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Conserved domains on  [gi|504406380|ref|WP_014593482|]
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MULTISPECIES: glutamine amidotransferase [Pantoea]

Protein Classification

type 1 glutamine amidotransferase family protein( domain architecture ID 73)

type 1 glutamine amidotransferase (GATase1) family protein

CATH:  3.40.50.880
PubMed:  10387030
SCOP:  3001405

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GAT_1 super family cl00020
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 6-226 4.35e-92

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.


The actual alignment was detected with superfamily member PRK09065:

Pssm-ID: 469582 [Multi-domain]  Cd Length: 237  Bit Score: 270.68  E-value: 4.35e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504406380   6 ALPLALIQLDVPPANVVEKIGEQPVWFIDALNLQPDDYVIVRPHLGETLPQFTDISGAVLSGSWAMVTDHADWSERTAAW 85
Cdd:PRK09065   1 VKPLLIIQTGTPPPSIRARYGDFPHWIRVALGLAEQPVVVVRVFAGEPLPAPDDFAGVIITGSWAMVTDRLDWSERTADW 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504406380  86 IRAAMEARLPLLGVCYGHQLMAYALGGKVGDNPNGWERGLMTLTTTSQARHDPLLATLPETFEAWLSHRQSVMTPPAHAT 165
Cdd:PRK09065  81 LRQAAAAGMPLLGICYGHQLLAHALGGEVGYNPAGRESGTVTVELHPAAADDPLFAGLPAQFPAHLTHLQSVLRLPPGAV 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504406380 166 VLAVSDMDGCQVLRYSACALSVQFHPEFDRRIMDACLPENEENDGTELQGAD----------WARSLLYHF 226
Cdd:PRK09065 161 VLARSAQDPHQAFRYGPHAWGVQFHPEFTAHIMRAYLRARADCLRREGLDARtllrevseapWARKLLRRF 231
 
Name Accession Description Interval E-value
PRK09065 PRK09065
glutamine amidotransferase; Provisional
 6-226 4.35e-92

glutamine amidotransferase; Provisional


Pssm-ID: 181635 [Multi-domain]  Cd Length: 237  Bit Score: 270.68  E-value: 4.35e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504406380   6 ALPLALIQLDVPPANVVEKIGEQPVWFIDALNLQPDDYVIVRPHLGETLPQFTDISGAVLSGSWAMVTDHADWSERTAAW 85
Cdd:PRK09065   1 VKPLLIIQTGTPPPSIRARYGDFPHWIRVALGLAEQPVVVVRVFAGEPLPAPDDFAGVIITGSWAMVTDRLDWSERTADW 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504406380  86 IRAAMEARLPLLGVCYGHQLMAYALGGKVGDNPNGWERGLMTLTTTSQARHDPLLATLPETFEAWLSHRQSVMTPPAHAT 165
Cdd:PRK09065  81 LRQAAAAGMPLLGICYGHQLLAHALGGEVGYNPAGRESGTVTVELHPAAADDPLFAGLPAQFPAHLTHLQSVLRLPPGAV 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504406380 166 VLAVSDMDGCQVLRYSACALSVQFHPEFDRRIMDACLPENEENDGTELQGAD----------WARSLLYHF 226
Cdd:PRK09065 161 VLARSAQDPHQAFRYGPHAWGVQFHPEFTAHIMRAYLRARADCLRREGLDARtllrevseapWARKLLRRF 231
GuaA1 COG0518
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ...
 26-220 3.80e-62

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: 194.01  E-value: 3.80e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504406380  26 GEQPVWFIDALNLQPDDYVIVRPHLGETLPQFTDI---SGAVLSGSWAMVTDHADWSERTAAWIRAAMEARLPLLGVCYG 102
Cdd:COG0518   12 GQYPGLIARRLREAGIELDVLRVYAGEILPYDPDLedpDGLILSGGPMSVYDEDPWLEDEPALIREAFELGKPVLGICYG 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504406380 103 HQLMAYALGGKVGDNPnGWERGLMTLTTTSqarHDPLLATLPETFEAWLSHRQSVMTPPAHATVLAVSDMDGCQVLRYSA 182
Cdd:COG0518   92 AQLLAHALGGKVEPGP-GREIGWAPVELTE---ADPLFAGLPDEFTVWMSHGDTVTELPEGAEVLASSDNCPNQAFRYGR 167

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 504406380 183 CALSVQFHPEFDRRIMDACLPENEENDGTELQGADWAR 220
Cdd:COG0518  168 RVYGVQFHPEVTHTMMEAWLEERADELAAEELLAEASL 205
GATase1_1 cd01741
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 8-192 1.10e-53

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: 171.27  E-value: 1.10e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504406380   8 PLALIQLDVPpanvvEKIGEQPVWfIDALNLQPDDYVIVRPHLGETLPQFTDISGAVLSGSWAMV-TDHADWSERTAAWI 86
Cdd:cd01741    1 RILILQHDTP-----EGPGLFEDL-LREAGAETIEIDVVDVYAGELLPDLDDYDGLVILGGPMSVdEDDYPWLKKLKELI 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504406380  87 RAAMEARLPLLGVCYGHQLMAYALGGKVGDNPNGWERGLMTLTTTSQARHDPLLATLPETFEAWLSHRQSVMTPPAHATV 166
Cdd:cd01741   75 RQALAAGKPVLGICLGHQLLARALGGKVGRNPKGWEIGWFPVTLTEAGKADPLFAGLPDEFPVFHWHGDTVVELPPGAVL 154

                        170       180
                 ....*....|....*....|....*.
gi 504406380 167 LAVSDMDGCQVLRYSACALSVQFHPE 192
Cdd:cd01741  155 LASSEACPNQAFRYGDRALGLQFHPE 180
guaA_Nterm TIGR00888
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine ...
 61-192 9.59e-21

