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Conserved domains on  [gi|502824742|ref|WP_013059718|]
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MULTISPECIES: imidazole glycerol phosphate synthase subunit HisH [Priestia]

Protein Classification

imidazole glycerol phosphate synthase subunit HisH( domain architecture ID 10793738)

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 PRK13141
imidazole glycerol phosphate synthase subunit HisH; Provisional
 1-208 7.06e-126

imidazole glycerol phosphate synthase subunit HisH; Provisional


:

Pssm-ID: 237288 [Multi-domain]  Cd Length: 205  Bit Score: 353.67  E-value: 7.06e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824742   1 MIGIIDYGMGNLYSVSKALERLNYDYIISADPAELRKAKGLILPGVGAFKDAMEQLNQTKLTDFIKEEVAKGMPLLGICL 80
Cdd:PRK13141   1 MIAIIDYGMGNLRSVEKALERLGAEAVITSDPEEILAADGVILPGVGAFPDAMANLRERGLDEVIKEAVASGKPLLGICL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824742  81 GMQLLFEESDENGVTKGLELLKGRVERIPgitaEGQTYKVPHMGWNSLDFHQQSALLDGISEG-HVYFVHSYYVKTNDQD 159
Cdd:PRK13141  81 GMQLLFESSEEFGETEGLGLLPGRVRRFP----PEEGLKVPHMGWNQLELKKESPLLKGIPDGaYVYFVHSYYADPCDEE 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 502824742 160 VLLATSPYDVEVPAVVGKEHVFGTQFHPEKSSAIGMQMLQNYANFLEKR 208
Cdd:PRK13141 157 YVAATTDYGVEFPAAVGKDNVFGAQFHPEKSGDVGLKILKNFVEMVEEC 205
 
Name Accession Description Interval E-value
hisH PRK13141
imidazole glycerol phosphate synthase subunit HisH; Provisional
 1-208 7.06e-126

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237288 [Multi-domain]  Cd Length: 205  Bit Score: 353.67  E-value: 7.06e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824742   1 MIGIIDYGMGNLYSVSKALERLNYDYIISADPAELRKAKGLILPGVGAFKDAMEQLNQTKLTDFIKEEVAKGMPLLGICL 80
Cdd:PRK13141   1 MIAIIDYGMGNLRSVEKALERLGAEAVITSDPEEILAADGVILPGVGAFPDAMANLRERGLDEVIKEAVASGKPLLGICL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824742  81 GMQLLFEESDENGVTKGLELLKGRVERIPgitaEGQTYKVPHMGWNSLDFHQQSALLDGISEG-HVYFVHSYYVKTNDQD 159
Cdd:PRK13141  81 GMQLLFESSEEFGETEGLGLLPGRVRRFP----PEEGLKVPHMGWNQLELKKESPLLKGIPDGaYVYFVHSYYADPCDEE 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 502824742 160 VLLATSPYDVEVPAVVGKEHVFGTQFHPEKSSAIGMQMLQNYANFLEKR 208
Cdd:PRK13141 157 YVAATTDYGVEFPAAVGKDNVFGAQFHPEKSGDVGLKILKNFVEMVEEC 205
HisH COG0118
Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH [Amino acid ...
 1-199 2.90e-118

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: 334.31  E-value: 2.90e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824742   1 MIGIIDYGMGNLYSVSKALERLNYDYIISADPAELRKAKGLILPGVGAFKDAMEQLNQTKLTDFIKEEVAKGMPLLGICL 80
Cdd:COG0118    2 MIAIIDYGMGNLRSVAKALERLGAEVVVTSDPDEIRAADRLVLPGVGAFGDAMENLRERGLDEAIREAVAGGKPVLGICL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824742  81 GMQLLFEESDENGVTKGLELLKGRVERIPgitaeGQTYKVPHMGWNSLDFHQQSALLDGISEG-HVYFVHSYYVKTNDQD 159
Cdd:COG0118   82 GMQLLFERSEENGDTEGLGLIPGEVVRFP-----ASDLKVPHMGWNTVEIAKDHPLFAGIPDGeYFYFVHSYYVPPDDPE 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 502824742 160 VLLATSPYDVEVPAVVGKEHVFGTQFHPEKSSAIGMQMLQ 199
Cdd:COG0118  157 DVVATTDYGVPFTAAVERGNVFGTQFHPEKSGAAGLRLLK 196
GATase1_IGP_Synthase cd01748
Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate ...
 2-200 1.95e-109

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: 311.74  E-value: 1.95e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824742   2 IGIIDYGMGNLYSVSKALERLNYDYIISADPAELRKAKGLILPGVGAFKDAMEQLNQTKLTDFIKEEVAKGMPLLGICLG 81
Cdd:cd01748    1 IAIIDYGMGNLRSVANALERLGAEVIITSDPEEILSADKLILPGVGAFGDAMANLRERGLIEALKEAIASGKPFLGICLG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824742  82 MQLLFEESDENGVTKGLELLKGRVERIPgitaEGQTYKVPHMGWNSLDFHQQSALLDGISEG-HVYFVHSYYVKTNDQDV 160
Cdd:cd01748   81 MQLLFESSEEGGGTKGLGLIPGKVVRFP----ASEGLKVPHMGWNQLEITKESPLFKGIPDGsYFYFVHSYYAPPDDPDY 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 502824742 161 LLATSPYDVEVPAVVGKEHVFGTQFHPEKSSAIGMQMLQN 200
Cdd:cd01748  157 ILATTDYGGKFPAAVEKDNIFGTQFHPEKSGKAGLKLLKN 196
IMP_synth_hisH TIGR01855
imidazole glycerol phosphate synthase, glutamine amidotransferase subunit; This model ...
 2-202 2.65e-86

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: 253.40  E-value: 2.65e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824742    2 IGIIDYGMGNLYSVSKALERLNYDYIISADPAELRKAKGLILPGVGAFKDAMEQLNQTKLTDFIKEEVAKGMPLLGICLG 81
Cdd:TIGR01855   1 IVIIDYGVGNLGSVKRALKRVGAEPVVVKDSKEAELADKLILPGVGAFGAAMARLRENGLDLFVELVVRLGKPVLGICLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824742   82 MQLLFEESDENGVTKGLELLKGRVERIpgitaegQTYKVPHMGWNSLDFHQQSALLDGISEG-HVYFVHSYYVKTNDQDV 160
Cdd:TIGR01855  81 MQLLFERSEEGGGVPGLGLIKGNVVKL-------EARKVPHMGWNEVHPVKESPLLNGIDEGaYFYFVHSYYAVCEEEAV 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 502824742  161 lLATSPYDVEVPAVVGKEHVFGTQFHPEKSSAIGMQMLQNYA 202
Cdd:TIGR01855 154 -LAYADYGEKFPAAVQKGNIFGTQFHPEKSGKTGLKLLENFL 194
GATase pfam00117
Glutamine amidotransferase class-I;
4-207 1.53e-26

