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Conserved domains on  [gi|56679615|gb|AAV96281|]
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glutamine amidotransferase, class I [Ruegeria pomeroyi DSS-3]

Protein Classification

type 1 glutamine amidotransferase( domain architecture ID 10109690)

type 1 glutamine amidotransferase similar to Pseudomonas sp. gamma-glutamyl-L-alaninol (GALO) hydrolase, which catalyzes the hydrolysis of GALO to form L-alaninol and L-glutamate, and to Arabidopsis thaliana gamma-glutamyl peptidases, which hydrolyze the gamma-glutamyl peptide bond of glutathione conjugates

EC:  3.4.-.-
Gene Ontology:  GO:0016787
MEROPS:  C26
PubMed:  10387030
SCOP:  4003747

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GATase1_1 cd01741
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 4-196 7.67e-37

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: 128.90  E-value: 7.67e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56679615   4 ILIVESSSPGIASARRELGRAApqnfsrvfaaAIPDIKIRVVEPYLKELtCADFDGVDGVVMT-GAGDDWAADDDLATPI 82
Cdd:cd01741   2 ILILQHDTPEGPGLFEDLLREA----------GAETIEIDVVDVYAGEL-LPDLDDYDGLVILgGPMSVDEDDYPWLKKL 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56679615  83 RAACDLALETGRPVLGVCYGLQIATVCLGGKIAASPKGKETGLAlKVELTEQGARHPMMQGRRQGFSVACAHRDEVIRMP 162
Cdd:cd01741  71 KELIRQALAAGKPVLGICLGHQLLARALGGKVGRNPKGWEIGWF-PVTLTEAGKADPLFAGLPDEFPVFHWHGDTVVELP 149

                       170       180       190
                ....*....|....*....|....*....|....
gi 56679615 163 DGGQRLAYNAHSDVQAMSVQQSgvdFWGLQYHPE 196
Cdd:cd01741 150 PGAVLLASSEACPNQAFRYGDR---ALGLQFHPE 180
 
Name Accession Description Interval E-value
GATase1_1 cd01741
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 4-196 7.67e-37

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: 128.90  E-value: 7.67e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56679615   4 ILIVESSSPGIASARRELGRAApqnfsrvfaaAIPDIKIRVVEPYLKELtCADFDGVDGVVMT-GAGDDWAADDDLATPI 82
Cdd:cd01741   2 ILILQHDTPEGPGLFEDLLREA----------GAETIEIDVVDVYAGEL-LPDLDDYDGLVILgGPMSVDEDDYPWLKKL 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56679615  83 RAACDLALETGRPVLGVCYGLQIATVCLGGKIAASPKGKETGLAlKVELTEQGARHPMMQGRRQGFSVACAHRDEVIRMP 162
Cdd:cd01741  71 KELIRQALAAGKPVLGICLGHQLLARALGGKVGRNPKGWEIGWF-PVTLTEAGKADPLFAGLPDEFPVFHWHGDTVVELP 149

                       170       180       190
                ....*....|....*....|....*....|....
gi 56679615 163 DGGQRLAYNAHSDVQAMSVQQSgvdFWGLQYHPE 196
Cdd:cd01741 150 PGAVLLASSEACPNQAFRYGDR---ALGLQFHPE 180
GuaA1 COG0518
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ...
 26-236 7.61e-36

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: 127.37  E-value: 7.61e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56679615  26 PQNFSRVFAAAipDIKIRVVEPYLKEL--TCADFDGVDGVVMTGAGDDWAADDDLATPIRAACDLALETGRPVLGVCYGL 103
Cdd:COG0518  15 PGLIARRLREA--GIELDVLRVYAGEIlpYDPDLEDPDGLILSGGPMSVYDEDPWLEDEPALIREAFELGKPVLGICYGA 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56679615 104 QIATVCLGGKIAASPkGKETGLAlKVELTEQgarHPMMQGRRQGFSVACAHRDEVIRMPDGGQRLAYNAHSDVQAMSVqq 183
Cdd:COG0518  93 QLLAHALGGKVEPGP-GREIGWA-PVELTEA---DPLFAGLPDEFTVWMSHGDTVTELPEGAEVLASSDNCPNQAFRY-- 165