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: 86.21  E-value: 9.59e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504406380   61 SGAVLSGSWAMVtdhadWSERTAAWIRAAMEARLPLLGVCYGHQLMAYALGGKVGDNPNGwERGLMTLTTTSQarhDPLL 140
Cdd:TIGR00888  43 KGIILSGGPSSV-----YAENAPRADEKIFELGVPVLGICYGMQLMAKQLGGEVGRAEKR-EYGKAELEILDE---DDLF 113

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 504406380  141 ATLPETFEAWLSHRQSVMTPPAHATVLAVSdmDGCQVlrysaCALS--------VQFHPE 192
Cdd:TIGR00888 114 RGLPDESTVWMSHGDKVKELPEGFKVLATS--DNCPV-----AAMAheekpiygVQFHPE 166
GATase pfam00117
Glutamine amidotransferase class-I;
86-206 6.71e-20

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 83.83  E-value: 6.71e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504406380   86 IRAAMEARLPLLGVCYGHQLMAYALGGKVGDNPNGWERGlmtltTTSQARHDP--LLATLPETFEAWLSHRQSVM--TPP 161
Cdd:pfam00117  63 IREARELKIPILGICLGHQLLALAFGGKVVKAKKFGHHG-----KNSPVGDDGcgLFYGLPNVFIVRRYHSYAVDpdTLP 137

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 504406380  162 AHATVLAVSDmDGCQVlrysaCAL--------SVQFHPEFDRRIMDACLPENE 206
Cdd:pfam00117 138 DGLEVTATSE-NDGTI-----MGIrhkklpifGVQFHPESILTPHGPEILFNF 184
 
Name Accession Description Interval E-value
PRK09065 PRK09065
glutamine amidotransferase; Provisional
 6-226 4.35e-92

glutamine amidotransferase; Provisional


Pssm-ID: 181635 [Multi-domain]  Cd Length: 237  Bit Score: 270.68  E-value: 4.35e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504406380   6 ALPLALIQLDVPPANVVEKIGEQPVWFIDALNLQPDDYVIVRPHLGETLPQFTDISGAVLSGSWAMVTDHADWSERTAAW 85
Cdd:PRK09065   1 VKPLLIIQTGTPPPSIRARYGDFPHWIRVALGLAEQPVVVVRVFAGEPLPAPDDFAGVIITGSWAMVTDRLDWSERTADW 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504406380  86 IRAAMEARLPLLGVCYGHQLMAYALGGKVGDNPNGWERGLMTLTTTSQARHDPLLATLPETFEAWLSHRQSVMTPPAHAT 165
Cdd:PRK09065  81 LRQAAAAGMPLLGICYGHQLLAHALGGEVGYNPAGRESGTVTVELHPAAADDPLFAGLPAQFPAHLTHLQSVLRLPPGAV 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504406380 166 VLAVSDMDGCQVLRYSACALSVQFHPEFDRRIMDACLPENEENDGTELQGAD----------WARSLLYHF 226
Cdd:PRK09065 161 VLARSAQDPHQAFRYGPHAWGVQFHPEFTAHIMRAYLRARADCLRREGLDARtllrevseapWARKLLRRF 231
GuaA1 COG0518
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ...
 26-220 3.80e-62

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: 194.01  E-value: 3.80e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504406380  26 GEQPVWFIDALNLQPDDYVIVRPHLGETLPQFTDI---SGAVLSGSWAMVTDHADWSERTAAWIRAAMEARLPLLGVCYG 102
Cdd:COG0518   12 GQYPGLIARRLREAGIELDVLRVYAGEILPYDPDLedpDGLILSGGPMSVYDEDPWLEDEPALIREAFELGKPVLGICYG 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504406380 103 HQLMAYALGGKVGDNPnGWERGLMTLTTTSqarHDPLLATLPETFEAWLSHRQSVMTPPAHATVLAVSDMDGCQVLRYSA 182
Cdd:COG0518   92 AQLLAHALGGKVEPGP-GREIGWAPVELTE---ADPLFAGLPDEFTVWMSHGDTVTELPEGAEVLASSDNCPNQAFRYGR 167

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 504406380 183 CALSVQFHPEFDRRIMDACLPENEENDGTELQGADWAR 220
Cdd:COG0518  168 RVYGVQFHPEVTHTMMEAWLEERADELAAEELLAEASL 205
GATase1_1 cd01741
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 8-192 1.10e-53

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: 171.27  E-value: 1.10e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504406380   8 PLALIQLDVPpanvvEKIGEQPVWfIDALNLQPDDYVIVRPHLGETLPQFTDISGAVLSGSWAMV-TDHADWSERTAAWI 86
Cdd:cd01741    1 RILILQHDTP-----EGPGLFEDL-LREAGAETIEIDVVDVYAGELLPDLDDYDGLVILGGPMSVdEDDYPWLKKLKELI 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504406380  87 RAAMEARLPLLGVCYGHQLMAYALGGKVGDNPNGWERGLMTLTTTSQARHDPLLATLPETFEAWLSHRQSVMTPPAHATV 166
Cdd:cd01741   75 RQALAAGKPVLGICLGHQLLARALGGKVGRNPKGWEIGWFPVTLTEAGKADPLFAGLPDEFPVFHWHGDTVVELPPGAVL 154

                        170       180
                 ....*....|....*....|....*.
gi 504406380 167 LAVSDMDGCQVLRYSACALSVQFHPE 192
Cdd:cd01741  155 LASSEACPNQAFRYGDRALGLQFHPE 180
PRK07567 PRK07567
glutamine amidotransferase; Provisional
 32-194 3.61e-25

glutamine amidotransferase; Provisional


Pssm-ID: 181035 [Multi-domain]  Cd Length: 242  Bit Score: 99.25  E-value: 3.61e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504406380  32 FIDALNLQPDDYVIVRPHLGET-LPQFTDISGAVLSGSWAMVTDHAD----WSERTAAWIRAAME----ARLPLLGVCYG 102
Cdd:PRK07567  23 FLRYTGLDPAELRRIRLDREPLpDLDLDDYSGVIVGGSPFNVSDPAEskspWQRRVEAELSGLLDevvaRDFPFLGACYG 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504406380 103 HQLMAYALGGKVgDNPNGWERGLMTLTTTSQARHDPLLATLPETFEAWLSHRQSVMTPPAHATVLAVSdmDGC--QVLRY 180
Cdd:PRK07567 103 VGTLGHHQGGVV-DRTYGEPVGAVTVSLTDAGRADPLLAGLPDTFTAFVGHKEAVSALPPGAVLLATS--PTCpvQMFRV 179