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 100.39  E-value: 1.53e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824742    4 IIDYGMGNLYSVSKALERLNYDYII---SADPAELRKAK--GLIL-PGVGAFKDAmEQLNQTkltdfIKEEVAKGMPLLG 77
Cdd:pfam00117   2 LIDNGDSFTYNLARALRELGVEVTVvpnDTPAEEILEENpdGIILsGGPGSPGAA-GGAIEA-----IREARELKIPILG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824742   78 ICLGMQLLFEESdengvtkGLELLKGRveripgitaegqtyKVPHMGWNSLDFHQQSALLDGISEG-HVYFVHSYYVKTN 156
Cdd:pfam00117  76 ICLGHQLLALAF-------GGKVVKAK--------------KFGHHGKNSPVGDDGCGLFYGLPNVfIVRRYHSYAVDPD 134

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 502824742  157 ---DQDVLLATSPYDVEVPAVVGKEH-VFGTQFHPEK-SSAIGMQMLqnyANFLEK 207
Cdd:pfam00117 135 tlpDGLEVTATSENDGTIMGIRHKKLpIFGVQFHPESiLTPHGPEIL---FNFFIK 187
 
Name Accession Description Interval E-value
hisH PRK13141
imidazole glycerol phosphate synthase subunit HisH; Provisional
 1-208 7.06e-126

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237288 [Multi-domain]  Cd Length: 205  Bit Score: 353.67  E-value: 7.06e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824742   1 MIGIIDYGMGNLYSVSKALERLNYDYIISADPAELRKAKGLILPGVGAFKDAMEQLNQTKLTDFIKEEVAKGMPLLGICL 80
Cdd:PRK13141   1 MIAIIDYGMGNLRSVEKALERLGAEAVITSDPEEILAADGVILPGVGAFPDAMANLRERGLDEVIKEAVASGKPLLGICL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824742  81 GMQLLFEESDENGVTKGLELLKGRVERIPgitaEGQTYKVPHMGWNSLDFHQQSALLDGISEG-HVYFVHSYYVKTNDQD 159
Cdd:PRK13141  81 GMQLLFESSEEFGETEGLGLLPGRVRRFP----PEEGLKVPHMGWNQLELKKESPLLKGIPDGaYVYFVHSYYADPCDEE 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 502824742 160 VLLATSPYDVEVPAVVGKEHVFGTQFHPEKSSAIGMQMLQNYANFLEKR 208
Cdd:PRK13141 157 YVAATTDYGVEFPAAVGKDNVFGAQFHPEKSGDVGLKILKNFVEMVEEC 205
HisH COG0118
Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH [Amino acid ...
 1-199 2.90e-118

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: 334.31  E-value: 2.90e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824742   1 MIGIIDYGMGNLYSVSKALERLNYDYIISADPAELRKAKGLILPGVGAFKDAMEQLNQTKLTDFIKEEVAKGMPLLGICL 80
Cdd:COG0118    2 MIAIIDYGMGNLRSVAKALERLGAEVVVTSDPDEIRAADRLVLPGVGAFGDAMENLRERGLDEAIREAVAGGKPVLGICL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824742  81 GMQLLFEESDENGVTKGLELLKGRVERIPgitaeGQTYKVPHMGWNSLDFHQQSALLDGISEG-HVYFVHSYYVKTNDQD 159
Cdd:COG0118   82 GMQLLFERSEENGDTEGLGLIPGEVVRFP-----ASDLKVPHMGWNTVEIAKDHPLFAGIPDGeYFYFVHSYYVPPDDPE 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 502824742 160 VLLATSPYDVEVPAVVGKEHVFGTQFHPEKSSAIGMQMLQ 199
Cdd:COG0118  157 DVVATTDYGVPFTAAVERGNVFGTQFHPEKSGAAGLRLLK 196
GATase1_IGP_Synthase cd01748
Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate ...
 2-200 1.95e-109

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: 311.74  E-value: 1.95e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824742   2 IGIIDYGMGNLYSVSKALERLNYDYIISADPAELRKAKGLILPGVGAFKDAMEQLNQTKLTDFIKEEVAKGMPLLGICLG 81
Cdd:cd01748    1 IAIIDYGMGNLRSVANALERLGAEVIITSDPEEILSADKLILPGVGAFGDAMANLRERGLIEALKEAIASGKPFLGICLG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824742  82 MQLLFEESDENGVTKGLELLKGRVERIPgitaEGQTYKVPHMGWNSLDFHQQSALLDGISEG-HVYFVHSYYVKTNDQDV 160
Cdd:cd01748   81 MQLLFESSEEGGGTKGLGLIPGKVVRFP----ASEGLKVPHMGWNQLEITKESPLFKGIPDGsYFYFVHSYYAPPDDPDY 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 502824742 161 LLATSPYDVEVPAVVGKEHVFGTQFHPEKSSAIGMQMLQN 200
Cdd:cd01748  157 ILATTDYGGKFPAAVEKDNIFGTQFHPEKSGKAGLKLLKN 196
hisH PRK13181
imidazole glycerol phosphate synthase subunit HisH; Provisional
 1-202 7.25e-97

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 183878 [Multi-domain]  Cd Length: 199  Bit Score: 280.21  E-value: 7.25e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824742   1 MIGIIDYGMGNLYSVSKALERLNYDYIISADPAELRKAKGLILPGVGAFKDAMEQLNQTKLTDFIKEEVAKGMPLLGICL 80
Cdd:PRK13181   1 MIAIIDYGAGNLRSVANALKRLGVEAVVSSDPEEIAGADKVILPGVGAFGQAMRSLRESGLDEALKEHVEKKQPVLGICL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824742  81 GMQLLFEESDEnGVTKGLELLKGRVERIPGItaegqTYKVPHMGWNSLDFHQQSALLDGISEG-HVYFVHSYYVKTNDQD 159
Cdd:PRK13181  81 GMQLLFESSEE-GNVKGLGLIPGDVKRFRSE-----PLKVPQMGWNSVKPLKESPLFKGIEEGsYFYFVHSYYVPCEDPE 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 502824742 160 VLLATSPYDVEVPAVVGKEHVFGTQFHPEKSSAIGMQMLQNYA 202
Cdd:PRK13181 155 DVLATTEYGVPFCSAVAKDNIYAVQFHPEKSGKAGLKLLKNFA 197
hisH PRK13143
imidazole glycerol phosphate synthase subunit HisH; Provisional
 1-205 4.12e-95