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 56679615 184 sGVDFWGLQYHPEISPSIVANAIREHGSLFSNTGIDIEDLLKVETDLETAQRL 236
Cdd:COG0518 166 -GRRVYGVQFHPEVTHTMMEAWLEERADELAAEELLAEASLHDPELREAGRRL 217
PRK09065 PRK09065
glutamine amidotransferase; Provisional
 1-243 1.45e-25

glutamine amidotransferase; Provisional


Pssm-ID: 181635 [Multi-domain]  Cd Length: 237  Bit Score: 100.81  E-value: 1.45e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56679615    1 MPEILIVESSSPgIASARRELGRAaPQNFSRvfAAAIPDIKIRVVEPYLKELTcADFDGVDGVVMTGAGDDWAADDDLAT 80
Cdd:PRK09065   1 VKPLLIIQTGTP-PPSIRARYGDF-PHWIRV--ALGLAEQPVVVVRVFAGEPL-PAPDDFAGVIITGSWAMVTDRLDWSE 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56679615   81 PIRAACDLALETGRPVLGVCYGLQIATVCLGGKIAASPKGKETGLaLKVELTEQGARHPMMQGRRQGFSVACAHRDEVIR 160
Cdd:PRK09065  76 RTADWLRQAAAAGMPLLGICYGHQLLAHALGGEVGYNPAGRESGT-VTVELHPAAADDPLFAGLPAQFPAHLTHLQSVLR 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56679615  161 MPDGGQRLAYNAHSDVQAMSVQQSGvdfWGLQYHPEISPSIVANAIREHGSLFSNTGIDIEDLLKVETDLETAQRLgcsL 240
Cdd:PRK09065 155 LPPGAVVLARSAQDPHQAFRYGPHA---WGVQFHPEFTAHIMRAYLRARADCLRREGLDARTLLREVSEAPWARKL---L 228


                 ...
gi 56679615  241 ADF 243
Cdd:PRK09065 229 RRF 231
GATase pfam00117
Glutamine amidotransferase class-I;
89-200 1.27e-10

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 59.17  E-value: 1.27e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56679615    89 ALETGRPVLGVCYGLQIATVCLGGKIAASPKGKETGLALKVELTEQGARhpmmQGRRQGFSVACAHRDEVIRM--PDGGQ 166
Cdd:pfam00117  66 ARELKIPILGICLGHQLLALAFGGKVVKAKKFGHHGKNSPVGDDGCGLF----YGLPNVFIVRRYHSYAVDPDtlPDGLE 141

                          90       100       110
                  ....*....|....*....|....*....|....
gi 56679615   167 RLAYNAHsDVQAMSVQQSGVDFWGLQYHPEISPS 200
Cdd:pfam00117 142 VTATSEN-DGTIMGIRHKKLPIFGVQFHPESILT 174
 
Name Accession Description Interval E-value
GATase1_1 cd01741
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 4-196 7.67e-37

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: 128.90  E-value: 7.67e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56679615   4 ILIVESSSPGIASARRELGRAApqnfsrvfaaAIPDIKIRVVEPYLKELtCADFDGVDGVVMT-GAGDDWAADDDLATPI 82
Cdd:cd01741   2 ILILQHDTPEGPGLFEDLLREA----------GAETIEIDVVDVYAGEL-LPDLDDYDGLVILgGPMSVDEDDYPWLKKL 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56679615  83 RAACDLALETGRPVLGVCYGLQIATVCLGGKIAASPKGKETGLAlKVELTEQGARHPMMQGRRQGFSVACAHRDEVIRMP 162
Cdd:cd01741  71 KELIRQALAAGKPVLGICLGHQLLARALGGKVGRNPKGWEIGWF-PVTLTEAGKADPLFAGLPDEFPVFHWHGDTVVELP 149

