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Conserved domains on  [gi|15234763|ref|NP_194782|]
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Class I glutamine amidotransferase-like superfamily protein [Arabidopsis thaliana]

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 ...
 35-194 1.65e-46

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: 153.17  E-value: 1.65e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234763  35 GDEGEHWDSFRVVSGEFPdeKDLEKYDGFVISGSSHDAFEND-DWILKLCDIVKKIDEMKKKILGICFGHQIIARVRGGT 113
Cdd:cd01741  24 GAETIEIDVVDVYAGELL--PDLDDYDGLVILGGPMSVDEDDyPWLKKLKELIRQALAAGKPVLGICLGHQLLARALGGK 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234763 114 VGRAKKGPELKLGDITIVKDAITPGSYFGneIPDSIAIIKCHQDEVLVLPETAKVLAYSKNYEVEMYSIEDHLFCIQGHP 193
Cdd:cd01741 102 VGRNPKGWEIGWFPVTLTEAGKADPLFAG--LPDEFPVFHWHGDTVVELPPGAVLLASSEACPNQAFRYGDRALGLQFHP 179


                .
gi 15234763 194 E 194
Cdd:cd01741 180 E 180
 
Name Accession Description Interval E-value
GATase1_1 cd01741
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 35-194 1.65e-46

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: 153.17  E-value: 1.65e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234763  35 GDEGEHWDSFRVVSGEFPdeKDLEKYDGFVISGSSHDAFEND-DWILKLCDIVKKIDEMKKKILGICFGHQIIARVRGGT 113
Cdd:cd01741  24 GAETIEIDVVDVYAGELL--PDLDDYDGLVILGGPMSVDEDDyPWLKKLKELIRQALAAGKPVLGICLGHQLLARALGGK 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234763 114 VGRAKKGPELKLGDITIVKDAITPGSYFGneIPDSIAIIKCHQDEVLVLPETAKVLAYSKNYEVEMYSIEDHLFCIQGHP 193
Cdd:cd01741 102 VGRNPKGWEIGWFPVTLTEAGKADPLFAG--LPDEFPVFHWHGDTVVELPPGAVLLASSEACPNQAFRYGDRALGLQFHP 179


                .
gi 15234763 194 E 194
Cdd:cd01741 180 E 180
GuaA1 COG0518
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ...
 23-245 4.60e-46

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: 153.18  E-value: 4.60e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234763  23 YGGYHNVFVTTFGDEGEHWDSFRVVSGEF-PDEKDLEKYDGFVISGSSHDAFENDDWILKLCDIVKKIDEMKKKILGICF 101
Cdd:COG0518  11 GGQYPGLIARRLREAGIELDVLRVYAGEIlPYDPDLEDPDGLILSGGPMSVYDEDPWLEDEPALIREAFELGKPVLGICY 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234763 102 GHQIIARVRGGTVGRAkKGPELKLGDITIV-KDAITPGsyfgneIPDSIAIIKCHQDEVLVLPETAKVLAYSKNYEVEMY 180
Cdd:COG0518  91 GAQLLAHALGGKVEPG-PGREIGWAPVELTeADPLFAG------LPDEFTVWMSHGDTVTELPEGAEVLASSDNCPNQAF 163

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15234763 181 SIEDHLFCIQGHPEYNKeilfEIVDRVLALGYVKQEFADAAKATMENRGADRKLWETICKNFLKG 245
Cdd:COG0518 164 RYGRRVYGVQFHPEVTH----TMMEAWLEERADELAAEELLAEASLHDPELREAGRRLLRNFLRE 224
PRK05665 PRK05665
amidotransferase; Provisional
 14-195 1.86e-33

amidotransferase; Provisional


Pssm-ID: 168162 [Multi-domain]  Cd Length: 240  Bit Score: 121.07  E-value: 1.86e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234763   14 LDSEFVKKtYGGYHNVFVTTFGDEGEHW--DSFRVVSGEFPdeKDLEKYDGFVISGSSHDAFENDDWILKLCDIVKKIDE 91
Cdd:PRK05665  13 LRPELVAQ-YQGYGRMFEQLFARQPIAAefVVYNVVQGDYP--ADDEKFDAYLVTGSKADSFGTDPWIQTLKTYLLKLYE 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234763   92 MKKKILGICFGHQIIARVRGGTVGRAKKGpelklGDITIVKDAITPGSYFGNEIPDSIAIIKCHQDEVLVLPETAKVLAY 171
Cdd:PRK05665  90 RGDKLLGVCFGHQLLALLLGGKAERASQG-----WGVGIHRYQLAAHAPWMSPAVTELTLLISHQDQVTALPEGATVIAS 164

