NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|262089297|gb|ACY24518|]
View 

GMP synthase/glutamine amidotransferase domain protein [uncultured crenarchaeote 57a5]

Protein Classification

type 1 glutamine amidotransferase( domain architecture ID 11424847)

type 1 glutamine amidotransferase may be involved in the hydrolysis of ammonia from glutamine and the transfer of the amino group to an acceptor substrate

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
GuaA1 COG0518
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ...
 9-210 1.85e-59

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: 186.30  E-value: 1.85e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089297   9 GFEIETKHVKKDSI---PQEVDNYAAIVILGGYMSVYQNLPFLEEQQKLIRNANHHQVPLLGICLGSQLIAQALGGRVYK 85
Cdd:COG0518   26 GIELDVLRVYAGEIlpyDPDLEDPDGLILSGGPMSVYDEDPWLEDEPALIREAFELGKPVLGICYGAQLLAHALGGKVEP 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089297  86 GQRKEIGWFEVKVNNEgrNDIFKGItNERIKVFQWHGDTY-ELPKSAILLASSNLYP-QAFKVGTSI-GILFHLEVTHEI 162
Cdd:COG0518  106 GPGREIGWAPVELTEA--DPLFAGL-PDEFTVWMSHGDTVtELPEGAEVLASSDNCPnQAFRYGRRVyGVQFHPEVTHTM 182

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 262089297 163 IRNWTSNYRLEMTEVGVSTDSILNnkkneFENLADNCKVVYSNFFKMI 210
Cdd:COG0518  183 MEAWLEERADELAAEELLAEASLH-----DPELREAGRRLLRNFLREI 225
 
Name Accession Description Interval E-value
GuaA1 COG0518
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ...
 9-210 1.85e-59

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: 186.30  E-value: 1.85e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089297   9 GFEIETKHVKKDSI---PQEVDNYAAIVILGGYMSVYQNLPFLEEQQKLIRNANHHQVPLLGICLGSQLIAQALGGRVYK 85
Cdd:COG0518   26 GIELDVLRVYAGEIlpyDPDLEDPDGLILSGGPMSVYDEDPWLEDEPALIREAFELGKPVLGICYGAQLLAHALGGKVEP 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089297  86 GQRKEIGWFEVKVNNEgrNDIFKGItNERIKVFQWHGDTY-ELPKSAILLASSNLYP-QAFKVGTSI-GILFHLEVTHEI 162
Cdd:COG0518  106 GPGREIGWAPVELTEA--DPLFAGL-PDEFTVWMSHGDTVtELPEGAEVLASSDNCPnQAFRYGRRVyGVQFHPEVTHTM 182

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 262089297 163 IRNWTSNYRLEMTEVGVSTDSILNnkkneFENLADNCKVVYSNFFKMI 210
Cdd:COG0518  183 MEAWLEERADELAAEELLAEASLH-----DPELREAGRRLLRNFLREI 225
GATase1_1 cd01741
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 8-166 1.05e-57

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: 180.52  E-value: 1.05e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089297   8 VGFEIETKHVKKDSIPQEVDNYAAIVILGGYMSV-YQNLPFLEEQQKLIRNANHHQVPLLGICLGSQLIAQALGGRVYKG 86
Cdd:cd01741   26 ETIEIDVVDVYAGELLPDLDDYDGLVILGGPMSVdEDDYPWLKKLKELIRQALAAGKPVLGICLGHQLLARALGGKVGRN 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089297  87 QRK-EIGWFEVKVNNEGRNDIFKGITNERIKVFQWHGDT-YELPKSAILLASSNLYP-QAFKVGTSI-GILFHLEvtHEI 162
Cdd:cd01741  106 PKGwEIGWFPVTLTEAGKADPLFAGLPDEFPVFHWHGDTvVELPPGAVLLASSEACPnQAFRYGDRAlGLQFHPE--ERL 183


                 ....
gi 262089297 163 IRNW 166
Cdd:cd01741  184 LRNF 187
PRK07053 PRK07053
glutamine amidotransferase; Provisional
 4-166 1.44e-42

glutamine amidotransferase; Provisional


Pssm-ID: 235919 [Multi-domain]  Cd Length: 234  Bit Score: 143.16  E-value: 1.44e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089297   4 LFESVGFEIETKHVKKDSIPQEVDNYAAI-VILGGYMSVYQ--NLPFLEEQQKLIRNANHHQVPLLGICLGSQLIAQALG 80
Cdd:PRK07053  22 VLGARGYRVRYVDVGVDDLETLDALEPDLlVVLGGPIGVYDdeLYPFLAPEIALLRQRLAAGLPTLGICLGAQLIARALG 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089297  81 GRVYKGQRKEIGWFEVKVNNEGRNDIFKGITNErIKVFQWHGDTYELPKSAILLASSNLYP-QAFKVGTSI-GILFHLEV 158
Cdd:PRK07053 102 ARVYPGGQKEIGWAPLTLTDAGRASPLRHLGAG-TPVLHWHGDTFDLPEGATLLASTPACRhQAFAWGNHVlALQFHPEA 180


