGAEVIITSDPEEILSADKLILPGVGAFGDAMANLRERGLIEALKEAIasgKPFLGICLG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769949417  87 MQLLGKESQEHGQngseiIPCLDLCDASVEKIQA-EGLPLPHMGWNTITPEDNHPLFKGIPAGSYFYFVHSYAMPVFDHT 165
Cdd:cd01748   81 MQLLFESSEEGGG-----TKGLGLIPGKVVRFPAsEGLKVPHMGWNQLEITKESPLFKGIPDGSYFYFVHSYYAPPDDPD 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 769949417 166 EqqggkTIASAQYGQSFTAAVQSGNYYGVQFHPERSSKAGAKLIQNFL 213
Cdd:cd01748  156 Y-----ILATTDYGGKFPAAVEKDNIFGTQFHPEKSGKAGLKLLKNFL 198
hisH PRK13141
imidazole glycerol phosphate synthase subunit HisH; Provisional
 9-215 1.82e-92

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237288 [Multi-domain]  Cd Length: 205  Bit Score: 269.31  E-value: 1.82e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769949417   9 RVVIIDTGCANVSSVRFAIERLGYQVEVSKDPEVVLAADKLFLPGVGTASEAMQNLQQRDLVSLVKQV---TKPLLGICL 85
Cdd:PRK13141   1 MIAIIDYGMGNLRSVEKALERLGAEAVITSDPEEILAADGVILPGVGAFPDAMANLRERGLDEVIKEAvasGKPLLGICL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769949417  86 GMQLLGKESQEHGQngseiIPCLDLCDASVEKI-QAEGLPLPHMGWNTITPEDNHPLFKGIPAGSYFYFVHSY-AMPVFD 163
Cdd:PRK13141  81 GMQLLFESSEEFGE-----TEGLGLLPGRVRRFpPEEGLKVPHMGWNQLELKKESPLLKGIPDGAYVYFVHSYyADPCDE 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 769949417 164 HTeqqggkTIASAQYGQSFTAAVQSGNYYGVQFHPERSSKAGAKLIQNFLEL 215
Cdd:PRK13141 156 EY------VAATTDYGVEFPAAVGKDNVFGAQFHPEKSGDVGLKILKNFVEM 201
hisH PRK13181
imidazole glycerol phosphate synthase subunit HisH; Provisional
 9-215 4.22e-90

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 183878 [Multi-domain]  Cd Length: 199  Bit Score: 262.88  E-value: 4.22e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769949417   9 RVVIIDTGCANVSSVRFAIERLGYQVEVSKDPEVVLAADKLFLPGVGTASEAMQNLQQRDLVSLVK---QVTKPLLGICL 85
Cdd:PRK13181   1 MIAIIDYGAGNLRSVANALKRLGVEAVVSSDPEEIAGADKVILPGVGAFGQAMRSLRESGLDEALKehvEKKQPVLGICL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769949417  86 GMQLLGKESQEHGqngseiIPCLDLCDASVEKIQAEGLPLPHMGWNTITPEDNHPLFKGIPAGSYFYFVHSYAMPVFDHT 165
Cdd:PRK13181  81 GMQLLFESSEEGN------VKGLGLIPGDVKRFRSEPLKVPQMGWNSVKPLKESPLFKGIEEGSYFYFVHSYYVPCEDPE 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 769949417 166 EqqggkTIASAQYGQSFTAAVQSGNYYGVQFHPERSSKAGAKLIQNFLEL 215
Cdd:PRK13181 155 D-----VLATTEYGVPFCSAVAKDNIYAVQFHPEKSGKAGLKLLKNFAEL 199
IMP_synth_hisH TIGR01855
imidazole glycerol phosphate synthase, glutamine amidotransferase subunit; This model ...
 10-215 5.21e-88

imidazole glycerol phosphate synthase, glutamine amidotransferase subunit; This model represents the glutamine amidotransferase subunit (or domain, in eukaryotic systems) of imidazole glycerol phosphate synthase. This subunit catalyzes step 5 of histidine biosynthesis from PRPP. The other subunit, the cyclase, catalyzes step 6. [Amino acid biosynthesis, Histidine family]