                       170       180       190
                ....*....|....*....|....*....|....
gi 56679615 163 DGGQRLAYNAHSDVQAMSVQQSgvdFWGLQYHPE 196
Cdd:cd01741 150 PGAVLLASSEACPNQAFRYGDR---ALGLQFHPE 180
GuaA1 COG0518
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ...
 26-236 7.61e-36

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: 127.37  E-value: 7.61e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56679615  26 PQNFSRVFAAAipDIKIRVVEPYLKEL--TCADFDGVDGVVMTGAGDDWAADDDLATPIRAACDLALETGRPVLGVCYGL 103
Cdd:COG0518  15 PGLIARRLREA--GIELDVLRVYAGEIlpYDPDLEDPDGLILSGGPMSVYDEDPWLEDEPALIREAFELGKPVLGICYGA 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56679615 104 QIATVCLGGKIAASPkGKETGLAlKVELTEQgarHPMMQGRRQGFSVACAHRDEVIRMPDGGQRLAYNAHSDVQAMSVqq 183
Cdd:COG0518  93 QLLAHALGGKVEPGP-GREIGWA-PVELTEA---DPLFAGLPDEFTVWMSHGDTVTELPEGAEVLASSDNCPNQAFRY-- 165

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 56679615 184 sGVDFWGLQYHPEISPSIVANAIREHGSLFSNTGIDIEDLLKVETDLETAQRL 236
Cdd:COG0518 166 -GRRVYGVQFHPEVTHTMMEAWLEERADELAAEELLAEASLHDPELREAGRRL 217
PRK09065 PRK09065
glutamine amidotransferase; Provisional
 1-243 1.45e-25

glutamine amidotransferase; Provisional


Pssm-ID: 181635 [Multi-domain]  Cd Length: 237  Bit Score: 100.81  E-value: 1.45e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56679615    1 MPEILIVESSSPgIASARRELGRAaPQNFSRvfAAAIPDIKIRVVEPYLKELTcADFDGVDGVVMTGAGDDWAADDDLAT 80
Cdd:PRK09065   1 VKPLLIIQTGTP-PPSIRARYGDF-PHWIRV--ALGLAEQPVVVVRVFAGEPL-PAPDDFAGVIITGSWAMVTDRLDWSE 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56679615   81 PIRAACDLALETGRPVLGVCYGLQIATVCLGGKIAASPKGKETGLaLKVELTEQGARHPMMQGRRQGFSVACAHRDEVIR 160
Cdd:PRK09065  76 RTADWLRQAAAAGMPLLGICYGHQLLAHALGGEVGYNPAGRESGT-VTVELHPAAADDPLFAGLPAQFPAHLTHLQSVLR 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56679615  161 MPDGGQRLAYNAHSDVQAMSVQQSGvdfWGLQYHPEISPSIVANAIREHGSLFSNTGIDIEDLLKVETDLETAQRLgcsL 240
Cdd:PRK09065 155 LPPGAVVLARSAQDPHQAFRYGPHA---WGVQFHPEFTAHIMRAYLRARADCLRREGLDARTLLREVSEAPWARKL---L 228


                 ...
gi 56679615  241 ADF 243
Cdd:PRK09065 229 RRF 231
GATase1_GMP_Synthase cd01742
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine ...
 90-215 6.65e-17

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: 76.04  E-value: 6.65e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56679615  90 LETGRPVLGVCYGLQIATVCLGGKIAASPKGkETGLAlKVELTEQGarhPMMQGRRQGFSVACAHRDEVIRMPDGGQRLA 169
Cdd:cd01742  67 FELGVPVLGICYGMQLIAKALGGKVERGDKR-EYGKA-EIEIDDSS---PLFEGLPDEQTVWMSHGDEVVKLPEGFKVIA 141