                 ....*...
gi 262089297 159 THEIIRNW 166
Cdd:PRK07053 181 REDRFEAW 188
GATase pfam00117
Glutamine amidotransferase class-I;
5-166 1.04e-15

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 71.89  E-value: 1.04e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089297    5 FESVGFEIETkhVKKDSIPQEVD--NYAAIVILGGYMSVYqnlpFLEEQQKLIRNANHHQVPLLGICLGSQLIAQALGGR 82
Cdd:pfam00117  17 LRELGVEVTV--VPNDTPAEEILeeNPDGIILSGGPGSPG----AAGGAIEAIREARELKIPILGICLGHQLLALAFGGK 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089297   83 VYKGQRKEIGWFEVKVNNEGrNDIFKGiTNERIKVFQWHGDT---YELPKSAILLASS--NLYPQAFKVGTS--IGILFH 155
Cdd:pfam00117  91 VVKAKKFGHHGKNSPVGDDG-CGLFYG-LPNVFIVRRYHSYAvdpDTLPDGLEVTATSenDGTIMGIRHKKLpiFGVQFH 168

                         170
                  ....*....|....*.
gi 262089297  156 LEVTH-----EIIRNW 166
Cdd:pfam00117 169 PESILtphgpEILFNF 184
IMP_synth_hisH TIGR01855
imidazole glycerol phosphate synthase, glutamine amidotransferase subunit; This model ...
 2-166 3.95e-07

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: 48.48  E-value: 3.95e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089297    2 KKLFESVGFEIEtkhVKKDsiPQEVDNYAAIVI--LGGYMSVYQNLpfleEQQKLIRNANHH---QVPLLGICLGSQLIA 76
Cdd:TIGR01855  15 KRALKRVGAEPV---VVKD--SKEAELADKLILpgVGAFGAAMARL----RENGLDLFVELVvrlGKPVLGICLGMQLLF 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089297   77 Q---------ALG---GRVYKGQRK---EIGWFEVKVNNEgrNDIFKGItNERIKVFQWHgdTYELP-KSAILLASSNL- 139
Cdd:TIGR01855  86 ErseegggvpGLGlikGNVVKLEARkvpHMGWNEVHPVKE--SPLLNGI-DEGAYFYFVH--SYYAVcEEEAVLAYADYg 160

                         170       180       190
                  ....*....|....*....|....*....|...
gi 262089297  140 --YPQAFKVGTSIGILFHLEVTHE----IIRNW 166
Cdd:TIGR01855 161 ekFPAAVQKGNIFGTQFHPEKSGKtglkLLENF 193
 
Name Accession Description Interval E-value
GuaA1 COG0518
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ...
 9-210 1.85e-59

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: 186.30  E-value: 1.85e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089297   9 GFEIETKHVKKDSI---PQEVDNYAAIVILGGYMSVYQNLPFLEEQQKLIRNANHHQVPLLGICLGSQLIAQALGGRVYK 85
Cdd:COG0518   26 GIELDVLRVYAGEIlpyDPDLEDPDGLILSGGPMSVYDEDPWLEDEPALIREAFELGKPVLGICYGAQLLAHALGGKVEP 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089297  86 GQRKEIGWFEVKVNNEgrNDIFKGItNERIKVFQWHGDTY-ELPKSAILLASSNLYP-QAFKVGTSI-GILFHLEVTHEI 162
Cdd:COG0518  106 GPGREIGWAPVELTEA--DPLFAGL-PDEFTVWMSHGDTVtELPEGAEVLASSDNCPnQAFRYGRRVyGVQFHPEVTHTM 182

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 262089297 163 IRNWTSNYRLEMTEVGVSTDSILNnkkneFENLADNCKVVYSNFFKMI 210
Cdd:COG0518  183 MEAWLEERADELAAEELLAEASLH-----DPELREAGRRLLRNFLREI 225
GATase1_1 cd01741
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 8-166 1.05e-57

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: 180.52  E-value: 1.05e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089297   8 VGFEIETKHVKKDSIPQEVDNYAAIVILGGYMSV-YQNLPFLEEQQKLIRNANHHQVPLLGICLGSQLIAQALGGRVYKG 86
Cdd:cd01741   26 ETIEIDVVDVYAGELLPDLDDYDGLVILGGPMSVdEDDYPWLKKLKELIRQALAAGKPVLGICLGHQLLARALGGKVGRN 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089297  87 QRK-EIGWFEVKVNNEGRNDIFKGITNERIKVFQWHGDT-YELPKSAILLASSNLYP-QAFKVGTSI-GILFHLEvtHEI 162
Cdd:cd01741  106 PKGwEIGWFPVTLTEAGKADPLFAGLPDEFPVFHWHGDTvVELPPGAVLLASSEACPnQAFRYGDRAlGLQFHPE--ERL 183