Pssm-ID: 273836 [Multi-domain]  Cd Length: 196  Bit Score: 257.64  E-value: 5.21e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769949417   10 VVIIDTGCANVSSVRFAIERLGYQVEVSKDPEVVLAADKLFLPGVGTASEAMQNLQQRDLVSLVKQV---TKPLLGICLG 86
Cdd:TIGR01855   1 IVIIDYGVGNLGSVKRALKRVGAEPVVVKDSKEAELADKLILPGVGAFGAAMARLRENGLDLFVELVvrlGKPVLGICLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769949417   87 MQLLGKESQEHGQngseiIPCLDLCDASVEKIQAEglPLPHMGWNTITPEDNHPLFKGIPAGSYFYFVHSYAMPVFDHTe 166
Cdd:TIGR01855  81 MQLLFERSEEGGG-----VPGLGLIKGNVVKLEAR--KVPHMGWNEVHPVKESPLLNGIDEGAYFYFVHSYYAVCEEEA- 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 769949417  167 qqggkTIASAQYGQSFTAAVQSGNYYGVQFHPERSSKAGAKLIQNFLEL 215
Cdd:TIGR01855 153 -----VLAYADYGEKFPAAVQKGNIFGTQFHPEKSGKTGLKLLENFLEL 196
hisH PRK13146
imidazole glycerol phosphate synthase subunit HisH; Provisional
 8-214 2.93e-76

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237290 [Multi-domain]  Cd Length: 209  Bit Score: 228.13  E-value: 2.93e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769949417   8 QRVVIIDTGCANVSSVRFAIERLG--YQVEVSKDPEVVLAADKLFLPGVGTASEAMQNLQQRDLVSLVKQV----TKPLL 81
Cdd:PRK13146   2 MTVAIIDYGSGNLRSAAKALERAGagADVVVTADPDAVAAADRVVLPGVGAFADCMRGLRAVGLGEAVIEAvlaaGRPFL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769949417  82 GICLGMQLLGKESQEHGQngseiIPCLDLCDASVEKIQAEG--LPLPHMGWNTITPEDNHPLFKGIPAGSYFYFVHSYAM 159
Cdd:PRK13146  82 GICVGMQLLFERGLEHGD-----TPGLGLIPGEVVRFQPDGpaLKVPHMGWNTVDQTRDHPLFAGIPDGARFYFVHSYYA 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 769949417 160 PVFDhteqqGGKTIASAQYGQSFTAAVQSGNYYGVQFHPERSSKAGAKLIQNFLE 214
Cdd:PRK13146 157 QPAN-----PADVVAWTDYGGPFTAAVARDNLFATQFHPEKSQDAGLALLRNFLA 206
hisH PRK13143
imidazole glycerol phosphate synthase subunit HisH; Provisional
 8-215 5.75e-75

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237289 [Multi-domain]  Cd Length: 200  Bit Score: 224.75  E-value: 5.75e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769949417   8 QRVVIIDTGCANVSSVRFAIERLGYQVEVSKDPEVVLAADKLFLPGVGTASEAMQNLQQ-RDLVSLVKQVTKPLLGICLG 86
Cdd:PRK13143   1 MMIVIIDYGVGNLRSVSKALERAGAEVVITSDPEEILDADGIVLPGVGAFGAAMENLSPlRDVILEAARSGKPFLGICLG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769949417  87 MQLLGKESQEHGQNGSeiipcLDLCDASVEKIQAeGLPLPHMGWNTITPEDNHPLFKGIpAGSYFYFVHSYAMPVFDhte 166
Cdd:PRK13143  81 MQLLFESSEEGGGVRG-----LGLFPGRVVRFPA-GVKVPHMGWNTVKVVKDCPLFEGI-DGEYVYFVHSYYAYPDD--- 150

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 769949417 167 qqGGKTIASAQYGQSFTAAVQSGNYYGVQFHPERSSKAGAKLIQNFLEL 215
Cdd:PRK13143 151 --EDYVVATTDYGIEFPAAVCNDNVFGTQFHPEKSGETGLKILENFVEL 197
PLN02617 PLN02617
imidazole glycerol phosphate synthase hisHF
 3-214 4.05e-53

imidazole glycerol phosphate synthase hisHF


Pssm-ID: 178226 [Multi-domain]  Cd Length: 538  Bit Score: 178.37  E-value: 4.05e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769949417   3 ATNTQQRVV-IIDTGCANVSSVRFAIERLGYQVEVSKDPEVVLAADKLFLPGVGTASEAMQNLQQRDLVSLVK---QVTK 78
Cdd:PLN02617   1 ASNSADSEVtLLDYGAGNVRSVRNAIRHLGFTIKDVQTPEDILNADRLIFPGVGAFGSAMDVLNNRGMAEALReyiQNDR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769949417  79 PLLGICLGMQLLGKESQEHGQ-NGSEIIPcldlcdASVEKIQA-EGLPLPHMGWNTITPEDNHPLFKGIPaGSYFYFVHS 156
Cdd:PLN02617  81 PFLGICLGLQLLFESSEENGPvEGLGVIP------GVVGRFDSsNGLRVPHIGWNALQITKDSELLDGVG-GRHVYFVHS 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 769949417 157 Y-AMPVFDHTEQqggkTIASAQYGQSFTAAVQSGNYYGVQFHPERSSKAGAKLIQNFLE 214
Cdd:PLN02617 154 YrATPSDENKDW----VLATCNYGGEFIASVRKGNVHAVQFHPEKSGATGLSILRRFLE 208
hisH PRK13152
imidazole glycerol phosphate synthase subunit HisH; Provisional
 10-215 1.65e-52