                        170
                 ....*....|....
gi 504406380 181 SACALSVQFHPEFD 194
Cdd:PRK07567 180 GENVYATQFHPELD 193
GATase1_GMP_Synthase cd01742
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine ...
 59-192 9.38e-24

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: 93.75  E-value: 9.38e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504406380  59 DISGAVLSGSWAMVtdHADWSERTAAWIraaMEARLPLLGVCYGHQLMAYALGGKVGDNPNGwERGLMTLTTTSqarHDP 138
Cdd:cd01742   41 NPKGIILSGGPSSV--YEEDAPRVDPEI---FELGVPVLGICYGMQLIAKALGGKVERGDKR-EYGKAEIEIDD---SSP 111

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504406380 139 LLATLPETFEAWLSHRQSVMTPPAHATVLAVSdmDGCQVlrysaCALS--------VQFHPE 192
Cdd:cd01742  112 LFEGLPDEQTVWMSHGDEVVKLPEGFKVIASS--DNCPV-----AAIAneekkiygVQFHPE 166
guaA_Nterm TIGR00888
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine ...
 61-192 9.59e-21

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: 86.21  E-value: 9.59e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504406380   61 SGAVLSGSWAMVtdhadWSERTAAWIRAAMEARLPLLGVCYGHQLMAYALGGKVGDNPNGwERGLMTLTTTSQarhDPLL 140
Cdd:TIGR00888  43 KGIILSGGPSSV-----YAENAPRADEKIFELGVPVLGICYGMQLMAKQLGGEVGRAEKR-EYGKAELEILDE---DDLF 113

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 504406380  141 ATLPETFEAWLSHRQSVMTPPAHATVLAVSdmDGCQVlrysaCALS--------VQFHPE 192
Cdd:TIGR00888 114 RGLPDESTVWMSHGDKVKELPEGFKVLATS--DNCPV-----AAMAheekpiygVQFHPE 166
guaA PRK00074
GMP synthase; Reviewed
 61-192 1.11e-20

GMP synthase; Reviewed


Pssm-ID: 234614 [Multi-domain]  Cd Length: 511  Bit Score: 90.11  E-value: 1.11e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504406380  61 SGAVLSGSWAMVTDhaDWSERTAAWIraaMEARLPLLGVCYGHQLMAYALGGKVGDNPNGwERGLMTLTTTSqarHDPLL 140
Cdd:PRK00074  48 KGIILSGGPASVYE--EGAPRADPEI---FELGVPVLGICYGMQLMAHQLGGKVERAGKR-EYGRAELEVDN---DSPLF 118

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 504406380 141 ATLPETFEAWLSHRQSVMTPPAHATVLAVSdmDGCQVlrysaCALS--------VQFHPE 192
Cdd:PRK00074 119 KGLPEEQDVWMSHGDKVTELPEGFKVIAST--ENCPI-----AAIAneerkfygVQFHPE 171
GATase pfam00117
Glutamine amidotransferase class-I;
86-206 6.71e-20

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 83.83  E-value: 6.71e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504406380   86 IRAAMEARLPLLGVCYGHQLMAYALGGKVGDNPNGWERGlmtltTTSQARHDP--LLATLPETFEAWLSHRQSVM--TPP 161
Cdd:pfam00117  63 IREARELKIPILGICLGHQLLALAFGGKVVKAKKFGHHG-----KNSPVGDDGcgLFYGLPNVFIVRRYHSYAVDpdTLP 137

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 504406380  162 AHATVLAVSDmDGCQVlrysaCAL--------SVQFHPEFDRRIMDACLPENE 206
Cdd:pfam00117 138 DGLEVTATSE-NDGTI-----MGIrhkklpifGVQFHPESILTPHGPEILFNF 184
PRK06490 PRK06490
glutamine amidotransferase; Provisional
 45-198 9.42e-18

glutamine amidotransferase; Provisional


Pssm-ID: 180590 [Multi-domain]  Cd Length: 239  Bit Score: 79.23  E-value: 9.42e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504406380  45 IVRPHLGETLPQ-FTDISGAVLSGSWAMVTDHADWSERTAAWIRAAMEARLPLLGVCYGHQLMAYALGGKVGDNPNGW-E 122
Cdd:PRK06490  37 IRRPRLGDPLPDtLEDHAGAVIFGGPMSANDPDDFIRREIDWISVPLKENKPFLGICLGAQMLARHLGARVAPHPDGRvE 116

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504406380 123 RGLMTLTTTSQARHdplLATLPETFEAWlsHRQSvMTPPAHATVLAVSDMDGCQVLRYSACALSVQFHPEFDRRIM 198
Cdd:PRK06490 117 IGYYPLRPTEAGRA---LMHWPEMVYHW--HREG-FDLPAGAELLATGDDFPNQAFRYGDNAWGLQFHPEVTRAMM 186
PRK00758 PRK00758
GMP synthase subunit A; Validated
 91-192 1.12e-16

GMP synthase subunit A; Validated


Pssm-ID: 179112 [Multi-domain]  Cd Length: 184  Bit Score: 75.27  E-value: 1.12e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504406380  91 EARLPLLGVCYGHQLMAYALGGKVGDNPNGwERGLMTLTTTSqarHDPLLATLPETFEAWLSHRQSVMTPPAHATVLAVS 170
Cdd:PRK00758  65 ELDVPILGICLGHQLIAKAFGGEVGRGEYG-EYALVEVEILD---EDDILKGLPPEIRVWASHADEVKELPDGFEILARS 140