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237289 [Multi-domain]  Cd Length: 200  Bit Score: 275.59  E-value: 4.12e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824742   1 MIGIIDYGMGNLYSVSKALERLNYDYIISADPAELRKAKGLILPGVGAFKDAMEQLNqtKLTDFIKEEVAKGMPLLGICL 80
Cdd:PRK13143   2 MIVIIDYGVGNLRSVSKALERAGAEVVITSDPEEILDADGIVLPGVGAFGAAMENLS--PLRDVILEAARSGKPFLGICL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824742  81 GMQLLFEESDENGVTKGLELLKGRVERIPGitaegqTYKVPHMGWNSLDFHQQSALLDGISEGHVYFVHSYYVKTNDQDV 160
Cdd:PRK13143  80 GMQLLFESSEEGGGVRGLGLFPGRVVRFPA------GVKVPHMGWNTVKVVKDCPLFEGIDGEYVYFVHSYYAYPDDEDY 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 502824742 161 LLATSPYDVEVPAVVGKEHVFGTQFHPEKSSAIGMQMLQNYANFL 205
Cdd:PRK13143 154 VVATTDYGIEFPAAVCNDNVFGTQFHPEKSGETGLKILENFVELI 198
hisH PRK13146
imidazole glycerol phosphate synthase subunit HisH; Provisional
 2-206 1.49e-92

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237290 [Multi-domain]  Cd Length: 209  Bit Score: 269.73  E-value: 1.49e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824742   2 IGIIDYGMGNLYSVSKALERL--NYDYIISADPAELRKAKGLILPGVGAFKDAMEQLNQTKLTDFIKEEV-AKGMPLLGI 78
Cdd:PRK13146   4 VAIIDYGSGNLRSAAKALERAgaGADVVVTADPDAVAAADRVVLPGVGAFADCMRGLRAVGLGEAVIEAVlAAGRPFLGI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824742  79 CLGMQLLFEESDENGVTKGLELLKGRVERIpgiTAEGQTYKVPHMGWNSLDFHQQSALLDGISEG-HVYFVHSYYVKTND 157
Cdd:PRK13146  84 CVGMQLLFERGLEHGDTPGLGLIPGEVVRF---QPDGPALKVPHMGWNTVDQTRDHPLFAGIPDGaRFYFVHSYYAQPAN 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 502824742 158 QDVLLATSPYDVEVPAVVGKEHVFGTQFHPEKSSAIGMQMLqnyANFLE 206
Cdd:PRK13146 161 PADVVAWTDYGGPFTAAVARDNLFATQFHPEKSQDAGLALL---RNFLA 206
IMP_synth_hisH TIGR01855
imidazole glycerol phosphate synthase, glutamine amidotransferase subunit; This model ...
 2-202 2.65e-86

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: 253.40  E-value: 2.65e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824742    2 IGIIDYGMGNLYSVSKALERLNYDYIISADPAELRKAKGLILPGVGAFKDAMEQLNQTKLTDFIKEEVAKGMPLLGICLG 81
Cdd:TIGR01855   1 IVIIDYGVGNLGSVKRALKRVGAEPVVVKDSKEAELADKLILPGVGAFGAAMARLRENGLDLFVELVVRLGKPVLGICLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824742   82 MQLLFEESDENGVTKGLELLKGRVERIpgitaegQTYKVPHMGWNSLDFHQQSALLDGISEG-HVYFVHSYYVKTNDQDV 160
Cdd:TIGR01855  81 MQLLFERSEEGGGVPGLGLIKGNVVKL-------EARKVPHMGWNEVHPVKESPLLNGIDEGaYFYFVHSYYAVCEEEAV 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 502824742  161 lLATSPYDVEVPAVVGKEHVFGTQFHPEKSSAIGMQMLQNYA 202
Cdd:TIGR01855 154 -LAYADYGEKFPAAVQKGNIFGTQFHPEKSGKTGLKLLENFL 194
hisH PRK13170
imidazole glycerol phosphate synthase subunit HisH; Provisional
 1-206 2.26e-69

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 183877 [Multi-domain]  Cd Length: 196  Bit Score: 210.48  E-value: 2.26e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824742   1 MIGIIDYGMGNLYSVSKALERLNYDYIISADPAELRKAKGLILPGVGAFKDAMEQLNQTKLTDFIKeevAKGMPLLGICL 80
Cdd:PRK13170   2 NVVIIDTGCANLSSVKFAIERLGYEPVVSRDPDVILAADKLFLPGVGTAQAAMDQLRERELIDLIK---ACTQPVLGICL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824742  81 GMQLLFEESDENGVTKGLELLKGRVERIPgitaeGQTYKVPHMGWNSLDFHQQSALLDGISEG-HVYFVHSYYVKTNdqD 159
Cdd:PRK13170  79 GMQLLGERSEESGGVDCLGIIDGPVKKMT-----DFGLPLPHMGWNQVTPQAGHPLFQGIEDGsYFYFVHSYAMPVN--E 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 502824742 160 VLLATSPYDVEVPAVVGKEHVFGTQFHPEKSSAIGMQMLQnyaNFLE 206
Cdd:PRK13170 152 YTIAQCNYGEPFSAAIQKDNFFGVQFHPERSGAAGAQLLK---NFLE 195
PLN02617 PLN02617
imidazole glycerol phosphate synthase hisHF
 4-210 6.44e-65

imidazole glycerol phosphate synthase hisHF


Pssm-ID: 178226 [Multi-domain]  Cd Length: 538  Bit Score: 209.18  E-value: 6.44e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824742   4 IIDYGMGNLYSVSKALERLNYDYIISADPAELRKAKGLILPGVGAFKDAMEQLNQTKLTDFIKEEVAKGMPLLGICLGMQ 83
Cdd:PLN02617  11 LLDYGAGNVRSVRNAIRHLGFTIKDVQTPEDILNADRLIFPGVGAFGSAMDVLNNRGMAEALREYIQNDRPFLGICLGLQ 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824742  84 LLFEESDENGVTKGLELLKGRVERIPgitaEGQTYKVPHMGWNSLDFHQQSALLDGISEGHVYFVHSYY-VKTND-QDVL 161
Cdd:PLN02617  91 LLFESSEENGPVEGLGVIPGVVGRFD----SSNGLRVPHIGWNALQITKDSELLDGVGGRHVYFVHSYRaTPSDEnKDWV 166

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 502824742 162 LATSPYDVEVPAVVGKEHVFGTQFHPEKSSAIGMQMLQnyaNFLEKRSP 210
Cdd:PLN02617 167 LATCNYGGEFIASVRKGNVHAVQFHPEKSGATGLSILR---RFLEPKSS 212
hisH PRK13152
imidazole glycerol phosphate synthase subunit HisH; Provisional
 1-202 2.65e-62