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 171876 [Multi-domain]  Cd Length: 201  Bit Score: 167.71  E-value: 1.65e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769949417  10 VVIIDTGCANVSSVRFAIERLGYQVEVSKDPEVVLAADKLFLPGVGTASEAMQNLQQRDLVSLVKQVT----KPLLGICL 85
Cdd:PRK13152   2 IALIDYKAGNLNSVAKAFEKIGAINFIAKNPKDLQKADKLLLPGVGSFKEAMKNLKELGFIEALKEQVlvqkKPILGICL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769949417  86 GMQLLGKESQEHGQNGSeiipcLDLCDASVEKIQAE-GLPLPHMGWNTITPEDNHPLFKGIPAGSYFYFVHSYAMPVFDH 164
Cdd:PRK13152  82 GMQLFLERGYEGGVCEG-----LGFIEGEVVKFEEDlNLKIPHMGWNELEILKQSPLYQGIPEKSDFYFVHSFYVKCKDE 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 769949417 165 TEQqggktiASAQYGQSFTAAVQSGNYYGVQFHPERSSKAGAKLIQNFLEL 215
Cdd:PRK13152 157 FVS------AKAQYGHKFVASLQKDNIFATQFHPEKSQNLGLKLLENFARL 201
hisH PRK13142
imidazole glycerol phosphate synthase subunit HisH; Provisional
 10-214 2.34e-49

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 171871 [Multi-domain]  Cd Length: 192  Bit Score: 159.22  E-value: 2.34e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769949417  10 VVIIDTGCANVSSVRFAIERLGYQVEVSKDPEVVLAADKLFLPGVGTASEAMQNLQQRDLVSLVKQVT-KPLLGICLGMQ 88
Cdd:PRK13142   2 IVIVDYGLGNISNVKRAIEHLGYEVVVSNTSKIIDQAETIILPGVGHFKDAMSEIKRLNLNAILAKNTdKKMIGICLGMQ 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769949417  89 LLGKESQEHGQNGSEIIPcldlcdASVEKIQAEgLPLPHMGWNTItpEDNHPLFKgipagSYFYFVHSYAMPVFDHteqq 168
Cdd:PRK13142  82 LMYEHSDEGDASGLGFIP------GNISRIQTE-YPVPHLGWNNL--VSKHPMLN-----QDVYFVHSYQAPMSEN---- 143

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 769949417 169 ggkTIASAQYGQSFTAAVQSGNYYGVQFHPERSSKAGAKLIQNFLE 214
Cdd:PRK13142 144 ---VIAYAQYGADIPAIVQFNNYIGIQFHPEKSGTYGLQILRQAIQ 186
hisH PRK14004
imidazole glycerol phosphate synthase subunit HisH; Provisional
 10-215 2.42e-42

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 172505 [Multi-domain]  Cd Length: 210  Bit Score: 141.96  E-value: 2.42e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769949417  10 VVIIDTGCANVSSVRFAIERLGYQVEVSKDPEVVLAADKLFLPGVGTASEAMQNLQQRDLVSLV-KQVT--KPLLGICLG 86
Cdd:PRK14004   2 IAILDYGMGNIHSCLKAVSLYTKDFVFTSDPETIENSKALILPGDGHFDKAMENLNSTGLRSTIdKHVEsgKPLFGICIG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769949417  87 MQLLGKESQEHGQNG-SEIIPCLDLCDASVEKIQAEGLPLPHMGWNT--ITPEDNHPLFKGIPAGSYFYFVHSYAmpvfd 163
Cdd:PRK14004  82 FQILFESSEETNQGTkKEQIEGLGYIKGKIKKFEGKDFKVPHIGWNRlqIRRKDKSKLLKGIGDQSFFYFIHSYR----- 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 769949417 164 HTEQQGGKTIASAQY-GQSFTAAVQSGNYYGVQFHPERSSKAGAKLIQNFLEL 215
Cdd:PRK14004 157 PTGAEGNAITGLCDYyQEKFPAVVEKENIFGTQFHPEKSHTHGLKLLENFIEF 209
hisH CHL00188
imidazole glycerol phosphate synthase subunit hisH; Provisional
 9-214 3.14e-37