                 ....
gi 262089297 163 IRNW 166
Cdd:cd01741  184 LRNF 187
PRK07053 PRK07053
glutamine amidotransferase; Provisional
 4-166 1.44e-42

glutamine amidotransferase; Provisional


Pssm-ID: 235919 [Multi-domain]  Cd Length: 234  Bit Score: 143.16  E-value: 1.44e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089297   4 LFESVGFEIETKHVKKDSIPQEVDNYAAI-VILGGYMSVYQ--NLPFLEEQQKLIRNANHHQVPLLGICLGSQLIAQALG 80
Cdd:PRK07053  22 VLGARGYRVRYVDVGVDDLETLDALEPDLlVVLGGPIGVYDdeLYPFLAPEIALLRQRLAAGLPTLGICLGAQLIARALG 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089297  81 GRVYKGQRKEIGWFEVKVNNEGRNDIFKGITNErIKVFQWHGDTYELPKSAILLASSNLYP-QAFKVGTSI-GILFHLEV 158
Cdd:PRK07053 102 ARVYPGGQKEIGWAPLTLTDAGRASPLRHLGAG-TPVLHWHGDTFDLPEGATLLASTPACRhQAFAWGNHVlALQFHPEA 180


                 ....*...
gi 262089297 159 THEIIRNW 166
Cdd:PRK07053 181 REDRFEAW 188
PRK06490 PRK06490
glutamine amidotransferase; Provisional
 20-174 4.03e-33

glutamine amidotransferase; Provisional


Pssm-ID: 180590 [Multi-domain]  Cd Length: 239  Bit Score: 118.91  E-value: 4.03e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089297  20 DSIPQEVDNYAAIVILGGYMSVYQNLPFLEEQQKLIRNANHHQVPLLGICLGSQLIAQALGGRVYKGQ--RKEIGWFEVK 97
Cdd:PRK06490  44 DPLPDTLEDHAGAVIFGGPMSANDPDDFIRREIDWISVPLKENKPFLGICLGAQMLARHLGARVAPHPdgRVEIGYYPLR 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089297  98 VNNEGRndifkGITNERIKVFQWHGDTYELPKSAILLASSNLYP-QAFKVG-TSIGILFHLEVTHEIIRNWT--SNYRLE 173
Cdd:PRK06490 124 PTEAGR-----ALMHWPEMVYHWHREGFDLPAGAELLATGDDFPnQAFRYGdNAWGLQFHPEVTRAMMHRWVvrGAHRLT 198


                 .
gi 262089297 174 M 174
Cdd:PRK06490 199 L 199
PRK00758 PRK00758
GMP synthase subunit A; Validated
 12-165 1.60e-20

GMP synthase subunit A; Validated


Pssm-ID: 179112 [Multi-domain]  Cd Length: 184  Bit Score: 84.52  E-value: 1.60e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089297  12 IETKHVKKDSIPQEVDNYAAIVILGGYmsvyqnlPFLEE---QQKLIRNANhhqVPLLGICLGSQLIAQALGGRVYKGQR 88
Cdd:PRK00758  24 VDAKIIPNTTPVEEIKAFEDGLILSGG-------PDIERagnCPEYLKELD---VPILGICLGHQLIAKAFGGEVGRGEY 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089297  89 KEIGWFEVKVNNEgrNDIFKGITNErIKVFQWHGD-TYELPKSAILLASSNLYP-QAFKVGT-SI-GILFHLEVTH---- 160
Cdd:PRK00758  94 GEYALVEVEILDE--DDILKGLPPE-IRVWASHADeVKELPDGFEILARSDICEvEAMKHKEkPIyGVQFHPEVAHteyg 170


                 ....*.
gi 262089297 161 -EIIRN 165
Cdd:PRK00758 171 eEIFKN 176
GATase1_GMP_Synthase cd01742
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine ...
 28-166 5.05e-19

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: 80.66  E-value: 5.05e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089297  28 NYAAIVILGGYMSVY-QNLPFLEEQqklIRNANhhqVPLLGICLGSQLIAQALGGRVYKGQRKEIGWFEVKVNNEgrNDI 106
Cdd:cd01742   41 NPKGIILSGGPSSVYeEDAPRVDPE---IFELG---VPVLGICYGMQLIAKALGGKVERGDKREYGKAEIEIDDS--SPL 112

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 262089297 107 FKGItNERIKVFQWHGDTY-ELPKSAILLASS-NLYPQAFKVGTS--IGILFHLEVTH-----EIIRNW 166
Cdd:cd01742  113 FEGL-PDEQTVWMSHGDEVvKLPEGFKVIASSdNCPVAAIANEEKkiYGVQFHPEVTHtekgkEILKNF 180
PRK08250 PRK08250
glutamine amidotransferase; Provisional
 6-137 6.14e-19

glutamine amidotransferase; Provisional


Pssm-ID: 181323 [Multi-domain]  Cd Length: 235  Bit Score: 81.55  E-value: 6.14e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089297   6 ESVGFEIETKHV-KKDSIPQEVDNYAAIVILGGYMS---VYQNLPFL--EEQQKLIRNANHHQVPLLGICLGSQLIAQAL 79
Cdd:PRK08250  22 ENRGYDISYSRVyAGEALPENADGFDLLIVMGGPQSprtTREECPYFdsKAEQRLINQAIKAGKAVIGVCLGAQLIGEAL 101