                        170       180
                 ....*....|....*....|....
gi 15234763  172 SKNYEVEMYSIEDHLFCIQGHPEY 195
Cdd:PRK05665 165 SDFCPFAAYHIGDQVLCFQGHPEF 188
guaA_Nterm TIGR00888
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine ...
 87-200 5.58e-17

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: 76.20  E-value: 5.58e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234763    87 KKIDEMKKKILGICFGHQIIARVRGGTVGRAKKGpELKLGDITIVKDaitpGSYFGNeIPDSIAIIKCHQDEVLVLPETA 166
Cdd:TIGR00888  64 EKIFELGVPVLGICYGMQLMAKQLGGEVGRAEKR-EYGKAELEILDE----DDLFRG-LPDESTVWMSHGDKVKELPEGF 137

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 15234763   167 KVLAYSKNYEVEMYSIEDH-LFCIQGHPE-----YNKEIL 200
Cdd:TIGR00888 138 KVLATSDNCPVAAMAHEEKpIYGVQFHPEvthteYGNELL 177
GATase pfam00117
Glutamine amidotransferase class-I;
53-201 5.57e-10

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 56.86  E-value: 5.57e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234763    53 DEKDLEKYDGFVISGSshdaFENDDWILKLCDIVKKIDEMKKKILGICFGHQIIARVRGGTVGRAKKGPELKlGDITIVK 132
Cdd:pfam00117  34 EEILEENPDGIILSGG----PGSPGAAGGAIEAIREARELKIPILGICLGHQLLALAFGGKVVKAKKFGHHG-KNSPVGD 108

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15234763   133 DAitPGSYFGneIPDSIAIIKCHQDEV--LVLPETAKVLAYSKNYE--VEMYSIEDHLFCIQGHPE-----YNKEILF 201
Cdd:pfam00117 109 DG--CGLFYG--LPNVFIVRRYHSYAVdpDTLPDGLEVTATSENDGtiMGIRHKKLPIFGVQFHPEsiltpHGPEILF 182
 
Name Accession Description Interval E-value
GATase1_1 cd01741
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 35-194 1.65e-46

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: 153.17  E-value: 1.65e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234763  35 GDEGEHWDSFRVVSGEFPdeKDLEKYDGFVISGSSHDAFEND-DWILKLCDIVKKIDEMKKKILGICFGHQIIARVRGGT 113
Cdd:cd01741  24 GAETIEIDVVDVYAGELL--PDLDDYDGLVILGGPMSVDEDDyPWLKKLKELIRQALAAGKPVLGICLGHQLLARALGGK 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234763 114 VGRAKKGPELKLGDITIVKDAITPGSYFGneIPDSIAIIKCHQDEVLVLPETAKVLAYSKNYEVEMYSIEDHLFCIQGHP 193
Cdd:cd01741 102 VGRNPKGWEIGWFPVTLTEAGKADPLFAG--LPDEFPVFHWHGDTVVELPPGAVLLASSEACPNQAFRYGDRALGLQFHP 179


                .
gi 15234763 194 E 194
Cdd:cd01741 180 E 180
GuaA1 COG0518
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ...
 23-245 4.60e-46

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: 153.18  E-value: 4.60e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234763  23 YGGYHNVFVTTFGDEGEHWDSFRVVSGEF-PDEKDLEKYDGFVISGSSHDAFENDDWILKLCDIVKKIDEMKKKILGICF 101
Cdd:COG0518  11 GGQYPGLIARRLREAGIELDVLRVYAGEIlPYDPDLEDPDGLILSGGPMSVYDEDPWLEDEPALIREAFELGKPVLGICY 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234763 102 GHQIIARVRGGTVGRAkKGPELKLGDITIV-KDAITPGsyfgneIPDSIAIIKCHQDEVLVLPETAKVLAYSKNYEVEMY 180
Cdd:COG0518  91 GAQLLAHALGGKVEPG-PGREIGWAPVELTeADPLFAG------LPDEFTVWMSHGDTVTELPEGAEVLASSDNCPNQAF 163