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 56679615 170 YNAHSDVQAMsvQQSGVDFWGLQYHPEISPSivanairEHGS-LFSN 215
Cdd:cd01742 142 SSDNCPVAAI--ANEEKKIYGVQFHPEVTHT-------EKGKeILKN 179
guaA PRK00074
GMP synthase; Reviewed
 90-200 7.36e-15

GMP synthase; Reviewed


Pssm-ID: 234614 [Multi-domain]  Cd Length: 511  Bit Score: 73.93  E-value: 7.36e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56679615   90 LETGRPVLGVCYGLQIATVCLGGKIAASPKGkETGLAlKVELTEQgarHPMMQGRRQGFSVACAHRDEVIRMPDGGQRLA 169
Cdd:PRK00074  72 FELGVPVLGICYGMQLMAHQLGGKVERAGKR-EYGRA-ELEVDND---SPLFKGLPEEQDVWMSHGDKVTELPEGFKVIA 146

                         90       100       110
                 ....*....|....*....|....*....|.
gi 56679615  170 YNAHSDVQAMSVQQSGvdFWGLQYHPEISPS 200
Cdd:PRK00074 147 STENCPIAAIANEERK--FYGVQFHPEVTHT 175
PLN02347 PLN02347
GMP synthetase
 87-200 1.54e-13

GMP synthetase


Pssm-ID: 215197 [Multi-domain]  Cd Length: 536  Bit Score: 70.10  E-value: 1.54e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56679615   87 DLALETGRPVLGVCYGLQIATVCLGGKIAASPKGkETGLALKVELTEQGARHPMMQGRRQgfSVACAHRDEVIRMPDGGQ 166
Cdd:PLN02347  80 DYCRERGVPVLGICYGMQLIVQKLGGEVKPGEKQ-EYGRMEIRVVCGSQLFGDLPSGETQ--TVWMSHGDEAVKLPEGFE 156

                         90       100       110
                 ....*....|....*....|....*....|....
gi 56679615  167 RLAYNAHSDVQAMSVQQSGvdFWGLQYHPEISPS 200
Cdd:PLN02347 157 VVAKSVQGAVVAIENRERR--IYGLQYHPEVTHS 188
PRK00758 PRK00758
GMP synthase subunit A; Validated
 87-215 1.34e-12

GMP synthase subunit A; Validated


Pssm-ID: 179112 [Multi-domain]  Cd Length: 184  Bit Score: 64.49  E-value: 1.34e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56679615   87 DLALETGRPVLGVCYGLQIATVCLGGKIAaspKGKETGLAL-KVELTEQgarHPMMQGRRQGFSVACAHRDEVIRMPDGG 165
Cdd:PRK00758  61 EYLKELDVPILGICLGHQLIAKAFGGEVG---RGEYGEYALvEVEILDE---DDILKGLPPEIRVWASHADEVKELPDGF 134

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 56679615  166 QRLAYNAHSDVQAMSvqQSGVDFWGLQYHPEISPSivanairEHGS-LFSN 215
Cdd:PRK00758 135 EILARSDICEVEAMK--HKEKPIYGVQFHPEVAHT-------EYGEeIFKN 176
GATase pfam00117
Glutamine amidotransferase class-I;
89-200 1.27e-10

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 59.17  E-value: 1.27e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56679615    89 ALETGRPVLGVCYGLQIATVCLGGKIAASPKGKETGLALKVELTEQGARhpmmQGRRQGFSVACAHRDEVIRM--PDGGQ 166
Cdd:pfam00117  66 ARELKIPILGICLGHQLLALAFGGKVVKAKKFGHHGKNSPVGDDGCGLF----YGLPNVFIVRRYHSYAVDPDtlPDGLE 141