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 262089297  80 GGRVYKGQRKEIGWFEVKVNNEGRNDIFKGITNERIKVFQWHGDTYELPKSAILLASS 137
Cdd:PRK08250 102 GAKYEHSPEKEIGYFPITLTEAGLKDPLLSHFGSTLTVGHWHNDMPGLTDQAKVLATS 159
PRK09065 PRK09065
glutamine amidotransferase; Provisional
 27-164 2.74e-18

glutamine amidotransferase; Provisional


Pssm-ID: 181635 [Multi-domain]  Cd Length: 237  Bit Score: 80.01  E-value: 2.74e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089297  27 DNYAAIVILGGYMSVYQNLPFLEEQQKLIRNANHHQVPLLGICLGSQLIAQALGGRV-YKGQRKEIGWFEVKVNNEGRND 105
Cdd:PRK09065  53 DDFAGVIITGSWAMVTDRLDWSERTADWLRQAAAAGMPLLGICYGHQLLAHALGGEVgYNPAGRESGTVTVELHPAAADD 132

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 262089297 106 -IFKGITnERIKVFQWHGDT-YELPKSAILLASSNLYP-QAFKVGTSI-GILFHLEVTHEIIR 164
Cdd:PRK09065 133 pLFAGLP-AQFPAHLTHLQSvLRLPPGAVVLARSAQDPhQAFRYGPHAwGVQFHPEFTAHIMR 194
guaA PRK00074
GMP synthase; Reviewed
 28-176 9.45e-18

GMP synthase; Reviewed


Pssm-ID: 234614 [Multi-domain]  Cd Length: 511  Bit Score: 80.86  E-value: 9.45e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089297  28 NYAAIVILGGYMSVYQ-NLPFLEEQqklIRNANhhqVPLLGICLGSQLIAQALGGRVYKGQRKEIGWFEVKVNNEgrNDI 106
Cdd:PRK00074  46 NPKGIILSGGPASVYEeGAPRADPE---IFELG---VPVLGICYGMQLMAHQLGGKVERAGKREYGRAELEVDND--SPL 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089297 107 FKGITnERIKVfqW--HGDT-YELPKSAILLASS-------------NLYpqafkvgtsiGILFHLEVTH-----EIIRN 165
Cdd:PRK00074 118 FKGLP-EEQDV--WmsHGDKvTELPEGFKVIASTencpiaaianeerKFY----------GVQFHPEVTHtpqgkKLLEN 184

                        170       180
                 ....*....|....*....|...
gi 262089297 166 -----------WT-SNYRLEMTE 176
Cdd:PRK00074 185 fvfdicgckgdWTmENFIEEAIE 207
GATase pfam00117
Glutamine amidotransferase class-I;
5-166 1.04e-15

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 71.89  E-value: 1.04e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089297    5 FESVGFEIETkhVKKDSIPQEVD--NYAAIVILGGYMSVYqnlpFLEEQQKLIRNANHHQVPLLGICLGSQLIAQALGGR 82
Cdd:pfam00117  17 LRELGVEVTV--VPNDTPAEEILeeNPDGIILSGGPGSPG----AAGGAIEAIREARELKIPILGICLGHQLLALAFGGK 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089297   83 VYKGQRKEIGWFEVKVNNEGrNDIFKGiTNERIKVFQWHGDT---YELPKSAILLASS--NLYPQAFKVGTS--IGILFH 155
Cdd:pfam00117  91 VVKAKKFGHHGKNSPVGDDG-CGLFYG-LPNVFIVRRYHSYAvdpDTLPDGLEVTATSenDGTIMGIRHKKLpiFGVQFH 168

                         170
                  ....*....|....*.
gi 262089297  156 LEVTH-----EIIRNW 166
Cdd:pfam00117 169 PESILtphgpEILFNF 184
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 3-75 7.48e-11

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: 56.83  E-value: 7.48e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 262089297   3 KLFESVGFEIETKHVKKDSIPQEVD--NYAAIVILGGYMSVYqNLPFLEEQQKLIRNANHHQVPLLGICLGSQLI 75
Cdd:cd03128   19 DALREAGAEVDVVSPDGGPVESDVDldDYDGLILPGGPGTPD-DLAWDEALLALLREAAAAGKPVLGICLGAQLL 92
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 3-75 9.37e-11

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: 56.84  E-value: 9.37e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 262089297   3 KLFESVGFEIETKHVKKDSIPQEVD--NYAAIVILGGYMSVYqNLPFLEEQQKLIRNANHHQVPLLGICLGSQLI 75
Cdd:cd01653   19 DALREAGAEVDVVSPDGGPVESDVDldDYDGLILPGGPGTPD-DLARDEALLALLREAAAAGKPILGICLGAQLL 92
PLN02347 PLN02347
GMP synthetase
 32-165 1.40e-10