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15234763 181 SIEDHLFCIQGHPEYNKeilfEIVDRVLALGYVKQEFADAAKATMENRGADRKLWETICKNFLKG 245
Cdd:COG0518 164 RYGRRVYGVQFHPEVTH----TMMEAWLEERADELAAEELLAEASLHDPELREAGRRLLRNFLRE 224
PRK05665 PRK05665
amidotransferase; Provisional
 14-195 1.86e-33

amidotransferase; Provisional


Pssm-ID: 168162 [Multi-domain]  Cd Length: 240  Bit Score: 121.07  E-value: 1.86e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234763   14 LDSEFVKKtYGGYHNVFVTTFGDEGEHW--DSFRVVSGEFPdeKDLEKYDGFVISGSSHDAFENDDWILKLCDIVKKIDE 91
Cdd:PRK05665  13 LRPELVAQ-YQGYGRMFEQLFARQPIAAefVVYNVVQGDYP--ADDEKFDAYLVTGSKADSFGTDPWIQTLKTYLLKLYE 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234763   92 MKKKILGICFGHQIIARVRGGTVGRAKKGpelklGDITIVKDAITPGSYFGNEIPDSIAIIKCHQDEVLVLPETAKVLAY 171
Cdd:PRK05665  90 RGDKLLGVCFGHQLLALLLGGKAERASQG-----WGVGIHRYQLAAHAPWMSPAVTELTLLISHQDQVTALPEGATVIAS 164

                        170       180
                 ....*....|....*....|....
gi 15234763  172 SKNYEVEMYSIEDHLFCIQGHPEY 195
Cdd:PRK05665 165 SDFCPFAAYHIGDQVLCFQGHPEF 188
GATase1_GMP_Synthase cd01742
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine ...
 46-194 3.21e-21

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: 87.21  E-value: 3.21e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234763  46 VVSGEFPDEKDLE-KYDGFVISGSSHDAFENDdwilkLCDIVKKIDEMKKKILGICFGHQIIARVRGGTVGRAKKGpELK 124
Cdd:cd01742  27 ILPNTTPLEEIKLkNPKGIILSGGPSSVYEED-----APRVDPEIFELGVPVLGICYGMQLIAKALGGKVERGDKR-EYG 100

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15234763 125 LGDITIVKDaitpGSYFGNeIPDSIAIIKCHQDEVLVLPETAKVLAYSKNYEVE-MYSIEDHLFCIQGHPE 194
Cdd:cd01742 101 KAEIEIDDS----SPLFEG-LPDEQTVWMSHGDEVVKLPEGFKVIASSDNCPVAaIANEEKKIYGVQFHPE 166
PRK00758 PRK00758
GMP synthase subunit A; Validated
 46-194 9.74e-21

GMP synthase subunit A; Validated


Pssm-ID: 179112 [Multi-domain]  Cd Length: 184  Bit Score: 86.06  E-value: 9.74e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234763   46 VVSGEFPDEKDLEKYDGFVISGSSHdafenddwILKLCDIVKKIDEMKKKILGICFGHQIIARVRGGTVGRAKKGpELKL 125
Cdd:PRK00758  28 IIPNTTPVEEIKAFEDGLILSGGPD--------IERAGNCPEYLKELDVPILGICLGHQLIAKAFGGEVGRGEYG-EYAL 98

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15234763  126 GDITIV-KDAITPGsyfgneIPDSIAIIKCHQDEVLVLPETAKVLAYSKNYEVE-MYSIEDHLFCIQGHPE 194
Cdd:PRK00758  99 VEVEILdEDDILKG------LPPEIRVWASHADEVKELPDGFEILARSDICEVEaMKHKEKPIYGVQFHPE 163
guaA_Nterm TIGR00888
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine ...
 87-200 5.58e-17

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: 76.20  E-value: 5.58e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234763    87 KKIDEMKKKILGICFGHQIIARVRGGTVGRAKKGpELKLGDITIVKDaitpGSYFGNeIPDSIAIIKCHQDEVLVLPETA 166
Cdd:TIGR00888  64 EKIFELGVPVLGICYGMQLMAKQLGGEVGRAEKR-EYGKAELEILDE----DDLFRG-LPDESTVWMSHGDKVKELPEGF 137

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 15234763   167 KVLAYSKNYEVEMYSIEDH-LFCIQGHPE-----YNKEIL 200
Cdd:TIGR00888 138 KVLATSDNCPVAAMAHEEKpIYGVQFHPEvthteYGNELL 177
PRK09065 PRK09065
glutamine amidotransferase; Provisional
 45-199 4.63e-13

glutamine amidotransferase; Provisional


Pssm-ID: 181635 [Multi-domain]  Cd Length: 237  Bit Score: 66.52  E-value: 4.63e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234763   45 RVVSGEFPDEKDLekYDGFVISGSSHDAFENDDWILKLCDIVKKIDEMKKKILGICFGHQIIARVRGGTVGRAKKGPElk 124
Cdd:PRK09065  42 RVFAGEPLPAPDD--FAGVIITGSWAMVTDRLDWSERTADWLRQAAAAGMPLLGICYGHQLLAHALGGEVGYNPAGRE-- 117