                          90       100       110
                  ....*....|....*....|....*....|....
gi 56679615   167 RLAYNAHsDVQAMSVQQSGVDFWGLQYHPEISPS 200
Cdd:pfam00117 142 VTATSEN-DGTIMGIRHKKLPIFGVQFHPESILT 174
PRK07567 PRK07567
glutamine amidotransferase; Provisional
 95-210 5.07e-10

glutamine amidotransferase; Provisional


Pssm-ID: 181035 [Multi-domain]  Cd Length: 242  Bit Score: 58.03  E-value: 5.07e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56679615   95 PVLGVCYGLQIATVCLGGKIAASpKGKETGlALKVELTEQGARHPMMQGRRQGFSVACAHRDEVIRMPDGGQRLAYNAHS 174
Cdd:PRK07567  95 PFLGACYGVGTLGHHQGGVVDRT-YGEPVG-AVTVSLTDAGRADPLLAGLPDTFTAFVGHKEAVSALPPGAVLLATSPTC 172

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 56679615  175 DVQAMSVQQSgvdFWGLQYHPEISPSIVANAI---REHG 210
Cdd:PRK07567 173 PVQMFRVGEN---VYATQFHPELDADGLKTRIdfyRDHG 208
GATase1_Anthranilate_Synthase cd01743
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ...
 80-201 1.39e-09

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: 56.00  E-value: 1.39e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56679615  80 TPIRAACDL----ALETGRPVLGVCYGLQIATVCLGGKI--AASPKGketGLALKVELTEQGarhpMMQGRRQGFSVACA 153
Cdd:cd01743  54 HPEDAGISLeiirALAGKVPILGVCLGHQAIAEAFGGKVvrAPEPMH---GKTSEIHHDGSG----LFKGLPQPFTVGRY 126

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 56679615 154 HRDEVIRMPDGGQRLAYNAHSDVQAMSVQQSGVDFWGLQYHPEispSI 201
Cdd:cd01743 127 HSLVVDPDPLPDLLEVTASTEDGVIMALRHRDLPIYGVQFHPE---SI 171
PRK06490 PRK06490
glutamine amidotransferase; Provisional
 87-197 4.84e-09

glutamine amidotransferase; Provisional


Pssm-ID: 180590 [Multi-domain]  Cd Length: 239  Bit Score: 55.35  E-value: 4.84e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56679615   87 DLALETGRPVLGVCYGLQIATVCLGGKIAASPKGK-ETGLaLKVELTEQG---ARHPMM--QGRRQGFSvacahrdevir 160
Cdd:PRK06490  80 SVPLKENKPFLGICLGAQMLARHLGARVAPHPDGRvEIGY-YPLRPTEAGralMHWPEMvyHWHREGFD----------- 147

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 56679615  161 MPDGGQRLAYNAHSDVQAMsvqQSGVDFWGLQYHPEI 197
Cdd:PRK06490 148 LPAGAELLATGDDFPNQAF---RYGDNAWGLQFHPEV 181
PRK05665 PRK05665
amidotransferase; Provisional
 90-196 9.89e-08

amidotransferase; Provisional


Pssm-ID: 168162 [Multi-domain]  Cd Length: 240  Bit Score: 51.35  E-value: 9.89e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56679615   90 LETGRPVLGVCYGLQIATVCLGGKIAASPKGKETGlalkVELTEQGARHPMMQGRRQGFSVACAHRDEVIRMPDGGQRLA 169
Cdd:PRK05665  88 YERGDKLLGVCFGHQLLALLLGGKAERASQGWGVG----IHRYQLAAHAPWMSPAVTELTLLISHQDQVTALPEGATVIA 163

                         90       100
                 ....*....|....*....|....*..
gi 56679615  170 YNAHSDVQAMSVQQSGVDFwglQYHPE 196
Cdd:PRK05665 164 SSDFCPFAAYHIGDQVLCF---QGHPE 187
PRK07053 PRK07053
glutamine amidotransferase; Provisional
 90-223 3.85e-07

glutamine amidotransferase; Provisional


Pssm-ID: 235919 [Multi-domain]  Cd Length: 234  Bit Score: 49.56  E-value: 3.85e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56679615   90 LETGRPVLGVCYGLQIATVCLGGKIAASPkGKETGLAlKVELTEQGARHPMmqgrrqgfsvacAHRDEVIRM-------- 161
Cdd:PRK07053  80 LAAGLPTLGICLGAQLIARALGARVYPGG-QKEIGWA-PLTLTDAGRASPL------------RHLGAGTPVlhwhgdtf 145