                         90       100
                 ....*....|....*....|...
gi 504406380 171 DMDGCQVLRYSACAL-SVQFHPE 192
Cdd:PRK00758 141 DICEVEAMKHKEKPIyGVQFHPE 163
PRK05665 PRK05665
amidotransferase; Provisional
 51-193 1.44e-13

amidotransferase; Provisional


Pssm-ID: 168162 [Multi-domain]  Cd Length: 240  Bit Score: 67.91  E-value: 1.44e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504406380  51 GETLPQFTDISGAVLSGSWAMVTDHADWSERTAAWIRAAMEARLPLLGVCYGHQLMAYALGGKVGDNPNGWERGLMTLTT 130
Cdd:PRK05665  49 GDYPADDEKFDAYLVTGSKADSFGTDPWIQTLKTYLLKLYERGDKLLGVCFGHQLLALLLGGKAERASQGWGVGIHRYQL 128

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504406380 131 TSQAR-HDPLLATLpetfEAWLSHRQSVMTPPAHATVLAVSDMdgCQVLRYSA--CALSVQFHPEF 193
Cdd:PRK05665 129 AAHAPwMSPAVTEL----TLLISHQDQVTALPEGATVIASSDF--CPFAAYHIgdQVLCFQGHPEF 188
GATase1_Anthranilate_Synthase cd01743
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ...
 85-192 9.58e-13

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: 64.48  E-value: 9.58e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504406380  85 WIRAAMEARLPLLGVCYGHQLMAYALGGKVG--DNPNGwerGlmtltTTSQARHDP--LLATLPETFEAWLSHRQSV--M 158
Cdd:cd01743   63 EIIRALAGKVPILGVCLGHQAIAEAFGGKVVraPEPMH---G-----KTSEIHHDGsgLFKGLPQPFTVGRYHSLVVdpD 134

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 504406380 159 TPPAHATVLAVSD----MdGCQVLRYSACalSVQFHPE 192
Cdd:cd01743  135 PLPDLLEVTASTEdgviM-ALRHRDLPIY--GVQFHPE 169
PabA COG0512
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ...
 88-192 8.92e-12

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: 61.98  E-value: 8.92e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504406380  88 AAMEARLPLLGVCYGHQLMAYALGGKVGDNPN---GwerglmtltTTSQARHD--PLLATLPETFEAWLSH-----RQSV 157
Cdd:COG0512   66 RAFAGKIPILGVCLGHQAIGEAFGGKVVRAPEpmhG---------KTSPITHDgsGLFAGLPNPFTATRYHslvvdRETL 136

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 504406380 158 mtpPAHATVLAVSDmDGcQV--LR---YSACAlsVQFHPE 192
Cdd:COG0512  137 ---PDELEVTAWTE-DG-EImgIRhreLPIEG--VQFHPE 169
PRK08250 PRK08250
glutamine amidotransferase; Provisional
 47-194 4.59e-11

glutamine amidotransferase; Provisional


Pssm-ID: 181323 [Multi-domain]  Cd Length: 235  Bit Score: 60.75  E-value: 4.59e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504406380  47 RPHLGETLPQftDISG----AVLSGSWAMVTDHADW----SERTAAWIRAAMEARLPLLGVCYGHQLMAYALGGKVGDNP 118
Cdd:PRK08250  32 RVYAGEALPE--NADGfdllIVMGGPQSPRTTREECpyfdSKAEQRLINQAIKAGKAVIGVCLGAQLIGEALGAKYEHSP 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504406380 119 NGwERGLMTLTTTSQARHDPLLATLPETFEawLSHRQSVM---TPpaHATVLAVSdmDGC--QVLRYSACALSVQFHPEF 193
Cdd:PRK08250 110 EK-EIGYFPITLTEAGLKDPLLSHFGSTLT--VGHWHNDMpglTD--QAKVLATS--EGCprQIVQYSNLVYGFQCHMEF 182


                 .
gi 504406380 194 D 194
Cdd:PRK08250 183 T 183
PuuD COG2071
Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (putrescine degradation), contains ...
 80-200 9.90e-11

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: 59.80  E-value: 9.90e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504406380  80 ERTA---AWIRAAMEARLPLLGVCYGHQLMAYALGGK-VGDNPNGWERGL--MTLTTTSQARHD----P--LLATL--PE 145
Cdd:COG2071   80 ERDAfelALIRAALERGKPVLGICRGMQLLNVALGGTlYQDLPDQVPGALdhRQPAPRYAPRHTveiePgsRLARIlgEE 159

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504406380 146 TFEAWLSHRQSVMTPPAHATVLAVSDmDGCqV----LRYSACALSVQFHPEF-------DRRIMDA 200
Cdd:COG2071  160 EIRVNSLHHQAVKRLGPGLRVSARAP-DGV-IeaieSPGAPFVLGVQWHPEWlaasdplSRRLFEA 223
Peptidase_C26 pfam07722
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ...
 77-192 3.07e-10

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: 58.04  E-value: 3.07e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504406380   77 DWSERtaAWIRAAMEARLPLLGVCYGHQLMAYALGG----KVGDNPNGWERGLMTLTTTSQARH------DPLLATLPET 146
Cdd:pfam07722  91 DAYEL--ALIRAALARGKPILGICRGFQLLNVALGGtlyqDIQEQPGFTDHREHCQVAPYAPSHavnvepGSLLASLLGS 168