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15234763  125 LGDITIvkdAITPG----SYFGNeIPDSIAIIKCHQDEVLVLPETAKVLAYSKNYEVEMYSIEDHLFCIQGHPEYNKEI 199
Cdd:PRK09065 118 SGTVTV---ELHPAaaddPLFAG-LPAQFPAHLTHLQSVLRLPPGAVVLARSAQDPHQAFRYGPHAWGVQFHPEFTAHI 192
guaA PRK00074
GMP synthase; Reviewed
 46-200 1.01e-11

GMP synthase; Reviewed


Pssm-ID: 234614 [Multi-domain]  Cd Length: 511  Bit Score: 63.91  E-value: 1.01e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234763   46 VVSGEFPDEKDLEK-YDGFVISGS-----SHDAFENDDWILklcdivkkidEMKKKILGICFGHQIIARVRGGTVGRAKK 119
Cdd:PRK00074  32 IVPYDISAEEIRAFnPKGIILSGGpasvyEEGAPRADPEIF----------ELGVPVLGICYGMQLMAHQLGGKVERAGK 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234763  120 GpELKLGDITIVKDaitpgSYFGNEIPDSIAIIKCHQDEVLVLPETAKVLAYSKNYEVEMYSIED-HLFCIQGHPE---- 194
Cdd:PRK00074 102 R-EYGRAELEVDND-----SPLFKGLPEEQDVWMSHGDKVTELPEGFKVIASTENCPIAAIANEErKFYGVQFHPEvtht 175


                 ....*..
gi 15234763  195 -YNKEIL 200
Cdd:PRK00074 176 pQGKKLL 182
GATase pfam00117
Glutamine amidotransferase class-I;
53-201 5.57e-10

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 56.86  E-value: 5.57e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234763    53 DEKDLEKYDGFVISGSshdaFENDDWILKLCDIVKKIDEMKKKILGICFGHQIIARVRGGTVGRAKKGPELKlGDITIVK 132
Cdd:pfam00117  34 EEILEENPDGIILSGG----PGSPGAAGGAIEAIREARELKIPILGICLGHQLLALAFGGKVVKAKKFGHHG-KNSPVGD 108

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15234763   133 DAitPGSYFGneIPDSIAIIKCHQDEV--LVLPETAKVLAYSKNYE--VEMYSIEDHLFCIQGHPE-----YNKEILF 201
Cdd:pfam00117 109 DG--CGLFYG--LPNVFIVRRYHSYAVdpDTLPDGLEVTATSENDGtiMGIRHKKLPIFGVQFHPEsiltpHGPEILF 182
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 34-106 7.82e-10

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: 54.91  E-value: 7.82e-10
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15234763  34 FGDEGEHWDSFRVVSGEFPDEKDLEKYDGFVISGSSHDAFEnDDWILKLCDIVKKIDEMKKKILGICFGHQII 106
Cdd:cd01653  21 LREAGAEVDVVSPDGGPVESDVDLDDYDGLILPGGPGTPDD-LARDEALLALLREAAAAGKPILGICLGAQLL 92
PRK07567 PRK07567
glutamine amidotransferase; Provisional
 45-194 1.28e-09

glutamine amidotransferase; Provisional


Pssm-ID: 181035 [Multi-domain]  Cd Length: 242  Bit Score: 56.87  E-value: 1.28e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234763   45 RVVSGEFPDeKDLEKYDGFVISGS----SHDAFENDDW-------ILKLCDIVKKIDemkKKILGICFGHQIIARVRGGT 113
Cdd:PRK07567  38 RLDREPLPD-LDLDDYSGVIVGGSpfnvSDPAESKSPWqrrveaeLSGLLDEVVARD---FPFLGACYGVGTLGHHQGGV 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234763  114 VGRAKkgPElKLGDITI------VKDAITPGsyfgneIPDSIAIIKCHQDEVLVLPETAKVLAYSKNYEVEMYSIEDHLF 187
Cdd:PRK07567 114 VDRTY--GE-PVGAVTVsltdagRADPLLAG------LPDTFTAFVGHKEAVSALPPGAVLLATSPTCPVQMFRVGENVY 184