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 56679615  162 --PDGGQRLAYNAHSDVQAMSVQQSGVdfwGLQYHPEISPSIVANAIREHGSLFSNTGIDIEDL 223
Cdd:PRK07053 146 dlPEGATLLASTPACRHQAFAWGNHVL---ALQFHPEAREDRFEAWLIGHAGELAAAGIDPRTL 206
PRK08250 PRK08250
glutamine amidotransferase; Provisional
 89-217 7.74e-06

glutamine amidotransferase; Provisional


Pssm-ID: 181323 [Multi-domain]  Cd Length: 235  Bit Score: 45.73  E-value: 7.74e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56679615   89 ALETGRPVLGVCYGLQIATVCLGGKIAASPKgKETGLaLKVELTEQGARHPMMQGRRQGFSVACAHRDevirMP---DGG 165
Cdd:PRK08250  80 AIKAGKAVIGVCLGAQLIGEALGAKYEHSPE-KEIGY-FPITLTEAGLKDPLLSHFGSTLTVGHWHND----MPgltDQA 153

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 56679615  166 QRLAYNAHSDVQAmsVQQSGVDFwGLQYHPEISPSIVANAIREHGSLFSNTG 217
Cdd:PRK08250 154 KVLATSEGCPRQI--VQYSNLVY-GFQCHMEFTVEAVELLIAHSQQELSQAQ 202
PuuD COG2071
Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (putrescine degradation), contains ...
 84-196 2.20e-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: 41.31  E-value: 2.20e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56679615  84 AACDLALETGRPVLGVCYGLQIATVCLGG------------KIAASPKGKETGLALKVELTEQGARHPMMQGRRqgFSVA 151
Cdd:COG2071  87 ALIRAALERGKPVLGICRGMQLLNVALGGtlyqdlpdqvpgALDHRQPAPRYAPRHTVEIEPGSRLARILGEEE--IRVN 164

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 56679615 152 CAHR---DEVirmpdgGQRLAYNAHSD---VQAMSVQQSGvDFWGLQYHPE 196
Cdd:COG2071 165 SLHHqavKRL------GPGLRVSARAPdgvIEAIESPGAP-FVLGVQWHPE 208
Peptidase_C26 pfam07722
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ...
 89-196 3.36e-04

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: 40.70  E-value: 3.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56679615    89 ALETGRPVLGVCYGLQIATVCLGGKIA-------------ASPKGKETGLALKVELTEQG--ARHPmmqGRRQgFSVACA 153
Cdd:pfam07722 101 ALARGKPILGICRGFQLLNVALGGTLYqdiqeqpgftdhrEHCQVAPYAPSHAVNVEPGSllASLL---GSEE-FRVNSL 176

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 56679615   154 HRDEVIRMPDGGQRLAYNAHSDVQAMSVQQSGVDFWGLQYHPE 196
Cdd:pfam07722 177 HHQAIDRLAPGLRVEAVAPDGTIEAIESPNAKGFALGVQWHPE 219
PRK05670 PRK05670
anthranilate synthase component II; Provisional
 95-201 1.80e-03

anthranilate synthase component II; Provisional


Pssm-ID: 235552 [Multi-domain]  Cd Length: 189  Bit Score: 38.19  E-value: 1.80e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56679615   95 PVLGVCYGLQIATVCLGGKIAASPK---GKetglALKVELTEQGarhpMMQGRRQGFSVACAHRDEVIR--MPDGgqrLA 169
Cdd:PRK05670  74 PILGVCLGHQAIGEAFGGKVVRAKEimhGK----TSPIEHDGSG----IFAGLPNPFTVTRYHSLVVDResLPDC---LE 142