imidazole glycerol phosphate synthase subunit hisH; Provisional


Pssm-ID: 214389 [Multi-domain]  Cd Length: 210  Bit Score: 128.85  E-value: 3.14e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769949417   9 RVVIIDTGCANVSSVRFAIERLGYQVEVSKDPEVVLAADKLFLPGVGTASEAMQNLQQRDLVSLVK---QVTKPLLGICL 85
Cdd:CHL00188   3 KIGIIDYSMGNLHSVSRAIQQAGQQPCIINSESELAQVHALVLPGVGSFDLAMKKLEKKGLITPIKkwiAEGNPFIGICL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769949417  86 GMQLLGKESQEhgqnGSEiiPCLDLCDASVEKIQAEGL-PLPHMGWNTI------TPEDNHPLFKGIPAGSYFYFVHSY- 157
Cdd:CHL00188  83 GLHLLFETSEE----GKE--EGLGIYKGQVKRLKHSPVkVIPHMGWNRLecqnseCQNSEWVNWKAWPLNPWAYFVHSYg 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 769949417 158 AMPvfdhtEQQGGKTIASAQYGQSFTAAVQSGNYYGVQFHPERSSKAGAKLIQNFLE 214
Cdd:CHL00188 157 VMP-----KSQACATTTTFYGKQQMVAAIEYDNIFAMQFHPEKSGEFGLWLLREFMK 208
GATase pfam00117
Glutamine amidotransferase class-I;
11-213 1.09e-20

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 85.37  E-value: 1.09e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769949417   11 VIIDTGCANVSSVRFAIERLGYQVEV----SKDPEVV-LAADKLFLPG----VGTASEAMQNLQQrdlvslVKQVTKPLL 81
Cdd:pfam00117   1 LLIDNGDSFTYNLARALRELGVEVTVvpndTPAEEILeENPDGIILSGgpgsPGAAGGAIEAIRE------ARELKIPIL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769949417   82 GICLGMQLLGkesQEHGqngseiipcldlcdASVEKIQAEglplPHMGWNTITPEDNHPLFKGIPAGSYFYFVHSYAmpV 161
Cdd:pfam00117  75 GICLGHQLLA---LAFG--------------GKVVKAKKF----GHHGKNSPVGDDGCGLFYGLPNVFIVRRYHSYA--V 131

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 769949417  162 FDHTEQQGGKTIASAQYGQSFTAAVQSGN-YYGVQFHPE-RSSKAGAKLIQNFL 213
Cdd:pfam00117 132 DPDTLPDGLEVTATSENDGTIMGIRHKKLpIFGVQFHPEsILTPHGPEILFNFF 185
GuaA1 COG0518
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ...
 78-199 8.19e-13

GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP synthase, glutamine amidotransferase domain is part of the Pathway/BioSystem: Purine biosynthesis


Pssm-ID: 440284 [Multi-domain]  Cd Length: 225  Bit Score: 64.97  E-value: 8.19e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769949417  78 KPLLGICLGMQLLGKesqehgQNGSEIIPCldlcdasvekiqaeglPLPHMGWNTITPEDNHPLFKGIPAGsyFYFVHSy 157
Cdd:COG0518   83 KPVLGICYGAQLLAH------ALGGKVEPG----------------PGREIGWAPVELTEADPLFAGLPDE--FTVWMS- 137

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 769949417 158 ampvfdHTEQ-----QGGKTIASaqygqSFTAAVQ----SGNYYGVQFHPE 199
Cdd:COG0518  138 ------HGDTvtelpEGAEVLAS-----SDNCPNQafryGRRVYGVQFHPE 177
guaA PRK00074
GMP synthase; Reviewed
 79-213 2.55e-12

GMP synthase; Reviewed


Pssm-ID: 234614 [Multi-domain]  Cd Length: 511  Bit Score: 65.07  E-value: 2.55e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769949417  79 PLLGICLGMQLLGKesqehgQNGSEiipcldlcdasVEK-IQAEglplphMGWNTITPEDNHPLFKGIPAGSYFYFVHSy 157
Cdd:PRK00074  77 PVLGICYGMQLMAH------QLGGK-----------VERaGKRE------YGRAELEVDNDSPLFKGLPEEQDVWMSHG- 132

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 769949417 158 ampvfDHTEQ--QGGKTIAS---AQYgqsftAAVQ--SGNYYGVQFHPE-RSSKAGAKLIQNFL 213
Cdd:PRK00074 133 -----DKVTElpEGFKVIAStenCPI-----AAIAneERKFYGVQFHPEvTHTPQGKKLLENFV 186
GATase1_Anthranilate_Synthase cd01743
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ...
 27-213 3.09e-12

Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase (ASase). This group contains proteins similar to para-aminobenzoate (PABA) synthase and ASase. These enzymes catalyze similar reactions and produce similar products, PABA and ortho-aminobenzoate (anthranilate). Each enzyme is composed of non-identical subunits: a glutamine amidotransferase subunit (component II) and a subunit that produces an aminobenzoate products (component I). ASase catalyses the synthesis of anthranilate from chorismate and glutamine and is a tetrameric protein comprising two copies each of components I and II. Component II of ASase belongs to the family of triad GTases which hydrolyze glutamine and transfer nascent ammonia between the active sites. In some bacteria, such as Escherichia coli, component II can be much larger than in other organisms, due to the presence of phosphoribosyl-anthranilate transferase (PRTase) activity. PRTase catalyses the second step in tryptophan biosynthesis and results in the addition of 5-phosphoribosyl-1-pyrophosphate to anthranilate to create N-5'-phosphoribosyl-anthranilate. In E.coli, the first step in the conversion of chorismate to PABA involves two proteins: PabA and PabB which co-operate to transfer the amide nitrogen of glutamine to chorismate forming 4-amino-4 deoxychorismate (ADC). PabA acts as a glutamine amidotransferase, supplying an amino group to PabB, which carries out the amination reaction. A third protein PabC then mediates elimination of pyruvate and aromatization to give PABA. Several organisms have bipartite proteins containing fused domains homologous to PabA and PabB commonly called PABA synthases. These hybrid PABA synthases may produce ADC and not PABA.


Pssm-ID: 153214 [Multi-domain]  Cd Length: 184  Bit Score: 62.55  E-value: 3.09e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769949417  27 IERLGYQVEV------SKDPEVVLAADKLFL-PGVGTASEAmqnlqqRDLVSLVKQVTK--PLLGICLGMQLLGkesQEH 97
Cdd:cd01743   18 LRELGAEVVVvrndeiTLEELELLNPDAIVIsPGPGHPEDA------GISLEIIRALAGkvPILGVCLGHQAIA---EAF 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769949417  98 GqngseiipcldlcdASVEKiqaegLPLPHMGWNTITPEDNHPLFKGIP----AGSYfyfvHSYAmpVFDHTEQQGGKTI 173
Cdd:cd01743   89 G--------------GKVVR-----APEPMHGKTSEIHHDGSGLFKGLPqpftVGRY----HSLV--VDPDPLPDLLEVT 143

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 769949417 174 ASAQYGQSFTAAVQSGNYYGVQFHPErS--SKAGAKLIQNFL 213
Cdd:cd01743  144 ASTEDGVIMALRHRDLPIYGVQFHPE-SilTEYGLRLLENFL 184
GATase1_1 cd01741
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 67-213 7.31e-10

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: 56.10  E-value: 7.31e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769949417  67 RDLVSLVKQVT---KPLLGICLGMQLLGKE---SQEHGQNGSEIipcldlcdasvekiqaeglplphmGWNTITPED--- 137
Cdd:cd01741   68 KKLKELIRQALaagKPVLGICLGHQLLARAlggKVGRNPKGWEI------------------------GWFPVTLTEagk 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769949417 138 NHPLFKGIPAGSYFYFVHS---YAMPvfdhteqQGGKTIASaqygqSFTAAVQ----SGNYYGVQFHPERsskagaKLIQ 210
Cdd:cd01741  124 ADPLFAGLPDEFPVFHWHGdtvVELP-------PGAVLLAS-----SEACPNQafryGDRALGLQFHPEE------RLLR 185


                 ...
gi 769949417 211 NFL 213
Cdd:cd01741  186 NFL 188
PabA COG0512
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ...
 10-215 1.85e-09

Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid transport and metabolism, Coenzyme transport and metabolism]; Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis


Pssm-ID: 440278 [Multi-domain]  Cd Length: 189  Bit Score: 55.04  E-value: 1.85e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769949417  10 VVIIDtgcaNVSSvrF------AIERLGYQVEVSK----DPEVV--LAADKLFL-PGVGTASEAMQNLqqrDLVSLVKQv 76
Cdd:COG0512    1 ILLID----NYDS--FtynlvqYLGELGAEVVVVRndeiTLEEIeaLAPDGIVLsPGPGTPEEAGISL---EVIRAFAG- 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769949417  77 TKPLLGICLGMQLLGkesQEHGqngseiipcldlcdASVEKiqaegLPLP---------HmgwntitpeDNHPLFKGIP- 146
Cdd:COG0512   71 KIPILGVCLGHQAIG---EAFG--------------GKVVR-----APEPmhgktspitH---------DGSGLFAGLPn 119

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769949417 147 ---AGSYfyfvHSYAmpvfdhteqqggktIASAQYGQSF--TAAVQSG--------NY--YGVQFHPErS--SKAGAKLI 209
Cdd:COG0512  120 pftATRY----HSLV--------------VDRETLPDELevTAWTEDGeimgirhrELpiEGVQFHPE-SilTEHGHQLL 180