                 ....*..
gi 15234763  188 CIQGHPE 194
Cdd:PRK07567 185 ATQFHPE 191
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 30-106 2.53e-09

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: 52.97  E-value: 2.53e-09
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15234763  30 FVTTFGDEGEHWDSFRVVSGEFPDEKDLEKYDGFVISGSsHDAFENDDWILKLCDIVKKIDEMKKKILGICFGHQII 106
Cdd:cd03128  17 PLDALREAGAEVDVVSPDGGPVESDVDLDDYDGLILPGG-PGTPDDLAWDEALLALLREAAAAGKPVLGICLGAQLL 92
GATase1_Anthranilate_Synthase cd01743
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ...
 52-194 4.45e-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: 54.46  E-value: 4.45e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234763  52 PDEKDLEKYDGFVIS---GSSHDAfenddwiLKLCDIVKKIDEmKKKILGICFGHQIIARVRGGTVGRAKKGPELKLGDI 128
Cdd:cd01743  35 LEELELLNPDAIVISpgpGHPEDA-------GISLEIIRALAG-KVPILGVCLGHQAIAEAFGGKVVRAPEPMHGKTSEI 106

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15234763 129 TIVKDAITPGsyfgneIPDSIAIIKCHQdevLV-----LPETAKVLAYSKNYEVeMySIEDHLFCIQG---HPE 194
Cdd:cd01743 107 HHDGSGLFKG------LPQPFTVGRYHS---LVvdpdpLPDLLEVTASTEDGVI-M-ALRHRDLPIYGvqfHPE 169
PRK05670 PRK05670
anthranilate synthase component II; Provisional
 89-119 4.49e-08

anthranilate synthase component II; Provisional


Pssm-ID: 235552 [Multi-domain]  Cd Length: 189  Bit Score: 51.67  E-value: 4.49e-08
                         10        20        30
                 ....*....|....*....|....*....|...
gi 15234763   89 IDEMKKK--ILGICFGHQIIARVRGGTVGRAKK 119
Cdd:PRK05670  66 IREFAGKvpILGVCLGHQAIGEAFGGKVVRAKE 98
PabA COG0512
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ...
 53-194 7.54e-08

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


Pssm-ID: 440278 [Multi-domain]  Cd Length: 189  Bit Score: 50.81  E-value: 7.54e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234763  53 DEKDLE-----KYDGFVIS---GSSHDAfenddwiLKLCDIVKKIdEMKKKILGICFGHQIIARVRGGTVGRAKK---Gp 121
Cdd:COG0512  31 DEITLEeiealAPDGIVLSpgpGTPEEA-------GISLEVIRAF-AGKIPILGVCLGHQAIGEAFGGKVVRAPEpmhG- 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234763 122 elKLGDITIVKDAItpgsyFGNeIPDSIAIIKCHQdevLV-----LPETAKVLAYSKNYEVeMySIEdH----LFCIQGH 192
Cdd:COG0512 102 --KTSPITHDGSGL-----FAG-LPNPFTATRYHS---LVvdretLPDELEVTAWTEDGEI-M-GIR-HrelpIEGVQFH 167


                ..
gi 15234763 193 PE 194
Cdd:COG0512 168 PE 169
PLN02347 PLN02347
GMP synthetase
 96-194 1.72e-06

GMP synthetase


Pssm-ID: 215197 [Multi-domain]  Cd Length: 536  Bit Score: 48.53  E-value: 1.72e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234763   96 ILGICFGHQIIARVRGGTVGRAKKGpELKLGDITIVKDAitpgSYFGNE-IPDSIAIIKCHQDEVLVLPETAKVLAYSKN 174
Cdd:PLN02347  89 VLGICYGMQLIVQKLGGEVKPGEKQ-EYGRMEIRVVCGS----QLFGDLpSGETQTVWMSHGDEAVKLPEGFEVVAKSVQ 163

                         90       100
                 ....*....|....*....|.
gi 15234763  175 YEV-EMYSIEDHLFCIQGHPE 194
Cdd:PLN02347 164 GAVvAIENRERRIYGLQYHPE 184
GATase1_CPSase cd01744
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ...
 46-194 3.57e-06