                         90       100       110
                 ....*....|....*....|....*....|...
gi 56679615  170 YNAHS-DVQAMSVQQSGVDFWGLQYHPEispSI 201
Cdd:PRK05670 143 VTAWTdDGEIMGVRHKELPIYGVQFHPE---SI 172
carA CHL00197
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional
 95-199 3.20e-03

carbamoyl-phosphate synthase arginine-specific small subunit; Provisional


Pssm-ID: 214392 [Multi-domain]  Cd Length: 382  Bit Score: 38.62  E-value: 3.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56679615   95 PVLGVCYGLQIATVCLGGKIAASPKGKE-----TGLALKVELTEQGarhpmmqgrrQGFSVacaHRDEVIRMPDGGQRLA 169
Cdd:CHL00197 265 PIFGICMGHQILSLALEAKTFKLKFGHRglnhpSGLNQQVEITSQN----------HGFAV---NLESLAKNKFYITHFN 331

                         90       100       110
                 ....*....|....*....|....*....|
gi 56679615  170 YNahsDVQAMSVQQSGVDFWGLQYHPEISP 199
Cdd:CHL00197 332 LN---DGTVAGISHSPKPYFSVQYHPEASP 358
PLN02771 PLN02771
carbamoyl-phosphate synthase (glutamine-hydrolyzing)
 95-199 4.30e-03

carbamoyl-phosphate synthase (glutamine-hydrolyzing)


Pssm-ID: 178370 [Multi-domain]  Cd Length: 415  Bit Score: 38.04  E-value: 4.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56679615   95 PVLGVCYGLQIATVCLGGKiaaspkgketglALKVELTEQGARHPMMQGRRQGFSVACAHRDEVI---RMPDGGQRLAYN 171
Cdd:PLN02771 312 PVFGICMGHQLLGQALGGK------------TFKMKFGHHGGNHPVRNNRTGRVEISAQNHNYAVdpaSLPEGVEVTHVN 379

                         90       100
                 ....*....|....*....|....*...
gi 56679615  172 AhSDVQAMSVQQSGVDFWGLQYHPEISP 199
Cdd:PLN02771 380 L-NDGSCAGLAFPALNVMSLQYHPEASP 406
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 24-112 8.15e-03

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: 35.27  E-value: 8.15e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56679615  24 AAPQNFSRVFAAAipDIKIRVVEPYLKELTC-ADFDGVDGVVMTGAGDDWAADDDLATPIRAACDlALETGRPVLGVCYG 102
Cdd:cd01653  12 LELASPLDALREA--GAEVDVVSPDGGPVESdVDLDDYDGLILPGGPGTPDDLARDEALLALLRE-AAAAGKPILGICLG 88

                        90
                ....*....|
gi 56679615 103 LQIATVCLGG 112
Cdd:cd01653  89 AQLLVLGVQF 98
PRK13566 PRK13566
anthranilate synthase component I;
82-207 9.01e-03

anthranilate synthase component I;


Pssm-ID: 237429 [Multi-domain]  Cd Length: 720  Bit Score: 37.20  E-value: 9.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56679615   82 IRAACDLALETGRPVLGVCYGLQIATVCLGGKIA--ASPkgkETGLALKVELTEQGArhpMMQGRRQGFSVACAH----- 154
Cdd:PRK13566 587 CKATIDAALARNLPIFGVCLGLQAIVEAFGGELGqlAYP---MHGKPSRIRVRGPGR---LFSGLPEEFTVGRYHslfad 660

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 56679615  155 RDeviRMPDGgqrLAYNAHS-DVQAMSVQQSGVDFWGLQYHPE--------ISPSIVANAIR 207
Cdd:PRK13566 661 PE---TLPDE---LLVTAETeDGVIMAIEHKTLPVAAVQFHPEsimtlggdVGLRIIENVVR 716
 
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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