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 171876 [Multi-domain]  Cd Length: 201  Bit Score: 192.75  E-value: 2.65e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824742   1 MIGIIDYGMGNLYSVSKALERLNYDYIISADPAELRKAKGLILPGVGAFKDAMEQLNQTKLTDFIKEEV-AKGMPLLGIC 79
Cdd:PRK13152   1 MIALIDYKAGNLNSVAKAFEKIGAINFIAKNPKDLQKADKLLLPGVGSFKEAMKNLKELGFIEALKEQVlVQKKPILGIC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824742  80 LGMQLLFEESDENGVTKGLELLKGRVERIpgitAEGQTYKVPHMGWNSLDFHQQSALLDGISEG-HVYFVHSYYVKTNDQ 158
Cdd:PRK13152  81 LGMQLFLERGYEGGVCEGLGFIEGEVVKF----EEDLNLKIPHMGWNELEILKQSPLYQGIPEKsDFYFVHSFYVKCKDE 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 502824742 159 DVlLATSPYDVEVPAVVGKEHVFGTQFHPEKSSAIGMQMLQNYA 202
Cdd:PRK13152 157 FV-SAKAQYGHKFVASLQKDNIFATQFHPEKSQNLGLKLLENFA 199
hisH CHL00188
imidazole glycerol phosphate synthase subunit hisH; Provisional
 2-201 1.48e-60

imidazole glycerol phosphate synthase subunit hisH; Provisional


Pssm-ID: 214389 [Multi-domain]  Cd Length: 210  Bit Score: 188.56  E-value: 1.48e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824742   2 IGIIDYGMGNLYSVSKALERLNYDYIISADPAELRKAKGLILPGVGAFKDAMEQLNQTKLTDFIKEEVAKGMPLLGICLG 81
Cdd:CHL00188   4 IGIIDYSMGNLHSVSRAIQQAGQQPCIINSESELAQVHALVLPGVGSFDLAMKKLEKKGLITPIKKWIAEGNPFIGICLG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824742  82 MQLLFEESDEnGVTKGLELLKGRVERIPGITAEgqtyKVPHMGWNSLDFHQ------QSALLDGIS-EGHVYFVHSYYVK 154
Cdd:CHL00188  84 LHLLFETSEE-GKEEGLGIYKGQVKRLKHSPVK----VIPHMGWNRLECQNsecqnsEWVNWKAWPlNPWAYFVHSYGVM 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 502824742 155 TNDQDVLLATSPYD-VEVPAVVGKEHVFGTQFHPEKSSAIGMQMLQNY 201
Cdd:CHL00188 159 PKSQACATTTTFYGkQQMVAAIEYDNIFAMQFHPEKSGEFGLWLLREF 206
hisH PRK14004
imidazole glycerol phosphate synthase subunit HisH; Provisional
 1-205 1.99e-57

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 172505 [Multi-domain]  Cd Length: 210  Bit Score: 180.48  E-value: 1.99e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824742   1 MIGIIDYGMGNLYSVSKALERLNYDYIISADPAELRKAKGLILPGVGAFKDAMEQLNQTKLTDFIKEEVAKGMPLLGICL 80
Cdd:PRK14004   1 MIAILDYGMGNIHSCLKAVSLYTKDFVFTSDPETIENSKALILPGDGHFDKAMENLNSTGLRSTIDKHVESGKPLFGICI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824742  81 GMQLLFEESDE-NGVTK-----GLELLKGRVERIpgitaEGQTYKVPHMGWNSLDFHQQ--SALLDGI-SEGHVYFVHSY 151
Cdd:PRK14004  81 GFQILFESSEEtNQGTKkeqieGLGYIKGKIKKF-----EGKDFKVPHIGWNRLQIRRKdkSKLLKGIgDQSFFYFIHSY 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 502824742 152 YVKTNDQDVLLATSPYDVE-VPAVVGKEHVFGTQFHPEKSSAIGMQMLQNYANFL 205
Cdd:PRK14004 156 RPTGAEGNAITGLCDYYQEkFPAVVEKENIFGTQFHPEKSHTHGLKLLENFIEFV 210
hisH PRK13142
imidazole glycerol phosphate synthase subunit HisH; Provisional
 1-198 9.14e-54

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 171871 [Multi-domain]  Cd Length: 192  Bit Score: 170.77  E-value: 9.14e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824742   1 MIGIIDYGMGNLYSVSKALERLNYDYIISADPAELRKAKGLILPGVGAFKDAMEQLNQTKLTDFIKEEVAKgmPLLGICL 80
Cdd:PRK13142   1 MIVIVDYGLGNISNVKRAIEHLGYEVVVSNTSKIIDQAETIILPGVGHFKDAMSEIKRLNLNAILAKNTDK--KMIGICL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824742  81 GMQLLFEESDEnGVTKGLELLKGRVERIpgitaegQT-YKVPHMGWNSLDFHQQSALLDgiseghVYFVHSYYVKTNDQd 159
Cdd:PRK13142  79 GMQLMYEHSDE-GDASGLGFIPGNISRI-------QTeYPVPHLGWNNLVSKHPMLNQD------VYFVHSYQAPMSEN- 143

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 502824742 160 vLLATSPYDVEVPAVVGKEHVFGTQFHPEKSSAIGMQML 198
Cdd:PRK13142 144 -VIAYAQYGADIPAIVQFNNYIGIQFHPEKSGTYGLQIL 181
GATase pfam00117
Glutamine amidotransferase class-I;
4-207 1.53e-26

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 100.39  E-value: 1.53e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824742    4 IIDYGMGNLYSVSKALERLNYDYII---SADPAELRKAK--GLIL-PGVGAFKDAmEQLNQTkltdfIKEEVAKGMPLLG 77
Cdd:pfam00117   2 LIDNGDSFTYNLARALRELGVEVTVvpnDTPAEEILEENpdGIILsGGPGSPGAA-GGAIEA-----IREARELKIPILG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824742   78 ICLGMQLLFEESdengvtkGLELLKGRveripgitaegqtyKVPHMGWNSLDFHQQSALLDGISEG-HVYFVHSYYVKTN 156
Cdd:pfam00117  76 ICLGHQLLALAF-------GGKVVKAK--------------KFGHHGKNSPVGDDGCGLFYGLPNVfIVRRYHSYAVDPD 134

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 502824742  157 ---DQDVLLATSPYDVEVPAVVGKEH-VFGTQFHPEK-SSAIGMQMLqnyANFLEK 207
Cdd:pfam00117 135 tlpDGLEVTATSENDGTIMGIRHKKLpIFGVQFHPESiLTPHGPEIL---FNFFIK 187
GuaA1 COG0518
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ...
 28-208 1.28e-14