                 ....*.
gi 769949417 210 QNFLEL 215
Cdd:COG0512  181 ANFLEL 186
PRK05670 PRK05670
anthranilate synthase component II; Provisional
 30-215 1.01e-08

anthranilate synthase component II; Provisional


Pssm-ID: 235552 [Multi-domain]  Cd Length: 189  Bit Score: 52.82  E-value: 1.01e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769949417  30 LGYQVEVSKDPEVV------LAADKLFL-PGVGTASEAMQnlqqrdLVSLVKQV--TKPLLGICLGMQLLGkesqEHgqN 100
Cdd:PRK05670  22 LGAEVVVYRNDEITleeieaLNPDAIVLsPGPGTPAEAGI------SLELIREFagKVPILGVCLGHQAIG----EA--F 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769949417 101 GSEIIPCLDLCDASVEKIQaeglplpHmgwntitpeDNHPLFKGIP----AGSYfyfvHSYAmpvfdhteqqggktIASA 176
Cdd:PRK05670  90 GGKVVRAKEIMHGKTSPIE-------H---------DGSGIFAGLPnpftVTRY----HSLV--------------VDRE 135

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 769949417 177 QYGQSF--TA--------AVQSGNY--YGVQFHPErS--SKAGAKLIQNFLEL 215
Cdd:PRK05670 136 SLPDCLevTAwtddgeimGVRHKELpiYGVQFHPE-SilTEHGHKLLENFLEL 187
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 10-90 2.14e-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: 50.67  E-value: 2.14e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769949417  10 VVIIDTGCAN---VSSVRFAIERLGYQVE-VSKDPEVVLA------ADKLFLPGVGTASEAMQNLQqrDLVSLVKQV--- 76
Cdd:cd01653    1 VAVLLFPGFEeleLASPLDALREAGAEVDvVSPDGGPVESdvdlddYDGLILPGGPGTPDDLARDE--ALLALLREAaaa 78

                         90
                 ....*....|....
gi 769949417  77 TKPLLGICLGMQLL 90
Cdd:cd01653   79 GKPILGICLGAQLL 92
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 10-90 2.15e-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: 49.89  E-value: 2.15e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769949417  10 VVIIDTGCAN---VSSVRFAIERLGYQVE-VSKDPEVVLA------ADKLFLPGVGTASEAMQNLQqrDLVSLVKQV--- 76
Cdd:cd03128    1 VAVLLFGGSEeleLASPLDALREAGAEVDvVSPDGGPVESdvdlddYDGLILPGGPGTPDDLAWDE--ALLALLREAaaa 78

                         90
                 ....*....|....
gi 769949417  77 TKPLLGICLGMQLL 90
Cdd:cd03128   79 GKPVLGICLGAQLL 92
GATase1_GMP_Synthase cd01742
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine ...
 78-213 4.10e-08

Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase. GMP synthetase is a glutamine amidotransferase from the de novo purine biosynthetic pathway. Glutamine amidotransferase (GATase) activity catalyse the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. GMP synthetase catalyses the amination of the nucleotide precursor xanthosine 5'-monophosphate to form GMP. GMP synthetase belongs to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site.


Pssm-ID: 153213 [Multi-domain]  Cd Length: 181  Bit Score: 51.00  E-value: 4.10e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769949417  78 KPLLGICLGMQLLGKesqehgQNGseiipcldlcdASVEKIQAEGLplphmGWNTITPEDNHPLFKGIPAGSYFYFVHsy 157
Cdd:cd01742   71 VPVLGICYGMQLIAK------ALG-----------GKVERGDKREY-----GKAEIEIDDSSPLFEGLPDEQTVWMSH-- 126

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 769949417 158 ampvFDHTEQ--QGGKTIASAqyGQSFTAAVQSGNY--YGVQFHPERS-SKAGAKLIQNFL 213
Cdd:cd01742  127 ----GDEVVKlpEGFKVIASS--DNCPVAAIANEEKkiYGVQFHPEVThTEKGKEILKNFL 181
GATase1_CobQ cd01750
Type 1 glutamine amidotransferase (GATase1) domain found in Cobyric Acid Synthase (CobQ); Type ...
 24-139 1.61e-05

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: 43.77  E-value: 1.61e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769949417  24 RFAIERlGYQVEVSKDPEVVLAADKLFLPGVGTASEAMQNLQQRDLVSLVKQVT---KPLLGICLGMQLLGKE-SQEHGQ 99
Cdd:cd01750   17 PLAREP-GVDVRYVEVPEGLGDADLIILPGSKDTIQDLAWLRKRGLAEAIKNYAragGPVLGICGGYQMLGKYiVDPEGV 95