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 504406380  147 FEAWLS--HRQSVMTPP------AHA---TVLAVSdmdgcqVLRYSACALSVQFHPE 192
Cdd:pfam07722 169 EEFRVNslHHQAIDRLApglrveAVApdgTIEAIE------SPNAKGFALGVQWHPE 219
PRK05670 PRK05670
anthranilate synthase component II; Provisional
 93-192 3.75e-10

anthranilate synthase component II; Provisional


Pssm-ID: 235552 [Multi-domain]  Cd Length: 189  Bit Score: 57.45  E-value: 3.75e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504406380  93 RLPLLGVCYGHQLMAYALGGKVGDNPN---GwerglmtltTTSQARHD--PLLATLPETFEAWLSHRQSV--MTPPAHAT 165
Cdd:PRK05670  72 KVPILGVCLGHQAIGEAFGGKVVRAKEimhG---------KTSPIEHDgsGIFAGLPNPFTVTRYHSLVVdrESLPDCLE 142

                         90       100       110
                 ....*....|....*....|....*....|.
gi 504406380 166 VLAVSD----MdGCQVLRYSACAlsVQFHPE 192
Cdd:PRK05670 143 VTAWTDdgeiM-GVRHKELPIYG--VQFHPE 170
PRK07765 PRK07765
aminodeoxychorismate/anthranilate synthase component II;
86-192 8.40e-10

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181107 [Multi-domain]  Cd Length: 214  Bit Score: 56.98  E-value: 8.40e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504406380  86 IRAAMEARLPLLGVCYGHQLMAYALGGKVGDNPNgwerglMTLTTTSQARHDP--LLATLPETFEAWLSHRQSVM--TPP 161
Cdd:PRK07765  69 VRACAAAGTPLLGVCLGHQAIGVAFGATVDRAPE------LLHGKTSSVHHTGvgVLAGLPDPFTATRYHSLTILpeTLP 142

                         90       100       110
                 ....*....|....*....|....*....|..
gi 504406380 162 AHATVLAVSDMDGCQVLRYSACAL-SVQFHPE 192
Cdd:PRK07765 143 AELEVTARTDSGVIMAVRHRELPIhGVQFHPE 174
PRK07053 PRK07053
glutamine amidotransferase; Provisional
 72-196 8.69e-10

glutamine amidotransferase; Provisional


Pssm-ID: 235919 [Multi-domain]  Cd Length: 234  Bit Score: 56.88  E-value: 8.69e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504406380  72 VTDHAD--WSERTAAWIRAAMEARLPLLGVCYGHQLMAYALGGKVgdNPNGW-ERGLMTLTTTSQARHDPLlatlpetfe 148
Cdd:PRK07053  60 VYDDELypFLAPEIALLRQRLAAGLPTLGICLGAQLIARALGARV--YPGGQkEIGWAPLTLTDAGRASPL--------- 128

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 504406380 149 AWLSHRQSVM-------TPPAHATVLAVSDMDGCQVLRYSACALSVQFHPEFDRR 196
Cdd:PRK07053 129 RHLGAGTPVLhwhgdtfDLPEGATLLASTPACRHQAFAWGNHVLALQFHPEARED 183
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 32-112 1.37e-09

Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase (GATase1)-like domain. This group includes proteins similar to Class I glutamine amidotransferases, the intracellular PH1704 from Pyrococcus horikoshii, the C-terminal of the large catalase: Escherichia coli HP-II, Sinorhizobium meliloti Rm1021 ThuA. and, the A4 beta-galactosidase middle domain. The majority of proteins in this group have a reactive Cys found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For Class I glutamine amidotransferases proteins which transfer ammonia from the amide side chain of glutamine to an acceptor substrate, this Cys forms a Cys-His-Glu catalytic triad in the active site. Glutamine amidotransferases activity can be found in a range of biosynthetic enzymes included in this cd: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase, anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase, cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. For Pyrococcus horikoshii PH1704, the Cys of the nucleophile elbow together with a different His and, a Glu from an adjacent monomer form a catalytic triad different from the typical GATase1 triad. The E. coli HP-II C-terminal domain, S. meliloti Rm1021 ThuA and the A4 beta-galactosidase middle domain lack the catalytic triad typical GATaseI domains. GATase1-like domains can occur either as single polypeptides, as in Class I glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase.


Pssm-ID: 153210 [Multi-domain]  Cd Length: 115  Bit Score: 54.14  E-value: 1.37e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504406380  32 FIDALNLQPDDYVIVRPHLGE--TLPQFTDISGAVLSGSWaMVTDHADWSERTAAWIRAAMEARLPLLGVCYGHQLMAYA 109
Cdd:cd01653   17 PLDALREAGAEVDVVSPDGGPveSDVDLDDYDGLILPGGP-GTPDDLARDEALLALLREAAAAGKPILGICLGAQLLVLG 95


                 ...
gi 504406380 110 LGG 112
Cdd:cd01653   96 VQF 98
GATase1_2 cd01745
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 77-200 8.07e-09

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: 53.73  E-value: 8.07e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504406380  77 DWSERtaAWIRAAMEARLPLLGVCYGHQLMAYALGGkvgdnpngwerglmTL----TTTSqaRHDPLLATLPETFEawls 152
Cdd:cd01745   86 DAFEL--ALLRAALERGKPILGICRGMQLLNVALGG--------------TLyqdiRVNS--LHHQAIKRLADGLR---- 143

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 504406380 153 hrqsvmtPPAHA---TVLAVSDMDgcqvlrySACALSVQFHPEF-------DRRIMDA 200
Cdd:cd01745  144 -------VEARApdgVIEAIESPD-------RPFVLGVQWHPEWladtdpdSLKLFEA 187
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 32-106 3.01e-08

Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase (GATase1)-like domain. This group contains proteins similar to Class I glutamine amidotransferases, the intracellular PH1704 from Pyrococcus horikoshii, the C-terminal of the large catalase: Escherichia coli HP-II, Sinorhizobium meliloti Rm1021 ThuA, the A4 beta-galactosidase middle domain and peptidase E. The majority of proteins in this group have a reactive Cys found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For Class I glutamine amidotransferases proteins which transfer ammonia from the amide side chain of glutamine to an acceptor substrate, this Cys forms a Cys-His-Glu catalytic triad in the active site. Glutamine amidotransferases activity can be found in a range of biosynthetic enzymes included in this cd: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase, anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase (CPSase), cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. For Pyrococcus horikoshii PH1704, the Cys of the nucleophile elbow together with a different His and, a Glu from an adjacent monomer form a catalytic triad different from the typical GATase1 triad. Peptidase E is believed to be a serine peptidase having a Ser-His-Glu catalytic triad which differs from the Cys-His-Glu catalytic triad of typical GATase1 domains, by having a Ser in place of the reactive Cys at the nucleophile elbow. The E. coli HP-II C-terminal domain, S. meliloti Rm1021 ThuA and the A4 beta-galactosidase middle domain lack the catalytic triad typical GATaseI domains. GATase1-like domains can occur either as single polypeptides, as in Class I glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase. Peptidase E has a circular permutation in the common core of a typical GTAse1 domain.


Pssm-ID: 153222 [Multi-domain]  Cd Length: 92  Bit Score: 49.89  E-value: 3.01e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504406380  32 FIDALNLQPDDYVIVRPHLGE--TLPQFTDISGAVLSGSWaMVTDHADWSERTAAWIRAAMEARLPLLGVCYGHQLM 106
Cdd:cd03128   17 PLDALREAGAEVDVVSPDGGPveSDVDLDDYDGLILPGGP-GTPDDLAWDEALLALLREAAAAGKPVLGICLGAQLL 92
CarA COG0505
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ...
 86-195 7.27e-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: 51.95  E-value: 7.27e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504406380  86 IRAAMEARLPLLGVCYGHQLMAYALGGKVGDNPNGwERGL----MTLTT-----TSQArH----DPllATLPETfEAWLS 152
Cdd:COG0505  240 IRELLGKGIPIFGICLGHQLLALALGAKTYKLKFG-HRGAnhpvKDLETgrveiTSQN-HgfavDE--DSLPAT-DLEVT 314

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 504406380 153 HrqsvmtppahatvlaVSDMDG-CQVLRYSAC-ALSVQFHPE-----------FDR 195
Cdd:COG0505  315 H---------------VNLNDGtVEGLRHKDLpAFSVQYHPEaspgphdsaylFDR 355
PRK12564 PRK12564
carbamoyl-phosphate synthase small subunit;
86-192 4.13e-07

carbamoyl-phosphate synthase small subunit;


Pssm-ID: 237139 [Multi-domain]  Cd Length: 360  Bit Score: 49.69  E-value: 4.13e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504406380  86 IRAAMEARLPLLGVCYGHQLMAYALGG-----KVGdnpngwERGL----MTLTT-----TSQArH----DPllATLPETF 147
Cdd:PRK12564 241 IRELLEKKIPIFGICLGHQLLALALGAktykmKFG------HRGAnhpvKDLETgkveiTSQN-HgfavDE--DSLPANL 311

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 504406380 148 EAWlsHrqsvmtppahatvlaVSDMDG-CQVLRY-SACALSVQFHPE 192
Cdd:PRK12564 312 EVT--H---------------VNLNDGtVEGLRHkDLPAFSVQYHPE 341
GATase1_CPSase cd01744
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ...
 86-192 7.00e-07

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: 47.88  E-value: 7.00e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504406380  86 IRAAMEARLPLLGVCYGHQLMAYALGGKVGDNPNGwERGL----MTLTT-----TSQaRH----DPllATLPETFEawls 152
Cdd:cd01744   62 VRKLLGKKIPIFGICLGHQLLALALGAKTYKMKFG-HRGSnhpvKDLITgrvyiTSQ-NHgyavDP--DSLPGGLE---- 133

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 504406380 153 hrqsvmtppahatVLAVSDMDG-CQVLRY-SACALSVQFHPE 192
Cdd:cd01744  134 -------------VTHVNLNDGtVEGIRHkDLPVFSVQFHPE 162
PLN02347 PLN02347
GMP synthetase
 91-192 9.25e-07

GMP synthetase


Pssm-ID: 215197 [Multi-domain]  Cd Length: 536  Bit Score: 48.91  E-value: 9.25e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504406380  91 EARLPLLGVCYGHQLMAYALGGKVGDNPNGwERGLMTLTTtsqARHDPLLATLPE--TFEAWLSHRQSVMTPPAHATVLA 168
Cdd:PLN02347  84 ERGVPVLGICYGMQLIVQKLGGEVKPGEKQ-EYGRMEIRV---VCGSQLFGDLPSgeTQTVWMSHGDEAVKLPEGFEVVA 159

                         90       100
                 ....*....|....*....|....*
gi 504406380 169 VSDMDGCQVLRYSACAL-SVQFHPE 192
Cdd:PLN02347 160 KSVQGAVVAIENRERRIyGLQYHPE 184
PRK13566 PRK13566
anthranilate synthase component I;
83-192 1.15e-06

anthranilate synthase component I;


Pssm-ID: 237429 [Multi-domain]  Cd Length: 720  Bit Score: 48.76  E-value: 1.15e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504406380  83 AAWIRAAMEARLPLLGVCYGHQLMAYALGGKVG--DNPngwERGlmtltTTSQARH---DPLLATLPETFEAWLSH---- 153
Cdd:PRK13566 588 KATIDAALARNLPIFGVCLGLQAIVEAFGGELGqlAYP---MHG-----KPSRIRVrgpGRLFSGLPEEFTVGRYHslfa 659

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 504406380 154 -RQSVmtpPAHATVLAVSDmDGC------QVLRYSAcalsVQFHPE 192
Cdd:PRK13566 660 dPETL---PDELLVTAETE-DGVimaiehKTLPVAA----VQFHPE 697
PRK08007 PRK08007
aminodeoxychorismate synthase component 2;
93-192 8.25e-06

aminodeoxychorismate synthase component 2;