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: 69.97  E-value: 1.28e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824742  28 ISADPAELRKAKGLIL---PGvGAFkDAMEQLNQTKltDFIKEEVAKGMPLLGICLGMQLLfeesdengvtkgLELLKGR 104
Cdd:COG0518   39 ILPYDPDLEDPDGLILsggPM-SVY-DEDPWLEDEP--ALIREAFELGKPVLGICYGAQLL------------AHALGGK 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824742 105 VERIPGitaegqtykvPHMGWNSLDFHQQSALLDGISEG-HVYFVHSYYVKTNDQD-VLLATSPyDVEVPAVVGKEHVFG 182
Cdd:COG0518  103 VEPGPG----------REIGWAPVELTEADPLFAGLPDEfTVWMSHGDTVTELPEGaEVLASSD-NCPNQAFRYGRRVYG 171

                        170       180
                 ....*....|....*....|....*.
gi 502824742 183 TQFHPEKSSAIGMQMLQNYANFLEKR 208
Cdd:COG0518  172 VQFHPEVTHTMMEAWLEERADELAAE 197
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 2-86 2.66e-13

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: 63.77  E-value: 2.66e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824742   2 IGIIDYGMGN---LYSVSKALERLNYDY-IISADP------AELRKAKGLILPGVGAFKDAMEqlNQTKLTDFIKEEVAK 71
Cdd:cd01653    1 VAVLLFPGFEeleLASPLDALREAGAEVdVVSPDGgpvesdVDLDDYDGLILPGGPGTPDDLA--RDEALLALLREAAAA 78

                         90
                 ....*....|....*
gi 502824742  72 GMPLLGICLGMQLLF 86
Cdd:cd01653   79 GKPILGICLGAQLLV 93
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 2-85 1.06e-12

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: 61.45  E-value: 1.06e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824742   2 IGIIDYGMGN---LYSVSKALERLNYDY-IISADP------AELRKAKGLILPGVGAFKDAMEqlNQTKLTDFIKEEVAK 71
Cdd:cd03128    1 VAVLLFGGSEeleLASPLDALREAGAEVdVVSPDGgpvesdVDLDDYDGLILPGGPGTPDDLA--WDEALLALLREAAAA 78

                         90
                 ....*....|....
gi 502824742  72 GMPLLGICLGMQLL 85
Cdd:cd03128   79 GKPVLGICLGAQLL 92
guaA PRK00074
GMP synthase; Reviewed
 72-202 2.97e-11

GMP synthase; Reviewed


Pssm-ID: 234614 [Multi-domain]  Cd Length: 511  Bit Score: 61.99  E-value: 2.97e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824742  72 GMPLLGICLGMQLLfeesdengvtkgLELLKGRVERipGITAE-GQTykvphmgwnSLDFHQQSALLDGISEGH-VYFVH 149
Cdd:PRK00074  75 GVPVLGICYGMQLM------------AHQLGGKVER--AGKREyGRA---------ELEVDNDSPLFKGLPEEQdVWMSH 131

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 502824742 150 SYYVKTNDQD-VLLATSPyDVEVPAVVGKE-HVFGTQFHPE-KSSAIGMQMLQNYA 202
Cdd:PRK00074 132 GDKVTELPEGfKVIASTE-NCPIAAIANEErKFYGVQFHPEvTHTPQGKKLLENFV 186
GATase1_Anthranilate_Synthase cd01743
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ...
 11-205 5.74e-11

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: 59.09  E-value: 5.74e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824742  11 NLYSVskaLERLNYDYI------ISADPAELRKAKGLIL-PGVGAFKDAmeqlnqtKLTDFIKEEVAKGMPLLGICLGMQ 83
Cdd:cd01743   13 NLVQY---LRELGAEVVvvrndeITLEELELLNPDAIVIsPGPGHPEDA-------GISLEIIRALAGKVPILGVCLGHQ 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824742  84 LLFEEsdengvtkglelLKGRVERIPgitaegqtykVPHMGWNSLDFHQQSALLDGISEG-HVYFVHSYYVK--TNDQDV 160
Cdd:cd01743   83 AIAEA------------FGGKVVRAP----------EPMHGKTSEIHHDGSGLFKGLPQPfTVGRYHSLVVDpdPLPDLL 140

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 502824742 161 LLATSPYDVEVPAVVGKEH-VFGTQFHPEkS--SAIGMQMLqnyANFL 205
Cdd:cd01743  141 EVTASTEDGVIMALRHRDLpIYGVQFHPE-SilTEYGLRLL---ENFL 184
GATase1_1 cd01741
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 60-189 1.55e-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: 58.03  E-value: 1.55e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824742  60 KLTDFIKEEVAKGMPLLGICLGMQLLfeesdengvtkgLELLKGRVERIPgitaegqtyKVPHMGWNSLDFHQQSA---- 135
Cdd:cd01741   69 KLKELIRQALAAGKPVLGICLGHQLL------------ARALGGKVGRNP---------KGWEIGWFPVTLTEAGKadpl 127

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 502824742 136 LLDGISEGHVYFVHSYYVKTNDQD-VLLATSPYDvEVPAVVGKEHVFGTQFHPEK 189
Cdd:cd01741  128 FAGLPDEFPVFHWHGDTVVELPPGaVLLASSEAC-PNQAFRYGDRALGLQFHPEE 181
PabA COG0512
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ...
 28-206 5.48e-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: 53.50  E-value: 5.48e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824742  28 ISADPAELRKAKGLIL-PGVGAFKDAMeqlnqtKLTDFIKEeVAKGMPLLGICLGMQLLfeesdenGVTKGlellkGRVE 106
Cdd:COG0512   33 ITLEEIEALAPDGIVLsPGPGTPEEAG------ISLEVIRA-FAGKIPILGVCLGHQAI-------GEAFG-----GKVV 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824742 107 RIPGItAEGQTYKVphmgwnsldFHQQSALLDGISEGHV---YfvHSYYVKTND-QDVL--LATSPyDVEVPAVVGKEH- 179
Cdd:COG0512   94 RAPEP-MHGKTSPI---------THDGSGLFAGLPNPFTatrY--HSLVVDRETlPDELevTAWTE-DGEIMGIRHRELp 160