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 769949417 100 NGSEIIPCLDLCDA----SVEKI--QAEGLPLPHMGWNTITPEDNH 139
Cdd:cd01750   96 EGPGEIEGLGLLDVetefGPEKTtrRVTGRLDEEGEGGEVTGYEIH 141
PRK05637 PRK05637
anthranilate synthase component II; Provisional
 7-199 1.91e-05

anthranilate synthase component II; Provisional


Pssm-ID: 180178 [Multi-domain]  Cd Length: 208  Bit Score: 44.06  E-value: 1.91e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769949417   7 QQRVVIIDTGCANVSSVRFAIERLGYQVEV---SKDPEVVLAA--DKLFL-PGVGTASEA--MQNLQQRDLVSLvkqvtk 78
Cdd:PRK05637   1 MTHVVLIDNHDSFVYNLVDAFAVAGYKCTVfrnTVPVEEILAAnpDLICLsPGPGHPRDAgnMMALIDRTLGQI------ 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769949417  79 PLLGICLGMQLLgkesQEHgqNGSEIIPC---------LDLCDASVEKIQAEGLplphmgwnTITPEDNHPLFKG--IPA 147
Cdd:PRK05637  75 PLLGICLGFQAL----LEH--HGGKVEPCgpvhgttdnMILTDAGVQSPVFAGL--------ATDVEPDHPEIPGrkVPI 140

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 769949417 148 GSYfyfvHSYA-------MPVFDHTEQQGGKTIASAQygqsftaaVQSGNYYGVQFHPE 199
Cdd:PRK05637 141 ARY----HSLGcvvapdgMESLGTCSSEIGPVIMAAE--------TTDGKAIGLQFHPE 187
GATase1_PB cd01749
Glutamine Amidotransferase (GATase_I) involved in pyridoxine biosynthesis; Glutamine ...
 26-199 2.78e-05

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: 43.28  E-value: 2.78e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769949417  26 AIERLGYQVEVSKDPEVVLAADKLFLPgvGTASEAMQNLQQR-----DLVSLVKQvTKPLLGICLGMQLLGKESQehGQN 100
Cdd:cd01749   16 ALERLGVEVIEVRTPEDLEGIDGLIIP--GGESTTIGKLLRRtglldPLREFIRA-GKPVFGTCAGLILLAKEVE--DQG 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769949417 101 GSEIIPCLDLCDA------SVEKIQAEgLPLPHMGWNTitpednhplFKGIpagsyfyFVHSyamPVFdhtEQQGGKTIA 174
Cdd:cd01749   91 GQPLLGLLDITVRrnafgrQVDSFEAD-LDIPGLGLGP---------FPAV-------FIRA---PVI---EEVGPGVEV 147

                        170       180
                 ....*....|....*....|....*
gi 769949417 175 SAQYGQSfTAAVQSGNYYGVQFHPE 199
Cdd:cd01749  148 LAEYDGK-IVAVRQGNVLATSFHPE 171
PRK13527 PRK13527
glutamine amidotransferase subunit PdxT; Provisional
 20-199 3.07e-05

glutamine amidotransferase subunit PdxT; Provisional


Pssm-ID: 237412 [Multi-domain]  Cd Length: 200  Bit Score: 43.34  E-value: 3.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769949417  20 VSSVRFAIERLGYQVEVS--KDPEVVLAADKLFLPGvGTaSEAMQNLQQRD-----LVSLVKQvTKPLLGICLGMQLLGK 92
Cdd:PRK13527  16 IDALKRALDELGIDGEVVevRRPGDLPDCDALIIPG-GE-STTIGRLMKREgildeIKEKIEE-GLPILGTCAGLILLAK 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769949417  93 ESQEHGQNGSEiIPCLDLCDASVEK-------------IQAEGLPLPhmgwntitpednhplFKGIpagsyfyFVHSyam 159
Cdd:PRK13527  93 EVGDDRVTKTE-QPLLGLMDVTVKRnafgrqrdsfeaeIDLSGLDGP---------------FHAV-------FIRA--- 146

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 769949417 160 PVFDHTeqqGGKTIASAQYGQsFTAAVQSGNYYGVQFHPE 199
Cdd:PRK13527 147 PAITKV---GGDVEVLAKLDD-RIVAVEQGNVLATAFHPE 182
COG3442 COG3442
Glutamine amidotransferase related to the GATase domain of CobQ [General function prediction ...
 28-116 2.96e-04

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


Pssm-ID: 442666 [Multi-domain]  Cd Length: 241  Bit Score: 40.55  E-value: 2.96e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769949417  28 ERLGYQVEVSK----DPEVVLAADKLFLPGvGTASEamQNLQQRDLV----SLVKQVT--KPLLGICLGMQLLGKESQEH 97
Cdd:COG3442   29 EWRGIDVEVVEvnpgDDLPFDDVDIVFIGG-GQDRE--QEIVADDLLrikdALRAAIEdgVPVLAICGGYQLLGHYYETA 105

                         90
                 ....*....|....*....
gi 769949417  98 gqNGSEiIPCLDLCDASVE 116
Cdd:COG3442  106 --DGER-IPGLGILDVYTV 121
GATase1_CPSase cd01744
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ...
 10-110 6.54e-04

Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This group of sequences represents the small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II. CPSase II catalyzes the production of carbomyl phosphate (CP) from bicarbonate, glutamine and two molecules of MgATP. The reaction is believed to proceed by a series of four biochemical reactions involving a minimum of three discrete highly reactive intermediates. The synthesis of CP is critical for the initiation of two separate biosynthetic pathways. In one CP is coupled to aspartate, its carbon and nitrogen nuclei ultimately incorporated into the aromatic moieties of pyrimidine nucleotides. In the second pathway CP is condensed with ornithine at the start of the urea cycle and is utilized for the detoxification of ammonia and biosynthesis of arginine. CPSases may be encoded by one or by several genes, depending on the species. The E.coli enzyme is a heterodimer consisting of two polypeptide chains referred to as the small and large subunit. Ammonia an intermediate during the biosynthesis of carbomyl phosphate produced by the hydrolysis of glutamine in the small subunit of the enzyme is delivered via a molecular tunnel between the remotely located carboxyphosphate active site in the large subunit. CPSase IIs belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site. This group also contains the sequence from the mammalian urea cycle form which has lost the active site Cys, resulting in an ammonia-dependent form, CPSase I.


Pssm-ID: 153215 [Multi-domain]  Cd Length: 178  Bit Score: 39.02  E-value: 6.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769949417  10 VVIIDTGCANvSSVRFAIERlGYQVEV---SKDPEVVLA--ADKLFLP-GVGTASEAmqnlqqRDLVSLVKQV---TKPL 80
Cdd:cd01744    1 VVVIDFGVKH-NILRELLKR-GCEVTVvpyNTDAEEILKldPDGIFLSnGPGDPALL------DEAIKTVRKLlgkKIPI 72

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 769949417  81 LGICLGMQLLG--------KESQEH-GQNgseiIPCLDL 110
Cdd:cd01744   73 FGICLGHQLLAlalgaktyKMKFGHrGSN----HPVKDL 107
PRK07765 PRK07765
aminodeoxychorismate/anthranilate synthase component II;
30-91 7.86e-04

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181107 [Multi-domain]  Cd Length: 214  Bit Score: 39.26  E-value: 7.86e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 769949417  30 LGYQVEVSKDPEVVLAADK---------LFLPGVGTASEAMQNLqqrDLVSLVKQVTKPLLGICLGMQLLG 91
Cdd:PRK07765  23 LGVEAEVWRNDDPRLADEAavaaqfdgvLLSPGPGTPERAGASI---DMVRACAAAGTPLLGVCLGHQAIG 90
PRK06895 PRK06895
anthranilate synthase component II;
77-215 1.33e-03

anthranilate synthase component II;


Pssm-ID: 235882 [Multi-domain]  Cd Length: 190  Bit Score: 38.18  E-value: 1.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769949417  77 TKPLLGICLGMQLLGK---------ESQEHGQNGseiipcldlcdasvekiqaeglplphmgwnTITPEDNHPLFKGIPA 147
Cdd:PRK06895  72 HKSILGVCLGHQTLCEffggelynlNNVRHGQQR------------------------------PLKVRSNSPLFDGLPE 121

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 769949417 148 GSYFYFVHSYAMPVFDHTEQqggkTIASAQYGQSFTAAVQSGNY--YGVQFHPERS-SKAGAKLIQNFLEL 215
Cdd:PRK06895 122 EFNIGLYHSWAVSEENFPTP----LEITAVCDENVVMAMQHKTLpiYGVQFHPESYiSEFGEQILRNWLAI 188
CarA COG0505
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ...
 9-91 4.95e-03

Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Carbamoylphosphate synthase small subunit is part of the Pathway/BioSystem: Arginine biosynthesis


Pssm-ID: 440271 [Multi-domain]  Cd Length: 361  Bit Score: 37.31  E-value: 4.95e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769949417   9 RVVIIDTGcanvssVRFAIERL----GYQVEV---SKDPEVVLA--ADKLFL---PG----VGTASEAMQNLQQRDlvsl 72
Cdd:COG0505  178 HVVALDFG------VKRNILRElaerGCRVTVvpaTTSAEEILAlnPDGVFLsngPGdpaaLDYAIETIRELLGKG---- 247

                         90
                 ....*....|....*....
gi 769949417  73 vkqvtKPLLGICLGMQLLG 91
Cdd:COG0505  248 -----IPIFGICLGHQLLA 261
PRK12564 PRK12564
carbamoyl-phosphate synthase small subunit;
70-91 7.94e-03

carbamoyl-phosphate synthase small subunit;


Pssm-ID: 237139 [Multi-domain]  Cd Length: 360  Bit Score: 36.59  E-value: 7.94e-03
                         10        20
                 ....*....|....*....|....*
gi 769949417  70 VSLVKQV---TKPLLGICLGMQLLG 91
Cdd:PRK12564 238 IEMIRELlekKIPIFGICLGHQLLA 262
 
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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