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


Pssm-ID: 153215 [Multi-domain]  Cd Length: 178  Bit Score: 45.95  E-value: 3.57e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234763  46 VVSGEFPDEKDL-EKYDGFVIS---GSSHDAfendDWILKLcdiVKKIDEMKKKILGICFGHQIIARVRGGTVGRAKKG- 120
Cdd:cd01744  25 VVPYNTDAEEILkLDPDGIFLSngpGDPALL----DEAIKT---VRKLLGKKIPIFGICLGHQLLALALGAKTYKMKFGh 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234763 121 -----PelklgditiVKDAITpgsyfGN-EI----------PDSiaiikchqdevlvLPETAKVLAYSKN-YEVEMYSIE 183
Cdd:cd01744  98 rgsnhP---------VKDLIT-----GRvYItsqnhgyavdPDS-------------LPGGLEVTHVNLNdGTVEGIRHK 150

                       170
                ....*....|..
gi 15234763 184 DH-LFCIQGHPE 194
Cdd:cd01744 151 DLpVFSVQFHPE 162
PuuD COG2071
Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (putrescine degradation), contains ...
 54-223 1.47e-05

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: 44.77  E-value: 1.47e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234763  54 EKDLEKYDGFVISGS-----SH----------------DAFEnddwiLKLcdiVKKIDEMKKKILGICFGHQIIARVRGG 112
Cdd:COG2071  44 DELLDRLDGLVLTGGadvdpALygeephpelgpidperDAFE-----LAL---IRAALERGKPVLGICRGMQLLNVALGG 115

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234763 113 T--------VGRAKK--GPELKLGDITIVKdaITPGSYFGNEIPDSIAIIKC--HQ--DEvlvLPETAKVLAYSKNYEVE 178
Cdd:COG2071 116 TlyqdlpdqVPGALDhrQPAPRYAPRHTVE--IEPGSRLARILGEEEIRVNSlhHQavKR---LGPGLRVSARAPDGVIE 190

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 15234763 179 MYSIEDHLFCI--QGHPEYnkeiLFEIVDRVLALgyvKQEFADAAKA 223
Cdd:COG2071 191 AIESPGAPFVLgvQWHPEW----LAASDPLSRRL---FEAFVEAARA 230
PRK06490 PRK06490
glutamine amidotransferase; Provisional
 57-194 3.66e-05

glutamine amidotransferase; Provisional


Pssm-ID: 180590 [Multi-domain]  Cd Length: 239  Bit Score: 43.80  E-value: 3.66e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234763   57 LEKYDGFVISGSSHDAFENDDWILKLCD-IVKKIDEmKKKILGICFGHQIIARVRGGTV-----GRAKKG--Pelklgdi 128
Cdd:PRK06490  50 LEDHAGAVIFGGPMSANDPDDFIRREIDwISVPLKE-NKPFLGICLGAQMLARHLGARVaphpdGRVEIGyyP------- 121

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15234763  129 tivkdaITPGSYfGNEIPDSIAIIKCHQDEVLVLPETAKVLAYSKNYEVEMYSIEDHLFCIQGHPE 194
Cdd:PRK06490 122 ------LRPTEA-GRALMHWPEMVYHWHREGFDLPAGAELLATGDDFPNQAFRYGDNAWGLQFHPE 180
PRK14607 PRK14607
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;
96-194 9.28e-05

bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;


Pssm-ID: 237764 [Multi-domain]  Cd Length: 534  Bit Score: 43.17  E-value: 9.28e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234763   96 ILGICFGHQIIARVRGGTVGRAKKgpeLKLGDIT-IVKDaitpGSYFGNEIPDSIAIIKCHQdevLV-----LPETAKVL 169
Cdd:PRK14607  76 ILGVCLGHQAIGYAFGGKIVHAKR---ILHGKTSpIDHN----GKGLFRGIPNPTVATRYHS---LVveeasLPECLEVT 145

                         90       100
                 ....*....|....*....|....*.
gi 15234763  170 AYSKNYEVEMYSIEDH-LFCIQGHPE 194
Cdd:PRK14607 146 AKSDDGEIMGIRHKEHpIFGVQFHPE 171
PRK08857 PRK08857
aminodeoxychorismate/anthranilate synthase component II;
93-194 6.39e-04

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181566 [Multi-domain]  Cd Length: 193  Bit Score: 39.47  E-value: 6.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234763   93 KKKILGICFGHQIIARVRGGTVGRAKKGPELKLGDITIVKDAITPGsyfgneIPDSIAIIKCHQDEVL--VLPETAKVLA 170
Cdd:PRK08857  72 KLPILGVCLGHQAIAQVFGGQVVRARQVMHGKTSPIRHTGRSVFKG------LNNPLTVTRYHSLVVKndTLPECFELTA 145