                        170       180
                 ....*....|....*....|....*....
gi 502824742 180 VFGTQFHPEkS--SAIGMQMLqnyANFLE 206
Cdd:COG0512  161 IEGVQFHPE-SilTEHGHQLL---ANFLE 185
PRK05670 PRK05670
anthranilate synthase component II; Provisional
 28-206 1.13e-08

anthranilate synthase component II; Provisional


Pssm-ID: 235552 [Multi-domain]  Cd Length: 189  Bit Score: 52.82  E-value: 1.13e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824742  28 ISADPAELRKAKGLIL-PGVGAFKDA--MEQLnqtkltdfIKEeVAKGMPLLGICLGMQLLfeesdenGVTKGlellkGR 104
Cdd:PRK05670  34 ITLEEIEALNPDAIVLsPGPGTPAEAgiSLEL--------IRE-FAGKVPILGVCLGHQAI-------GEAFG-----GK 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824742 105 VERIPgitaegqtyKVPHmGWNSLDFHQQSALLDGISEGhvyFV----HSYYV-KTNDQDVLLATSPY-DVEVPAVVGKE 178
Cdd:PRK05670  93 VVRAK---------EIMH-GKTSPIEHDGSGIFAGLPNP---FTvtryHSLVVdRESLPDCLEVTAWTdDGEIMGVRHKE 159

                        170       180       190
                 ....*....|....*....|....*....|.
gi 502824742 179 H-VFGTQFHPEkS--SAIGMQMLqnyANFLE 206
Cdd:PRK05670 160 LpIYGVQFHPE-SilTEHGHKLL---ENFLE 186
GATase1_CobQ cd01750
Type 1 glutamine amidotransferase (GATase1) domain found in Cobyric Acid Synthase (CobQ); Type ...
 2-101 6.16e-08

Type 1 glutamine amidotransferase (GATase1) domain found in Cobyric Acid Synthase (CobQ); Type 1 glutamine amidotransferase (GATase1) domain found in Cobyric Acid Synthase (CobQ). CobQ plays a role in cobalamin biosythesis. CobQ catalyses amidations at positions B, D, E, and G on adenosylcobyrinic A,C-diamide in the biosynthesis of cobalamin. CobQ belongs to the triad family of amidotransferases. Two of the three residues of the catalytic triad that are involved in glutamine binding, hydrolysis and transfer of the resulting ammonia to the acceptor substrate in other triad aminodotransferases are conserved in CobQ.


Pssm-ID: 153221 [Multi-domain]  Cd Length: 194  Bit Score: 50.71  E-value: 6.16e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824742   2 IGIIDYG-MGNlYSVSKALERL-NYDYIISADPAELRKAKGLILPGVGAFKDAMEQLNQTKLTDFIKEEVAKGMPLLGIC 79
Cdd:cd01750    1 IAVIRYPdISN-FTDLDPLAREpGVDVRYVEVPEGLGDADLIILPGSKDTIQDLAWLRKRGLAEAIKNYARAGGPVLGIC 79

                         90       100
                 ....*....|....*....|....*...
gi 502824742  80 LGMQLLFEE-SDENGVT-----KGLELL 101
Cdd:cd01750   80 GGYQMLGKYiVDPEGVEgpgeiEGLGLL 107
GATase1_PB cd01749
Glutamine Amidotransferase (GATase_I) involved in pyridoxine biosynthesis; Glutamine ...
 18-107 1.87e-07

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: 49.45  E-value: 1.87e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824742  18 ALERLNYDYIISADPAELRKAKGLILPG-----VGAFkdameqLNQTKLTDFIKEEVAKGMPLLGICLGMQLLFEESDEN 92
Cdd:cd01749   16 ALERLGVEVIEVRTPEDLEGIDGLIIPGgesttIGKL------LRRTGLLDPLREFIRAGKPVFGTCAGLILLAKEVEDQ 89

                         90
                 ....*....|....*
gi 502824742  93 GVTKGLELLKGRVER 107
Cdd:cd01749   90 GGQPLLGLLDITVRR 104
GATase1_GMP_Synthase cd01742
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine ...
 28-202 5.65e-07

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: 47.92  E-value: 5.65e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824742  28 ISADPAELRKAKGLILPG-------VGAFKdameqlnqtkltdfIKEEVAK-GMPLLGICLGMQLLfeeSDENGvtkgle 99
Cdd:cd01742   32 TPLEEIKLKNPKGIILSGgpssvyeEDAPR--------------VDPEIFElGVPVLGICYGMQLI---AKALG------ 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824742 100 llkGRVERipgitAEGQTYkvphmGWNSLDFHQQSALLDGISEG-HVYFVHSYYVKTNDQD-VLLATSPyDVEVPAVVGK 177
Cdd:cd01742   89 ---GKVER-----GDKREY-----GKAEIEIDDSSPLFEGLPDEqTVWMSHGDEVVKLPEGfKVIASSD-NCPVAAIANE 154

                        170       180
                 ....*....|....*....|....*..
gi 502824742 178 EH-VFGTQFHPE-KSSAIGMQMLQNYA 202
Cdd:cd01742  155 EKkIYGVQFHPEvTHTEKGKEILKNFL 181
PRK09065 PRK09065
glutamine amidotransferase; Provisional
 60-193 1.82e-06

glutamine amidotransferase; Provisional


Pssm-ID: 181635 [Multi-domain]  Cd Length: 237  Bit Score: 46.88  E-value: 1.82e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824742  60 KLTDFIKEEVAKGMPLLGICLGMQLLfeesdengvtkgLELLKGRVERIPGitaeGQtykvpHMGWNSLDFH---QQSAL 136
Cdd:PRK09065  76 RTADWLRQAAAAGMPLLGICYGHQLL------------AHALGGEVGYNPA----GR-----ESGTVTVELHpaaADDPL 134

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 502824742 137 LDGI-SEGHVYFVHSYYVKTNDQD-VLLATSPYDvEVPAVVGKEHVFGTQFHPEKSSAI 193
Cdd:PRK09065 135 FAGLpAQFPAHLTHLQSVLRLPPGaVVLARSAQD-PHQAFRYGPHAWGVQFHPEFTAHI 192
PRK06490 PRK06490
glutamine amidotransferase; Provisional
 63-193 3.47e-06

glutamine amidotransferase; Provisional


Pssm-ID: 180590 [Multi-domain]  Cd Length: 239  Bit Score: 46.11  E-value: 3.47e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824742  63 DFIKEEV-------AKGMPLLGICLGMQLLFEEsdengvtkglelLKGRVERIPGITAEgqtykvphMGWNSLDFHQQSA 135
Cdd:PRK06490  70 DFIRREIdwisvplKENKPFLGICLGAQMLARH------------LGARVAPHPDGRVE--------IGYYPLRPTEAGR 129

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 502824742 136 LLDGISEgHVYFVHSYYVKTNDQDVLLATSpYDVEVPAVVGKEHVFGTQFHPEKSSAI 193
Cdd:PRK06490 130 ALMHWPE-MVYHWHREGFDLPAGAELLATG-DDFPNQAFRYGDNAWGLQFHPEVTRAM 185
guaA_Nterm TIGR00888
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine ...
 72-202 4.40e-06

GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine de novo biosynthesis is well-conserved. However, it appears to split into two separate polypeptide chains in most of the Archaea. This N-terminal region would be the smaller subunit. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]