Pssm-ID: 181194 [Multi-domain]  Cd Length: 187  Bit Score: 44.91  E-value: 8.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504406380  93 RLPLLGVCYGHQLMAYALGGK--------------VGDNPNGWERGL---MTLTTTSQARHDPllATLPETFE--AWlSH 153
Cdd:PRK08007  72 RLPILGVCLGHQAMAQAFGGKvvraakvmhgktspITHNGEGVFRGLanpLTVTRYHSLVVEP--DSLPACFEvtAW-SE 148

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 504406380 154 RQSVMTppahatvlavsdmdgcqvLRYSACALS-VQFHPE 192
Cdd:PRK08007 149 TREIMG------------------IRHRQWDLEgVQFHPE 170
PRK07649 PRK07649
aminodeoxychorismate/anthranilate synthase component II;
93-192 1.09e-05

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181066 [Multi-domain]  Cd Length: 195  Bit Score: 44.79  E-value: 1.09e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504406380  93 RLPLLGVCYGHQLMAYALGGKVGDNpngwERgLMTlTTTSQARHD--PLLATLPETFEAWLSHRQSVM--TPPAHATVLA 168
Cdd:PRK07649  72 KIPIFGVCLGHQSIAQVFGGEVVRA----ER-LMH-GKTSLMHHDgkTIFSDIPNPFTATRYHSLIVKkeTLPDCLEVTS 145

                         90       100
                 ....*....|....*....|....*
gi 504406380 169 VSDMDGCQVLRYSACAL-SVQFHPE 192
Cdd:PRK07649 146 WTEEGEIMAIRHKTLPIeGVQFHPE 170
PLN02335 PLN02335
anthranilate synthase
 94-153 1.59e-05

anthranilate synthase


Pssm-ID: 177969 [Multi-domain]  Cd Length: 222  Bit Score: 44.40  E-value: 1.59e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 504406380  94 LPLLGVCYGHQLMAYALGGKVGDNPNGWERGLMTLTTTSQARHDPLLATLPETFEAWLSH 153
Cdd:PLN02335  92 VPLFGVCMGLQCIGEAFGGKIVRSPFGVMHGKSSPVHYDEKGEEGLFSGLPNPFTAGRYH 151
PRK06895 PRK06895
anthranilate synthase component II;
96-192 1.70e-05

anthranilate synthase component II;


Pssm-ID: 235882 [Multi-domain]  Cd Length: 190  Bit Score: 43.96  E-value: 1.70e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504406380  96 LLGVCYGHQLMAYALGGKVGDNPN---GWERGLMtltttsQARHDPLLATLPETFEAWLSHRQSVMTP--PAHATVLAVS 170
Cdd:PRK06895  75 ILGVCLGHQTLCEFFGGELYNLNNvrhGQQRPLK------VRSNSPLFDGLPEEFNIGLYHSWAVSEEnfPTPLEITAVC 148

                         90       100
                 ....*....|....*....|...
gi 504406380 171 DMDGCQVLRYSACAL-SVQFHPE 192
Cdd:PRK06895 149 DENVVMAMQHKTLPIyGVQFHPE 171
PRK14607 PRK14607
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;
93-192 1.72e-05

bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;


Pssm-ID: 237764 [Multi-domain]  Cd Length: 534  Bit Score: 45.09  E-value: 1.72e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504406380  93 RLPLLGVCYGHQLMAYALGGKVGDNPN--------------GWERGLMTLTTTSqaRHDPLL---ATLPETFEawlshrq 155
Cdd:PRK14607  73 KVPILGVCLGHQAIGYAFGGKIVHAKRilhgktspidhngkGLFRGIPNPTVAT--RYHSLVveeASLPECLE------- 143

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 504406380 156 svmtppahatVLAVSDmDG-CQVLRYSACAL-SVQFHPE 192
Cdd:PRK14607 144 ----------VTAKSD-DGeIMGIRHKEHPIfGVQFHPE 171
trpG CHL00101
anthranilate synthase component 2
 93-192 2.38e-05

anthranilate synthase component 2


Pssm-ID: 214365 [Multi-domain]  Cd Length: 190  Bit Score: 43.57  E-value: 2.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504406380  93 RLPLLGVCYGHQLMAYALGGKVGDNPNgwergLMTlTTTSQARH--DPLLATLPETFEAWLSHRQSV--MTPPAHATVLA 168
Cdd:CHL00101  72 YIPILGVCLGHQSIGYLFGGKIIKAPK-----PMH-GKTSKIYHnhDDLFQGLPNPFTATRYHSLIIdpLNLPSPLEITA 145

                         90       100
                 ....*....|....*....|....*...
gi 504406380 169 VSDmDG----CQvLRYSACALSVQFHPE 192
Cdd:CHL00101 146 WTE-DGlimaCR-HKKYKMLRGIQFHPE 171
PRK08857 PRK08857
aminodeoxychorismate/anthranilate synthase component II;
93-192 3.21e-05

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181566 [Multi-domain]  Cd Length: 193  Bit Score: 43.33  E-value: 3.21e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504406380  93 RLPLLGVCYGHQLMAYALGGKV--------------GDNPNGWERGLMT-LTTTsqaRHDPLLA---TLPETFE--AWLS 152
Cdd:PRK08857  72 KLPILGVCLGHQAIAQVFGGQVvrarqvmhgktspiRHTGRSVFKGLNNpLTVT---RYHSLVVkndTLPECFEltAWTE 148

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 504406380 153 HRQsvmtppahatvlavSDMDGCQVLRYSACAL-SVQFHPE 192
Cdd:PRK08857 149 LED--------------GSMDEIMGFQHKTLPIeAVQFHPE 175
PRK06774 PRK06774
aminodeoxychorismate synthase component II;
93-192 3.47e-05

aminodeoxychorismate synthase component II;