                         90       100       110
                 ....*....|....*....|....*....|
gi 15234763  171 YSKNYEVEMYSIEDH------LFCIQGHPE 194
Cdd:PRK08857 146 WTELEDGSMDEIMGFqhktlpIEAVQFHPE 175
PRK07765 PRK07765
aminodeoxychorismate/anthranilate synthase component II;
84-131 6.63e-04

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181107 [Multi-domain]  Cd Length: 214  Bit Score: 39.65  E-value: 6.63e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 15234763   84 DIVKKIDEMKKKILGICFGHQIIARVRGGTVGRAkkgPELKLGDITIV 131
Cdd:PRK07765  67 DMVRACAAAGTPLLGVCLGHQAIGVAFGATVDRA---PELLHGKTSSV 111
PRK08007 PRK08007
aminodeoxychorismate synthase component 2;
96-209 7.71e-04

aminodeoxychorismate synthase component 2;


Pssm-ID: 181194 [Multi-domain]  Cd Length: 187  Bit Score: 39.51  E-value: 7.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234763   96 ILGICFGHQIIARVRGGTVGRAKKGPELKLGDITIVKDAITPGsyfgneIPDSIAIIKCHQDEV--LVLPETAKVLAYSK 173
Cdd:PRK08007  75 ILGVCLGHQAMAQAFGGKVVRAAKVMHGKTSPITHNGEGVFRG------LANPLTVTRYHSLVVepDSLPACFEVTAWSE 148

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 15234763  174 NYEVE-MYSIEDHLFCIQGHPEynkEILFEIVDRVLA 209
Cdd:PRK08007 149 TREIMgIRHRQWDLEGVQFHPE---SILSEQGHQLLA 182
PRK12564 PRK12564
carbamoyl-phosphate synthase small subunit;
84-112 7.76e-04

carbamoyl-phosphate synthase small subunit;


Pssm-ID: 237139 [Multi-domain]  Cd Length: 360  Bit Score: 40.06  E-value: 7.76e-04
                         10        20
                 ....*....|....*....|....*....
gi 15234763   84 DIVKKIDEMKKKILGICFGHQIIARVRGG 112
Cdd:PRK12564 239 EMIRELLEKKIPIFGICLGHQLLALALGA 267
trpG_papA TIGR00566
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This ...
 96-129 7.96e-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: 39.39  E-value: 7.96e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 15234763    96 ILGICFGHQIIARVRGGTVGRAKKGPELKLGDIT 129
Cdd:TIGR00566  75 ILGVCLGHQAMGQAFGGDVVRANTVMHGKTSEIE 108
CPSaseIIsmall TIGR01368
carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small ...
 46-112 1.24e-03

carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small chain of the glutamine-dependent form (EC 6.3.5.5) of carbamoyl phosphate synthase, CPSase II. The C-terminal domain has glutamine amidotransferase activity. Note that the sequence from the mammalian urea cycle form has lost the active site Cys, resulting in an ammonia-dependent form, CPSase I (EC 6.3.4.16). CPSases of pyrimidine biosynthesis, arginine biosynthesis, and the urea cycle may be encoded by one or by several genes, depending on the species. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]


Pssm-ID: 273580 [Multi-domain]  Cd Length: 357  Bit Score: 39.53  E-value: 1.24e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15234763    46 VVSGEFPDEKDLEKY-DGFVISGSSHDAFENDDWIlklcDIVKKIDEmKKKILGICFGHQIIARVRGG 112
Cdd:TIGR01368 199 VVPYDTDAEEIKKYNpDGIFLSNGPGDPAAVEPAI----ETIRKLLE-KIPIFGICLGHQLLALAFGA 261
GATase1_2 cd01745
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 52-195 2.57e-03

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


Pssm-ID: 153216 [Multi-domain]  Cd Length: 189  Bit Score: 37.94  E-value: 2.57e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234763  52 PDEKDLEKY----DGFVISGS-----SHDAFEN-----------DDWILKLcdiVKKIDEMKKKILGICFGHQIIARVRG 111
Cdd:cd01745  42 DDEEDLEQYlellDGLLLTGGgdvdpPLYGEEPhpelgpidperDAFELAL---LRAALERGKPILGICRGMQLLNVALG 118