Pssm-ID: 129966 [Multi-domain]  Cd Length: 188  Bit Score: 45.38  E-value: 4.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824742   72 GMPLLGICLGMQLLfeesdengvtkgLELLKGRVERipgitAEGQTYkvphmGWNSLDFHQQSALLDGI-SEGHVYFVHS 150
Cdd:TIGR00888  70 GVPVLGICYGMQLM------------AKQLGGEVGR-----AEKREY-----GKAELEILDEDDLFRGLpDESTVWMSHG 127

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 502824742  151 YYVKT--NDQDVLLATSPYDVEVPAVVGKEhVFGTQFHPE-KSSAIGMQMLQNYA 202
Cdd:TIGR00888 128 DKVKElpEGFKVLATSDNCPVAAMAHEEKP-IYGVQFHPEvTHTEYGNELLENFV 181
PLN02347 PLN02347
GMP synthetase
 63-201 5.85e-06

GMP synthetase


Pssm-ID: 215197 [Multi-domain]  Cd Length: 536  Bit Score: 46.22  E-value: 5.85e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824742  63 DFIKEevaKGMPLLGICLGMQLLfeesdengvtkgLELLKGRVEripgiTAEGQTYkvphmGWNSLDFHQQSALLDGISE 142
Cdd:PLN02347  80 DYCRE---RGVPVLGICYGMQLI------------VQKLGGEVK-----PGEKQEY-----GRMEIRVVCGSQLFGDLPS 134

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824742 143 GHVYFVhsyYVKTNDQDVLLatsPYDVEV------PAVVGKEH----VFGTQFHPEKS-SAIGMQMLQNY 201
Cdd:PLN02347 135 GETQTV---WMSHGDEAVKL---PEGFEVvaksvqGAVVAIENrerrIYGLQYHPEVThSPKGMETLRHF 198
PRK00784 PRK00784
cobyric acid synthase;
31-101 9.89e-06

cobyric acid synthase;


Pssm-ID: 234838 [Multi-domain]  Cd Length: 488  Bit Score: 45.46  E-value: 9.89e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502824742  31 DPAELRKAKGLILPGVGAFKDAMEQLNQTKLTDFIKEEVAKGMPLLGICLGMQLLFEE-SDENGV------TKGLELL 101
Cdd:PRK00784 284 PGEPLPDADLVILPGSKNTIADLAWLRESGWDEAIRAHARRGGPVLGICGGYQMLGRRiADPDGVegapgsVEGLGLL 361
PRK13527 PRK13527
glutamine amidotransferase subunit PdxT; Provisional
 2-107 1.10e-05

glutamine amidotransferase subunit PdxT; Provisional


Pssm-ID: 237412 [Multi-domain]  Cd Length: 200  Bit Score: 44.49  E-value: 1.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824742   2 IGIIDYgMGN----LYSVSKALERLNydyiISADPAELRKAK------GLILPG-----VGAFkdaMEQLNqtkLTDFIK 66
Cdd:PRK13527   3 IGVLAL-QGDveehIDALKRALDELG----IDGEVVEVRRPGdlpdcdALIIPGgesttIGRL---MKREG---ILDEIK 71

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 502824742  67 EEVAKGMPLLGICLGMQLLFEESDENGVTKG----LELLKGRVER 107
Cdd:PRK13527  72 EKIEEGLPILGTCAGLILLAKEVGDDRVTKTeqplLGLMDVTVKR 116
CobQ COG1492
Cobyric acid synthase [Coenzyme transport and metabolism]; Cobyric acid synthase is part of ...
 31-101 2.45e-05

Cobyric acid synthase [Coenzyme transport and metabolism]; Cobyric acid synthase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 441101 [Multi-domain]  Cd Length: 493  Bit Score: 44.28  E-value: 2.45e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502824742  31 DPAELRKAKGLILPGVGAFKDAMEQLNQTKLTDFIKEEVAKGMPLLGICLGMQLLFEE-SDENGV------TKGLELL 101
Cdd:COG1492  284 PPEELGDADLVILPGSKNTIADLAWLRESGLDDAIRAHARRGGPVLGICGGYQMLGRRiADPDGVeggageVPGLGLL 361
Peptidase_C26 pfam07722
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ...
 65-188 4.12e-05

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


Pssm-ID: 429620 [Multi-domain]  Cd Length: 219  Bit Score: 43.01  E-value: 4.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824742   65 IKEEVAKGMPLLGICLGMQLLfeesdeNGVTKGleLLKGRVERIPGITAE-GQTYKVPHMGWNSLDFHQQSAL--LDGIS 141
Cdd:pfam07722  98 IRAALARGKPILGICRGFQLL------NVALGG--TLYQDIQEQPGFTDHrEHCQVAPYAPSHAVNVEPGSLLasLLGSE 169

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 502824742  142 EGHVYFVHSYYVKTNDQDVLL-ATSPYDVeVPAVVGKEH---VFGTQFHPE 188
Cdd:pfam07722 170 EFRVNSLHHQAIDRLAPGLRVeAVAPDGT-IEAIESPNAkgfALGVQWHPE 219
PRK13525 PRK13525
pyridoxal 5'-phosphate synthase glutaminase subunit PdxT;
17-107 8.60e-05

pyridoxal 5'-phosphate synthase glutaminase subunit PdxT;


Pssm-ID: 237411 [Multi-domain]  Cd Length: 189  Bit Score: 41.68  E-value: 8.60e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824742  17 KALERLNYDYIISADPAELRKAKGLILPGvGAfKDAMEQL-NQTKLTDFIKEEVAKGMPLLGICLGMQLLFEESdENGVT 95
Cdd:PRK13525  18 AALEALGAEAVEVRRPEDLDEIDGLILPG-GE-STTMGKLlRDFGLLEPLREFIASGLPVFGTCAGMILLAKEI-EGYEQ 94

                         90
                 ....*....|..
gi 502824742  96 KGLELLKGRVER 107
Cdd:PRK13525  95 EHLGLLDITVRR 106
GATase_3 pfam07685
CobB/CobQ-like glutamine amidotransferase domain;
37-106 1.67e-04

CobB/CobQ-like glutamine amidotransferase domain;


Pssm-ID: 429595 [Multi-domain]  Cd Length: 189  Bit Score: 41.07  E-value: 1.67e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502824742   37 KAKGLILPGVGAFKDAMEQLNQTKLTDFIKEEVAKGMPLLGICLGMQLLFEE-SDENGVT-KGLELLKGRVE 106
Cdd:pfam07685  42 DADLIILPGGKPTIQDLALLRNSGMDEAIKEAAEDGGPVLGICGGYQMLGETiEDPEGVRiEGLGLLDIETV 113
PLP_synth_Pdx2 TIGR03800
pyridoxal 5'-phosphate synthase, glutaminase subunit Pdx2; Pyridoxal 5'-phosphate (PLP) is ...
 17-107 2.34e-04