GMP synthetase


Pssm-ID: 215197 [Multi-domain]  Cd Length: 536  Bit Score: 60.08  E-value: 1.40e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089297  32 IVIL-GGYMSVY-QNLP-FLEEQQKLIRNANhhqVPLLGICLGSQLIAQALGGRVYKGQRKEIGWFEVKVnneGRNDIFK 108
Cdd:PLN02347  56 VVILsGGPHSVHvEGAPtVPEGFFDYCRERG---VPVLGICYGMQLIVQKLGGEVKPGEKQEYGRMEIRV---VCGSQLF 129

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 262089297 109 GITNERIKVFQW--HGD-TYELPKSAILLASS---------NLYPQAFkvgtsiGILFHLEVTH-----EIIRN 165
Cdd:PLN02347 130 GDLPSGETQTVWmsHGDeAVKLPEGFEVVAKSvqgavvaieNRERRIY------GLQYHPEVTHspkgmETLRH 197
GATase1_Anthranilate_Synthase cd01743
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ...
 4-166 1.32e-08

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: 52.54  E-value: 1.32e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089297   4 LFESVGFEIETkhVKKDSIPQEV---DNYAAIVI---------LGGYMSVYQNLpfleeqqklirnanHHQVPLLGICLG 71
Cdd:cd01743   17 YLRELGAEVVV--VRNDEITLEElelLNPDAIVIspgpghpedAGISLEIIRAL--------------AGKVPILGVCLG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089297  72 SQLIAQALGGRVYK------GQRKEIgwfevKVNNEGrndIFKGITNErikvFQ------WHGDTYELPKSAILLASS-N 138
Cdd:cd01743   81 HQAIAEAFGGKVVRapepmhGKTSEI-----HHDGSG---LFKGLPQP----FTvgryhsLVVDPDPLPDLLEVTASTeD 148

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 262089297 139 LYPQAFKVGTS--IGILFHLE--VT---HEIIRNW 166
Cdd:cd01743  149 GVIMALRHRDLpiYGVQFHPEsiLTeygLRLLENF 183
PabA COG0512
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ...
 54-166 2.14e-08

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: 51.96  E-value: 2.14e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089297  54 LIRNAnHHQVPLLGICLGSQLIAQALGGRVYKGQR----KEigwFEVKVNNEGrndIFKGITNErikvFQ------WHGD 123
Cdd:COG0512   64 VIRAF-AGKIPILGVCLGHQAIGEAFGGKVVRAPEpmhgKT---SPITHDGSG---LFAGLPNP----FTatryhsLVVD 132

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 262089297 124 TYELPKSAILLASS----------NLYPQafkvgtsIGILFHLE--VT---HEIIRNW 166
Cdd:COG0512  133 RETLPDELEVTAWTedgeimgirhRELPI-------EGVQFHPEsiLTehgHQLLANF 183
CarA COG0505
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ...
 48-85 7.35e-08

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: 51.56  E-value: 7.35e-08
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 262089297  48 LEEQQKLIRNANHHQVPLLGICLGSQLIAQALGGRVYK 85
Cdd:COG0505  233 LDYAIETIRELLGKGIPIFGICLGHQLLALALGAKTYK 270
PRK12564 PRK12564
carbamoyl-phosphate synthase small subunit;
48-85 1.62e-07

carbamoyl-phosphate synthase small subunit;


Pssm-ID: 237139 [Multi-domain]  Cd Length: 360  Bit Score: 50.46  E-value: 1.62e-07
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 262089297  48 LEEQQKLIRNANHHQVPLLGICLGSQLIAQALGGRVYK 85
Cdd:PRK12564 234 LDYAIEMIRELLEKKIPIFGICLGHQLLALALGAKTYK 271
hisH PRK13143
imidazole glycerol phosphate synthase subunit HisH; Provisional
 2-113 3.21e-07

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237289 [Multi-domain]  Cd Length: 200  Bit Score: 48.71  E-value: 3.21e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089297   2 KKLFESVGFEietkhVKKDSIPQEVDNYAAIVI--LGGYMSVYQNL-PFLEEQQKLIRNAnhhqVPLLGICLGSQLI--- 75
Cdd:PRK13143  17 SKALERAGAE-----VVITSDPEEILDADGIVLpgVGAFGAAMENLsPLRDVILEAARSG----KPFLGICLGMQLLfes 87

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 262089297  76 ------AQALG---GRV--YKGQRK--EIGWFEVKVNNEgrNDIFKGITNE 113
Cdd:PRK13143  88 seegggVRGLGlfpGRVvrFPAGVKvpHMGWNTVKVVKD--CPLFEGIDGE 136
IMP_synth_hisH TIGR01855
imidazole glycerol phosphate synthase, glutamine amidotransferase subunit; This model ...
 2-166 3.95e-07

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: 48.48  E-value: 3.95e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089297    2 KKLFESVGFEIEtkhVKKDsiPQEVDNYAAIVI--LGGYMSVYQNLpfleEQQKLIRNANHH---QVPLLGICLGSQLIA 76
Cdd:TIGR01855  15 KRALKRVGAEPV---VVKD--SKEAELADKLILpgVGAFGAAMARL----RENGLDLFVELVvrlGKPVLGICLGMQLLF 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089297   77 Q---------ALG---GRVYKGQRK---EIGWFEVKVNNEgrNDIFKGItNERIKVFQWHgdTYELP-KSAILLASSNL- 139
Cdd:TIGR01855  86 ErseegggvpGLGlikGNVVKLEARkvpHMGWNEVHPVKE--SPLLNGI-DEGAYFYFVH--SYYAVcEEEAVLAYADYg 160