Pssm-ID: 180689 [Multi-domain]  Cd Length: 191  Bit Score: 43.31  E-value: 3.47e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504406380  93 RLPLLGVCYGHQLMAYALGGKV--------------GDNPNGWERGL-MTLTTTsqaRHDPLL---ATLPETFE--AWLS 152
Cdd:PRK06774  72 KLPILGVCLGHQALGQAFGARVvrarqvmhgktsaiCHSGQGVFRGLnQPLTVT---RYHSLViaaDSLPGCFEltAWSE 148

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 504406380 153 HRqsvmtppahatvlavSDMDGCQVLRYSACALS-VQFHPE 192
Cdd:PRK06774 149 RG---------------GEMDEIMGIRHRTLPLEgVQFHPE 174
trpG_papA TIGR00566
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This ...
 93-192 1.84e-04

glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This model describes the glutamine amidotransferase domain or peptide of the tryptophan-biosynthetic pathway enzyme anthranilate synthase or of the folate biosynthetic pathway enzyme para-aminobenzoate synthase. In at least one case, a single polypeptide from Bacillus subtilis was shown to have both functions. This model covers a subset of the sequences described by the Pfam model GATase.


Pssm-ID: 273144 [Multi-domain]  Cd Length: 188  Bit Score: 40.93  E-value: 1.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504406380   93 RLPLLGVCYGHQLMAYALGGKVGD--------------NPNGWERGLMT-LTTTsqaRHDPLL---ATLPETFE--AWLS 152
Cdd:TIGR00566  72 KLPILGVCLGHQAMGQAFGGDVVRantvmhgktseiehNGAGIFRGLFNpLTAT---RYHSLVvepETLPTCFPvtAWEE 148

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 504406380  153 HRQSVMTppahatvlavsdmdgcqvLRYSACAL-SVQFHPE 192
Cdd:TIGR00566 149 ENIEIMA------------------IRHRDLPLeGVQFHPE 171
PLN02771 PLN02771
carbamoyl-phosphate synthase (glutamine-hydrolyzing)
 93-192 6.92e-04

carbamoyl-phosphate synthase (glutamine-hydrolyzing)


Pssm-ID: 178370 [Multi-domain]  Cd Length: 415  Bit Score: 40.35  E-value: 6.92e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504406380  93 RLPLLGVCYGHQLMAYALGGKV---------GDNPngwERGLMTLTTTSQARH-----DPllATLPETFEawlshrqsvm 158
Cdd:PLN02771 310 KVPVFGICMGHQLLGQALGGKTfkmkfghhgGNHP---VRNNRTGRVEISAQNhnyavDP--ASLPEGVE---------- 374

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 504406380 159 tppahatVLAVSDMDG-CQVLRYSAC-ALSVQFHPE 192
Cdd:PLN02771 375 -------VTHVNLNDGsCAGLAFPALnVMSLQYHPE 403
PRK09522 PRK09522
bifunctional anthranilate synthase glutamate amidotransferase component TrpG/anthranilate ...
 90-192 8.72e-04

bifunctional anthranilate synthase glutamate amidotransferase component TrpG/anthranilate phosphoribosyltransferase TrpD;


Pssm-ID: 181927 [Multi-domain]  Cd Length: 531  Bit Score: 40.01  E-value: 8.72e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504406380  90 MEARLPLLGVCYGHQLMAYALGGKVGdnpngwERGLMTLTTTSQARHD--PLLATLPETFEAWLSHRQSVMTPPAHATVL 167
Cdd:PRK09522  74 LRGKLPIIGICLGHQAIVEAYGGYVG------QAGEILHGKASSIEHDgqAMFAGLTNPLPVARYHSLVGSNIPAGLTIN 147

                         90       100
                 ....*....|....*....|....*....
gi 504406380 168 AvsDMDG-CQVLRYSA---CALsvQFHPE 192
Cdd:PRK09522 148 A--HFNGmVMAVRHDAdrvCGF--QFHPE 172
PRK12838 PRK12838
carbamoyl phosphate synthase small subunit; Reviewed
 93-192 2.04e-03

carbamoyl phosphate synthase small subunit; Reviewed


Pssm-ID: 183784 [Multi-domain]  Cd Length: 354  Bit Score: 38.72  E-value: 2.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504406380  93 RLPLLGVCYGHQLMAYALGGKVGDNPNGwERGL----MTLTT-----TSQaRHDPLL--ATLPETfeawlshrqsvmtpP 161
Cdd:PRK12838 237 SYPILGICLGHQLIALALGADTEKLPFG-HRGAnhpvIDLTTgrvwmTSQ-NHGYVVdeDSLDGT--------------P 300

                         90       100       110
                 ....*....|....*....|....*....|....
gi 504406380 162 AHATVLAVSD--MDGcqvLRY-SACALSVQFHPE 192
Cdd:PRK12838 301 LSVRFFNVNDgsIEG---LRHkKKPVLSVQFHPE 331
hisH PRK13146
imidazole glycerol phosphate synthase subunit HisH; Provisional
 86-192 4.60e-03

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237290 [Multi-domain]  Cd Length: 209  Bit Score: 37.07  E-value: 4.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504406380  86 IRAAMEARLPLLGVCYGHQLMAYA------------LGGKV----GDNPN------GWerglmtlTTTSQARHDPLLATL 143
Cdd:PRK13146  70 IEAVLAAGRPFLGICVGMQLLFERglehgdtpglglIPGEVvrfqPDGPAlkvphmGW-------NTVDQTRDHPLFAGI 142

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 504406380 144 PETFEAWLSHrqSVMTPPAH-ATVLAVSDMDG---CQVLRYSACAlsVQFHPE 192
Cdd:PRK13146 143 PDGARFYFVH--SYYAQPANpADVVAWTDYGGpftAAVARDNLFA--TQFHPE 191
 
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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