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234763 112 GTVGRakkgpelklgDITIvkdaitpGSYfgneipdsiaiikcHQDEVLVLPETAKVLAYSKNYEVEMYSIEDHLFCI-- 189
Cdd:cd01745 119 GTLYQ----------DIRV-------NSL--------------HHQAIKRLADGLRVEARAPDGVIEAIESPDRPFVLgv 167


                ....*.
gi 15234763 190 QGHPEY 195
Cdd:cd01745 168 QWHPEW 173
CarA COG0505
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ...
 86-108 4.87e-03

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


Pssm-ID: 440271 [Multi-domain]  Cd Length: 361  Bit Score: 37.69  E-value: 4.87e-03
                        10        20
                ....*....|....*....|...
gi 15234763  86 VKKIDEMKKKILGICFGHQIIAR 108
Cdd:COG0505 240 IRELLGKGIPIFGICLGHQLLAL 262
carA CHL00197
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional
 53-120 5.04e-03

carbamoyl-phosphate synthase arginine-specific small subunit; Provisional


Pssm-ID: 214392 [Multi-domain]  Cd Length: 382  Bit Score: 37.85  E-value: 5.04e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234763   53 DEKDLEKY--DGFVISGSSHDAFENDDWILKlcdiVKKIDEMKKKILGICFGHQIIARVRGGTVGRAKKG 120
Cdd:CHL00197 225 PYQDILSYqpDGILLSNGPGDPSAIHYGIKT----VKKLLKYNIPIFGICMGHQILSLALEAKTFKLKFG 290
PRK07649 PRK07649
aminodeoxychorismate/anthranilate synthase component II;
96-205 6.75e-03

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181066 [Multi-domain]  Cd Length: 195  Bit Score: 36.71  E-value: 6.75e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234763   96 ILGICFGHQIIARVRGGTVGRAKKGPELKLGDITIVKDAITPGsyfgneIPDSIAIIKCHQDEVL--VLPETAKVLAYSK 173
Cdd:PRK07649  75 IFGVCLGHQSIAQVFGGEVVRAERLMHGKTSLMHHDGKTIFSD------IPNPFTATRYHSLIVKkeTLPDCLEVTSWTE 148

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 15234763  174 nyEVEMYSIEDHLFCIQG---HPE-----YNKEILFEIVD 205
Cdd:PRK07649 149 --EGEIMAIRHKTLPIEGvqfHPEsimtsHGKELLQNFIR 186
hisH PRK13143
imidazole glycerol phosphate synthase subunit HisH; Provisional
 53-105 7.22e-03

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237289 [Multi-domain]  Cd Length: 200  Bit Score: 36.38  E-value: 7.22e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 15234763   53 DEKDLEKYDGFVISG--SSHDAFENddwILKLCDIVKKIDEMKKKILGICFGHQI 105
Cdd:PRK13143  32 DPEEILDADGIVLPGvgAFGAAMEN---LSPLRDVILEAARSGKPFLGICLGMQL 83
GATase1_IGP_Synthase cd01748
Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate ...
 53-194 7.88e-03

Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate synthase (IGPS); Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate synthase (IGPS). IGPS incorporates ammonia derived from glutamine into N1-[(5'-phosphoribulosyl)-formimino]-5-aminoimidazole-4-carboxamide ribonucleotide (PRFAR) to form 5'-(5-aminoimidazole-4-carboxamide) ribonucleotide (AICAR) and imidazole glycerol phosphate (IGP). The glutamine amidotransferase domain generates the ammonia nucleophile which is channeled from the glutaminase active site to the PRFAR active site. IGPS belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site.


Pssm-ID: 153219 [Multi-domain]  Cd Length: 198  Bit Score: 36.32  E-value: 7.88e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234763  53 DEKDLEKYDGFVISG--SSHDAFENDDwILKLCDIVKKIDEMKKKILGICFGHQIIAR-------VRG-----GTVGRAK 118
Cdd:cd01748  30 DPEEILSADKLILPGvgAFGDAMANLR-ERGLIEALKEAIASGKPFLGICLGMQLLFEsseegggTKGlglipGKVVRFP 108

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234763 119 KGPELKL---G--DITIVKD-----AITPGS--YFgneipdsiaiikchqdeV----LVLPETAKVLAYSkNYEVEMYSI 182
Cdd:cd01748 109 ASEGLKVphmGwnQLEITKEsplfkGIPDGSyfYF-----------------VhsyyAPPDDPDYILATT-DYGGKFPAA 170

                       170
                ....*....|....
gi 15234763 183 --EDHLFCIQGHPE 194
Cdd:cd01748 171 veKDNIFGTQFHPE 184
 
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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