                         170       180       190
                  ....*....|....*....|....*....|...
gi 262089297  140 --YPQAFKVGTSIGILFHLEVTHE----IIRNW 166
Cdd:TIGR01855 161 ekFPAAVQKGNIFGTQFHPEKSGKtglkLLENF 193
PRK05670 PRK05670
anthranilate synthase component II; Provisional
 53-113 4.35e-07

anthranilate synthase component II; Provisional


Pssm-ID: 235552 [Multi-domain]  Cd Length: 189  Bit Score: 48.20  E-value: 4.35e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 262089297  53 KLIRNAnHHQVPLLGICLGSQLIAQALGGRVykGQRKEI--G-WFEVKVNNEGrndIFKGITNE 113
Cdd:PRK05670  64 ELIREF-AGKVPILGVCLGHQAIGEAFGGKV--VRAKEImhGkTSPIEHDGSG---IFAGLPNP 121
PRK07567 PRK07567
glutamine amidotransferase; Provisional
 63-157 1.09e-06

glutamine amidotransferase; Provisional


Pssm-ID: 181035 [Multi-domain]  Cd Length: 242  Bit Score: 47.63  E-value: 1.09e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089297  63 VPLLGICLGSQLIAQALGGRVYKGQRKEIGWFEVKVNNEGRNDIFKGITNERIKVFQWHGDTYE-LPKSAILLASSNLYP 141
Cdd:PRK07567  94 FPFLGACYGVGTLGHHQGGVVDRTYGEPVGAVTVSLTDAGRADPLLAGLPDTFTAFVGHKEAVSaLPPGAVLLATSPTCP 173

                         90
                 ....*....|....*...
gi 262089297 142 -QAFKVGTSI-GILFHLE 157
Cdd:PRK07567 174 vQMFRVGENVyATQFHPE 191
hisH PRK13181
imidazole glycerol phosphate synthase subunit HisH; Provisional
 2-114 1.79e-06

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 183878 [Multi-domain]  Cd Length: 199  Bit Score: 46.78  E-value: 1.79e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089297   2 KKLFESVGFEIEtkhVKKDsiPQEVDNYAAIVI--LGGYMSVYQNL------PFLEEQQKLirnanhhQVPLLGICLGSQ 73
Cdd:PRK13181  16 ANALKRLGVEAV---VSSD--PEEIAGADKVILpgVGAFGQAMRSLresgldEALKEHVEK-------KQPVLGICLGMQ 83

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 262089297  74 LIA--------QALG---GRVYK---GQRK--EIGWFEVKvnNEGRNDIFKGITNER 114
Cdd:PRK13181  84 LLFesseegnvKGLGlipGDVKRfrsEPLKvpQMGWNSVK--PLKESPLFKGIEEGS 138
GATase1_CPSase cd01744
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ...
 48-88 2.20e-06

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: 46.34  E-value: 2.20e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 262089297  48 LEEQQKLIRNANHHQVPLLGICLGSQLIAQALGGRVYK---GQR 88
Cdd:cd01744   55 LDEAIKTVRKLLGKKIPIFGICLGHQLLALALGAKTYKmkfGHR 98
Peptidase_C26 pfam07722
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ...
 54-84 7.84e-06

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: 44.94  E-value: 7.84e-06
                          10        20        30
                  ....*....|....*....|....*....|.
gi 262089297   54 LIRNANHHQVPLLGICLGSQLIAQALGGRVY 84
Cdd:pfam07722  97 LIRAALARGKPILGICRGFQLLNVALGGTLY 127
PRK14607 PRK14607
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;
63-195 1.59e-05

bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;


Pssm-ID: 237764 [Multi-domain]  Cd Length: 534  Bit Score: 45.09  E-value: 1.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089297  63 VPLLGICLGSQLIAQALGGRVYKGQRKEIGWFEvKVNNEGRnDIFKGITNErIKVFQWH---GDTYELPKSAILLASSN- 138
Cdd:PRK14607  74 VPILGVCLGHQAIGYAFGGKIVHAKRILHGKTS-PIDHNGK-GLFRGIPNP-TVATRYHslvVEEASLPECLEVTAKSDd 150

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 262089297 139 ---------LYPqafkvgtSIGILFHLEVT-----HEIIRNWTsNYRLEMTEVGVSTDSILnnkknEFENL 195
Cdd:PRK14607 151 geimgirhkEHP-------IFGVQFHPESIlteegKRILKNFL-NYQREEIDIKSYLKKLV-----EGEDL 208
GATase1_2 cd01745
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 54-84 2.86e-05

Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group contains a subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain. GATase activity catalyses the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. Glutamine amidotransferases (GATase) includes the triad family of amidotransferases which have a conserved Cys-His-Glu catalytic triad in the glutaminase active site. In this subgroup this triad is conserved. GATase activity can be found in a range of biosynthetic enzymes, including: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase , anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase, cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. Glutamine amidotransferase (GATase) domains can occur either as single polypeptides, as in glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase.