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: 40.49  E-value: 2.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824742   17 KALERLNYDYIISADPAELRKAKGLILPGvGAFKDAMEQLNQTKLTDFIKEEVAKGMPLLGICLGMQLLFEESDENgvTK 96
Cdd:TIGR03800  16 RALEALGVEGVEVKRPEQLDEIDGLIIPG-GESTTISRLLDKYGMFEPLRNFILSGLPVFGTCAGLIMLAKEIIGQ--KE 92

                          90
                  ....*....|..
gi 502824742   97 G-LELLKGRVER 107
Cdd:TIGR03800  93 GqLGLLDMTVER 104
GATase1_FGAR_AT cd01740
Type 1 glutamine amidotransferase (GATase1)-like domain found in Formylglycinamide ...
 28-112 6.58e-04

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


Pssm-ID: 153211 [Multi-domain]  Cd Length: 238  Bit Score: 39.52  E-value: 6.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824742  28 ISADPAELRKAKGLILPG-------VGAFKDAMEQLnqtKLTDFIKEEVAKGMPLLGICLGMQLLFEesdengvtkgLEL 100
Cdd:cd01740   34 LLAGRKDLDDYDGVVLPGgfsygdyLRAGAIAAASP---LLMEEVKEFAERGGLVLGICNGFQILVE----------LGL 100

                         90
                 ....*....|..
gi 502824742 101 LKGRVERIPGIT 112
Cdd:cd01740  101 LPGALIRNKGLK 112
PRK12564 PRK12564
carbamoyl-phosphate synthase small subunit;
65-190 1.02e-03

carbamoyl-phosphate synthase small subunit;


Pssm-ID: 237139 [Multi-domain]  Cd Length: 360  Bit Score: 39.29  E-value: 1.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824742  65 IKEEVAKGMPLLGICLGMQLLfeesdengvtkglellkgrveripGITAEGQTYKVP--HMGWNsldfHqqsALLDGISe 142
Cdd:PRK12564 241 IRELLEKKIPIFGICLGHQLL------------------------ALALGAKTYKMKfgHRGAN----H---PVKDLET- 288

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502824742 143 GHVYFV---HSYYVKTNdqdvllaTSPYDVEVP-------AVVGKEH----VFGTQFHPEKS 190
Cdd:PRK12564 289 GKVEITsqnHGFAVDED-------SLPANLEVThvnlndgTVEGLRHkdlpAFSVQYHPEAS 343
PuuD COG2071
Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (putrescine degradation), contains ...
 65-85 1.18e-03

Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (putrescine degradation), contains GATase1-like domain [Amino acid transport and metabolism];


Pssm-ID: 441674 [Multi-domain]  Cd Length: 231  Bit Score: 38.61  E-value: 1.18e-03
                         10        20
                 ....*....|....*....|.
gi 502824742  65 IKEEVAKGMPLLGICLGMQLL 85
Cdd:COG2071   89 IRAALERGKPVLGICRGMQLL 109
CarA COG0505
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ...
 65-188 1.84e-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: 38.46  E-value: 1.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824742  65 IKEEVAKGMPLLGICLGMQLLfeesdengvtkglellkgrveripGITAEGQTYKVP--HMGWNsldfHqqsALLDgISE 142
Cdd:COG0505  240 IRELLGKGIPIFGICLGHQLL------------------------ALALGAKTYKLKfgHRGAN----H---PVKD-LET 287

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824742 143 GHVYFV---HSYYVktnDQDVLLATspyDVEVP-------AVVGKEH----VFGTQFHPE 188
Cdd:COG0505  288 GRVEITsqnHGFAV---DEDSLPAT---DLEVThvnlndgTVEGLRHkdlpAFSVQYHPE 341
PRK00758 PRK00758
GMP synthase subunit A; Validated
 1-188 2.52e-03

GMP synthase subunit A; Validated


Pssm-ID: 179112 [Multi-domain]  Cd Length: 184  Bit Score: 37.52  E-value: 2.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824742   1 MIGIIDYGMGNLYSVSKALERLNYDYII---SADPAELRK-AKGLILPGvGAfkdAMEQLNQTKltDFIKEEvakGMPLL 76
Cdd:PRK00758   1 KIVVVDNGGQYNHLIHRTLRYLGVDAKIipnTTPVEEIKAfEDGLILSG-GP---DIERAGNCP--EYLKEL---DVPIL 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824742  77 GICLGMQLLFEEsdengvtkglelLKGRVERipGITAE-GQTykvphmgwnSLDFHQQSALLDGI-SEGHVYFVHSYYVK 154
Cdd:PRK00758  72 GICLGHQLIAKA------------FGGEVGR--GEYGEyALV---------EVEILDEDDILKGLpPEIRVWASHADEVK 128

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 502824742 155 TNDQD-VLLATSpyDV-EVPAVVGKE-HVFGTQFHPE 188
Cdd:PRK00758 129 ELPDGfEILARS--DIcEVEAMKHKEkPIYGVQFHPE 163
GATase1_2 cd01745
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 65-85 2.58e-03

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: 153216 [Multi-domain]  Cd Length: 189  Bit Score: 37.56  E-value: 2.58e-03
                         10        20
                 ....*....|....*....|.
gi 502824742  65 IKEEVAKGMPLLGICLGMQLL 85
Cdd:cd01745   93 LRAALERGKPILGICRGMQLL 113
COG3442 COG3442
Glutamine amidotransferase related to the GATase domain of CobQ [General function prediction ...
 48-107 4.78e-03

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


Pssm-ID: 442666 [Multi-domain]  Cd Length: 241  Bit Score: 37.08  E-value: 4.78e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502824742  48 AFKDAMEQLNQTKltDFIKEEVAKGMPLLGICLGMQLL---FEESDENgVTKGLELLKGRVER 107
Cdd:COG3442   63 EQEIVADDLLRIK--DALRAAIEDGVPVLAICGGYQLLghyYETADGE-RIPGLGILDVYTVA 122
PRK03619 PRK03619
phosphoribosylformylglycinamidine synthase subunit PurQ;
34-87 9.64e-03

phosphoribosylformylglycinamidine synthase subunit PurQ;


Pssm-ID: 235140 [Multi-domain]  Cd Length: 219  Bit Score: 35.86  E-value: 9.64e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502824742  34 ELRKAKGLILPG------------VGAFKDAMEQlnqtkltdfIKEEVAKGMPLLGICLGMQLLFE 87
Cdd:PRK03619  38 DLDGVDAVVLPGgfsygdylrcgaIAAFSPIMKA---------VKEFAEKGKPVLGICNGFQILTE 94
 
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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