Pssm-ID: 153216 [Multi-domain]  Cd Length: 189  Bit Score: 42.95  E-value: 2.86e-05
                         10        20        30
                 ....*....|....*....|....*....|.
gi 262089297  54 LIRNANHHQVPLLGICLGSQLIAQALGGRVY 84
Cdd:cd01745   92 LLRAALERGKPILGICRGMQLLNVALGGTLY 122
PRK07649 PRK07649
aminodeoxychorismate/anthranilate synthase component II;
62-112 6.96e-05

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181066 [Multi-domain]  Cd Length: 195  Bit Score: 42.10  E-value: 6.96e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 262089297  62 QVPLLGICLGSQLIAQALGGRVYKGQRKEIGWFEvKVNNEGRNdIFKGITN 112
Cdd:PRK07649  72 KIPIFGVCLGHQSIAQVFGGEVVRAERLMHGKTS-LMHHDGKT-IFSDIPN 120
PRK12838 PRK12838
carbamoyl phosphate synthase small subunit; Reviewed
 46-85 9.77e-05

carbamoyl phosphate synthase small subunit; Reviewed


Pssm-ID: 183784 [Multi-domain]  Cd Length: 354  Bit Score: 42.19  E-value: 9.77e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 262089297  46 PFLEEQQKLIrnanhHQVPLLGICLGSQLIAQALGGRVYK 85
Cdd:PRK12838 226 PYLPEIKKLI-----SSYPILGICLGHQLIALALGADTEK 260
PLN02771 PLN02771
carbamoyl-phosphate synthase (glutamine-hydrolyzing)
 62-85 1.68e-04

carbamoyl-phosphate synthase (glutamine-hydrolyzing)


Pssm-ID: 178370 [Multi-domain]  Cd Length: 415  Bit Score: 41.89  E-value: 1.68e-04
                         10        20
                 ....*....|....*....|....
gi 262089297  62 QVPLLGICLGSQLIAQALGGRVYK 85
Cdd:PLN02771 310 KVPVFGICMGHQLLGQALGGKTFK 333
hisH PRK13141
imidazole glycerol phosphate synthase subunit HisH; Provisional
 2-113 2.25e-04

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237288 [Multi-domain]  Cd Length: 205  Bit Score: 40.50  E-value: 2.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089297   2 KKLFESVGFEIEtkhVKKDsiPQEVDNYAAIvIL---GGYMSVYQNLpfleEQQKL---IRNANHHQVPLLGICLGSQLI 75
Cdd:PRK13141  16 EKALERLGAEAV---ITSD--PEEILAADGV-ILpgvGAFPDAMANL----RERGLdevIKEAVASGKPLLGICLGMQLL 85

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 262089297  76 ---------AQALG---GRVYKGQRKE------IGWFEVKVNNEgrNDIFKGITNE 113
Cdd:PRK13141  86 fesseefgeTEGLGllpGRVRRFPPEEglkvphMGWNQLELKKE--SPLLKGIPDG 139
PuuD COG2071
Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (putrescine degradation), contains ...
 54-84 2.36e-04

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: 40.92  E-value: 2.36e-04
                         10        20        30
                 ....*....|....*....|....*....|.
gi 262089297  54 LIRNANHHQVPLLGICLGSQLIAQALGGRVY 84
Cdd:COG2071   88 LIRAALERGKPVLGICRGMQLLNVALGGTLY 118
PRK05665 PRK05665
amidotransferase; Provisional
 65-143 2.68e-04

amidotransferase; Provisional


Pssm-ID: 168162 [Multi-domain]  Cd Length: 240  Bit Score: 40.56  E-value: 2.68e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089297  65 LLGICLGSQLIAQALGGRVykgQRKEIGWfEVKVNNEGRNDIFKGITNER--IKVFQWHGD-TYELPKSAILLASSNLYP 141
Cdd:PRK05665  94 LLGVCFGHQLLALLLGGKA---ERASQGW-GVGIHRYQLAAHAPWMSPAVteLTLLISHQDqVTALPEGATVIASSDFCP 169


                 ..
gi 262089297 142 QA 143
Cdd:PRK05665 170 FA 171
PRK13527 PRK13527
glutamine amidotransferase subunit PdxT; Provisional
 1-163 2.70e-04

glutamine amidotransferase subunit PdxT; Provisional


Pssm-ID: 237412 [Multi-domain]  Cd Length: 200  Bit Score: 40.26  E-value: 2.70e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089297   1 MKKLFESVGFEIETKHVKKdsiPQEVDNYAAIVILGG----YMSVYQNLPFLEEqqklIRNANHHQVPLLGICLGSQLIA 76
Cdd:PRK13527  19 LKRALDELGIDGEVVEVRR---PGDLPDCDALIIPGGesttIGRLMKREGILDE----IKEKIEEGLPILGTCAGLILLA 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089297  77 QALGG-RVYKGQRKEIGWFEVKVNnegRN-----------DI-FKGITNERIKVFQWHGDTYELPKSAILLASSNLYPQA 143
Cdd:PRK13527  92 KEVGDdRVTKTEQPLLGLMDVTVK---RNafgrqrdsfeaEIdLSGLDGPFHAVFIRAPAITKVGGDVEVLAKLDDRIVA 168

                        170       180
                 ....*....|....*....|
gi 262089297 144 FKVGTSIGILFHLEVTHEII 163
Cdd:PRK13527 169 VEQGNVLATAFHPELTDDTR 188
PRK08857 PRK08857
aminodeoxychorismate/anthranilate synthase component II;
62-121 1.02e-03

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181566 [Multi-domain]  Cd Length: 193  Bit Score: 38.70  E-value: 1.02e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089297  62 QVPLLGICLGSQLIAQALGGRVYKGqRKEIGWFEVKVNNEGRNdIFKGITNErIKVFQWH 121
Cdd:PRK08857  72 KLPILGVCLGHQAIAQVFGGQVVRA-RQVMHGKTSPIRHTGRS-VFKGLNNP-LTVTRYH 128
GATase1_AraC_ArgR_like cd03136
AraC transcriptional regulators having an N-terminal Type 1 glutamine amidotransferase ...
 7-82 1.24e-03

AraC transcriptional regulators having an N-terminal Type 1 glutamine amidotransferase (GATase1)-like domain; A subgroup of AraC transcriptional regulators having an N-terminal Type 1 glutamine amidotransferase (GATase1)-like domain. This group contains proteins similar to the Pseudomonas aeruginosa ArgR regulator. ArgR functions in the control of expression of certain genes of arginine biosynthesis and catabolism. AraC regulators are defined by a AraC-type helix-turn-helix DNA binding domain at their C-terminal. AraC family transcriptional regulators are widespread among bacteria and are involved in regulating diverse and important biological functions, including carbon metabolism, stress responses and virulence in different microorganisms. The catalytic triad typical of GATase1 domains is not conserved in this GATase1-like domain. However, in common with typical GATase1domains a reactive cys residue is found in some sequences in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow.


Pssm-ID: 153230 [Multi-domain]  Cd Length: 185  Bit Score: 38.34  E-value: 1.24e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 262089297   7 SVGFEIETkhvkkDSIPQEVDNYAAIVILGGYMSVYQNLPFLEEQqklIRNANHHQVPLLGICLGSQLIAQA--LGGR 82
Cdd:cd03136   48 SNGLRVAP-----DAALEDAPPLDYLFVVGGLGARRAVTPALLAW---LRRAARRGVALGGIDTGAFLLARAglLDGR 117
PRK07765 PRK07765
aminodeoxychorismate/anthranilate synthase component II;
54-83 3.25e-03

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181107 [Multi-domain]  Cd Length: 214  Bit Score: 37.34  E-value: 3.25e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 262089297  54 LIRNANHHQVPLLGICLGSQLIAQALGGRV 83
Cdd:PRK07765  68 MVRACAAAGTPLLGVCLGHQAIGVAFGATV 97
GATase1_IGP_Synthase cd01748
Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate ...
 2-113 3.51e-03

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: 37.09  E-value: 3.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089297   2 KKLFESVGFEietkhVKKDSIPQEVDNYAAIVI--LGGYMSVYQNLpfleEQQKL---IRNANHHQVPLLGICLGSQLIA 76
Cdd:cd01748   15 ANALERLGAE-----VIITSDPEEILSADKLILpgVGAFGDAMANL----RERGLieaLKEAIASGKPFLGICLGMQLLF 85

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 262089297  77 ---------QALG---GRVYKGQRKE------IGWFEVKVNNEgrNDIFKGITNE 113
Cdd:cd01748   86 esseegggtKGLGlipGKVVRFPASEglkvphMGWNQLEITKE--SPLFKGIPDG 138
trpG CHL00101
anthranilate synthase component 2
 62-85 5.75e-03

anthranilate synthase component 2


Pssm-ID: 214365 [Multi-domain]  Cd Length: 190  Bit Score: 36.25  E-value: 5.75e-03
                         10        20
                 ....*....|....*....|....
gi 262089297  62 QVPLLGICLGSQLIAQALGGRVYK 85
Cdd:CHL00101  72 YIPILGVCLGHQSIGYLFGGKIIK 95
HisH COG0118
Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH [Amino acid ...
 53-113 6.82e-03

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: 36.17  E-value: 6.82e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 262089297  53 KLIRNANHHQVPLLGICLGSQLIA---------QALG---GRVYK---GQRK--EIGWFEVKVNNEGRndIFKGITNE 113
Cdd:COG0118   64 EAIREAVAGGKPVLGICLGMQLLFerseengdtEGLGlipGEVVRfpaSDLKvpHMGWNTVEIAKDHP--LFAGIPDG 139
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH