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Conserved domains on  [gi|15234767|ref|NP_194784|]
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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 ...
 27-198 2.15e-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: 170.89  E-value: 2.15e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234767  27 GGYFNVFVSTFGEEGEQWDLFRVIDGQFPdeNDLDKYDGFVISGSPHDAFGD-ADWIVKLCEVCQKLDHMKKKVLGICFG 105
Cdd:cd01741  13 PGLFEDLLREAGAETIEIDVVDVYAGELL--PDLDDYDGLVILGGPMSVDEDdYPWLKKLKELIRQALAAGKPVLGICLG 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234767 106 HQIITRVKGGKIGRALKGADMGLRSITIAKDNEKLRGYFGdveVPASLAIIKCHQDEVLELPESATLLASSEVCNVEMFS 185
Cdd:cd01741  91 HQLLARALGGKVGRNPKGWEIGWFPVTLTEAGKADPLFAG---LPDEFPVFHWHGDTVVELPPGAVLLASSEACPNQAFR 167

                       170
                ....*....|...
gi 15234767 186 IGDHFFCIQGHPE 198
Cdd:cd01741 168 YGDRALGLQFHPE 180
 
Name Accession Description Interval E-value
GATase1_1 cd01741
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 27-198 2.15e-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: 170.89  E-value: 2.15e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234767  27 GGYFNVFVSTFGEEGEQWDLFRVIDGQFPdeNDLDKYDGFVISGSPHDAFGD-ADWIVKLCEVCQKLDHMKKKVLGICFG 105
Cdd:cd01741  13 PGLFEDLLREAGAETIEIDVVDVYAGELL--PDLDDYDGLVILGGPMSVDEDdYPWLKKLKELIRQALAAGKPVLGICLG 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234767 106 HQIITRVKGGKIGRALKGADMGLRSITIAKDNEKLRGYFGdveVPASLAIIKCHQDEVLELPESATLLASSEVCNVEMFS 185
Cdd:cd01741  91 HQLLARALGGKVGRNPKGWEIGWFPVTLTEAGKADPLFAG---LPDEFPVFHWHGDTVVELPPGAVLLASSEACPNQAFR 167

                       170
                ....*....|...
gi 15234767 186 IGDHFFCIQGHPE 198
Cdd:cd01741 168 YGDRALGLQFHPE 180
GuaA1 COG0518
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ...
 37-249 2.40e-45

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: 151.25  E-value: 2.40e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234767  37 FGEEGEQWDLFRVIDGQF-PDENDLDKYDGFVISGSPHDAFGDADWIVKLCEVCQKLDHMKKKVLGICFGHQIITRVKGG 115
Cdd:COG0518  22 LREAGIELDVLRVYAGEIlPYDPDLEDPDGLILSGGPMSVYDEDPWLEDEPALIREAFELGKPVLGICYGAQLLAHALGG 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234767 116 KIGRAlKGADMGLRSITIAKDNEKLRGYFGDVEVPASlaiikcHQDEVLELPESATLLASSEVCNVEMFSIGDHFFCIQG 195
Cdd:COG0518 102 KVEPG-PGREIGWAPVELTEADPLFAGLPDEFTVWMS------HGDTVTELPEGAEVLASSDNCPNQAFRYGRRVYGVQF 174

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 15234767 196 HPEYNKEILFEIVDRVLNMKLMEQEFADkaksTMETAQPDRILWQKLCKNFLKG 249
Cdd:COG0518 175 HPEVTHTMMEAWLEERADELAAEELLAE----ASLHDPELREAGRRLLRNFLRE 224
PRK05665 PRK05665
amidotransferase; Provisional
 26-199 4.72e-38

amidotransferase; Provisional


Pssm-ID: 168162 [Multi-domain]  Cd Length: 240  Bit Score: 133.01  E-value: 4.72e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234767   26 YGGYFNVFVSTFGEEGEQWDL--FRVIDGQFPDENDldKYDGFVISGSPHDAFGDADWIVKLCEVCQKLDHMKKKVLGIC 103
Cdd:PRK05665  21 YQGYGRMFEQLFARQPIAAEFvvYNVVQGDYPADDE--KFDAYLVTGSKADSFGTDPWIQTLKTYLLKLYERGDKLLGVC 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234767  104 FGHQIITRVKGGKIGRALKGADMGLRSITIAKdneklRGYFGDVEVPaSLAIIKCHQDEVLELPESATLLASSEVCNVEM 183
Cdd:PRK05665  99 FGHQLLALLLGGKAERASQGWGVGIHRYQLAA-----HAPWMSPAVT-ELTLLISHQDQVTALPEGATVIASSDFCPFAA 172

                        170
                 ....*....|....*.
gi 15234767  184 FSIGDHFFCIQGHPEY 199
Cdd:PRK05665 173 YHIGDQVLCFQGHPEF 188
guaA_Nterm TIGR00888
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine ...
 65-204 4.42e-19

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: 81.98  E-value: 4.42e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234767    65 GFVISGSPHDAF-GDADwivklcEVCQKLDHMKKKVLGICFGHQIITRVKGGKIGRALKGaDMGLRSITIAKDNEKLRGY 143
Cdd:TIGR00888  44 GIILSGGPSSVYaENAP------RADEKIFELGVPVLGICYGMQLMAKQLGGEVGRAEKR-EYGKAELEILDEDDLFRGL 116

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15234767   144 FGDVEVPASlaiikcHQDEVLELPESATLLASSEVCNVEMFSIGDH-FFCIQGHPE-----YNKEIL 204
Cdd:TIGR00888 117 PDESTVWMS------HGDKVKELPEGFKVLATSDNCPVAAMAHEEKpIYGVQFHPEvthteYGNELL 177
GATase pfam00117
Glutamine amidotransferase class-I;
56-205 5.43e-09

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 54.17  E-value: 5.43e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234767    56 DENDLDKYDGFVISGSPhdafGDadwiVKLCEVC----QKLDHMKKKVLGICFGHQIITRVKGGKIGRALKGADMGLRSI 131
Cdd:pfam00117  34 EEILEENPDGIILSGGP----GS----PGAAGGAieaiREARELKIPILGICLGHQLLALAFGGKVVKAKKFGHHGKNSP 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234767   132 TIAKDNEKLRGyfgdveVPASLAIIKCHQDEVLE--LPESATLLASSE--VCNVEMFSIGDHFFCIQGHPE-----YNKE 202
Cdd:pfam00117 106 VGDDGCGLFYG------LPNVFIVRRYHSYAVDPdtLPDGLEVTATSEndGTIMGIRHKKLPIFGVQFHPEsiltpHGPE 179


                  ...
gi 15234767   203 ILF 205
Cdd:pfam00117 180 ILF 182
 
Name Accession Description Interval E-value
GATase1_1 cd01741
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 27-198 2.15e-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: 170.89  E-value: 2.15e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234767  27 GGYFNVFVSTFGEEGEQWDLFRVIDGQFPdeNDLDKYDGFVISGSPHDAFGD-ADWIVKLCEVCQKLDHMKKKVLGICFG 105
Cdd:cd01741  13 PGLFEDLLREAGAETIEIDVVDVYAGELL--PDLDDYDGLVILGGPMSVDEDdYPWLKKLKELIRQALAAGKPVLGICLG 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234767 106 HQIITRVKGGKIGRALKGADMGLRSITIAKDNEKLRGYFGdveVPASLAIIKCHQDEVLELPESATLLASSEVCNVEMFS 185
Cdd:cd01741  91 HQLLARALGGKVGRNPKGWEIGWFPVTLTEAGKADPLFAG---LPDEFPVFHWHGDTVVELPPGAVLLASSEACPNQAFR 167

                       170
                ....*....|...
gi 15234767 186 IGDHFFCIQGHPE 198
Cdd:cd01741 168 YGDRALGLQFHPE 180
GuaA1 COG0518
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ...
 37-249 2.40e-45

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: 151.25  E-value: 2.40e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234767  37 FGEEGEQWDLFRVIDGQF-PDENDLDKYDGFVISGSPHDAFGDADWIVKLCEVCQKLDHMKKKVLGICFGHQIITRVKGG 115
Cdd:COG0518  22 LREAGIELDVLRVYAGEIlPYDPDLEDPDGLILSGGPMSVYDEDPWLEDEPALIREAFELGKPVLGICYGAQLLAHALGG 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234767 116 KIGRAlKGADMGLRSITIAKDNEKLRGYFGDVEVPASlaiikcHQDEVLELPESATLLASSEVCNVEMFSIGDHFFCIQG 195
Cdd:COG0518 102 KVEPG-PGREIGWAPVELTEADPLFAGLPDEFTVWMS------HGDTVTELPEGAEVLASSDNCPNQAFRYGRRVYGVQF 174

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 15234767 196 HPEYNKEILFEIVDRVLNMKLMEQEFADkaksTMETAQPDRILWQKLCKNFLKG 249
Cdd:COG0518 175 HPEVTHTMMEAWLEERADELAAEELLAE----ASLHDPELREAGRRLLRNFLRE 224
PRK05665 PRK05665
amidotransferase; Provisional
 26-199 4.72e-38

amidotransferase; Provisional


Pssm-ID: 168162 [Multi-domain]  Cd Length: 240  Bit Score: 133.01  E-value: 4.72e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234767   26 YGGYFNVFVSTFGEEGEQWDL--FRVIDGQFPDENDldKYDGFVISGSPHDAFGDADWIVKLCEVCQKLDHMKKKVLGIC 103
Cdd:PRK05665  21 YQGYGRMFEQLFARQPIAAEFvvYNVVQGDYPADDE--KFDAYLVTGSKADSFGTDPWIQTLKTYLLKLYERGDKLLGVC 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234767  104 FGHQIITRVKGGKIGRALKGADMGLRSITIAKdneklRGYFGDVEVPaSLAIIKCHQDEVLELPESATLLASSEVCNVEM 183
Cdd:PRK05665  99 FGHQLLALLLGGKAERASQGWGVGIHRYQLAA-----HAPWMSPAVT-ELTLLISHQDQVTALPEGATVIASSDFCPFAA 172

                        170
                 ....*....|....*.
gi 15234767  184 FSIGDHFFCIQGHPEY 199
Cdd:PRK05665 173 YHIGDQVLCFQGHPEF 188
GATase1_GMP_Synthase cd01742
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine ...
 53-198 5.02e-23

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: 92.21  E-value: 5.02e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234767  53 QFPDENDLDKYDGFVISGSPHDAFGDadwivKLCEVCQKLDHMKKKVLGICFGHQIITRVKGGKIGRALKGADmGLRSIT 132
Cdd:cd01742  32 TPLEEIKLKNPKGIILSGGPSSVYEE-----DAPRVDPEIFELGVPVLGICYGMQLIAKALGGKVERGDKREY-GKAEIE 105

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15234767 133 IAKDNEKLRGYFGDVEVPASlaiikcHQDEVLELPESATLLASSEVCNVEMFSIGDH-FFCIQGHPE 198
Cdd:cd01742 106 IDDSSPLFEGLPDEQTVWMS------HGDEVVKLPEGFKVIASSDNCPVAAIANEEKkIYGVQFHPE 166
PRK00758 PRK00758
GMP synthase subunit A; Validated
 49-198 1.62e-20

GMP synthase subunit A; Validated


Pssm-ID: 179112 [Multi-domain]  Cd Length: 184  Bit Score: 85.67  E-value: 1.62e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234767   49 VIDGQFPDENDLDKYDGFVISGSPH-DAFGDADWIVKlcevcqkldHMKKKVLGICFGHQIITRVKGGKIGRALKGaDMG 127
Cdd:PRK00758  28 IIPNTTPVEEIKAFEDGLILSGGPDiERAGNCPEYLK---------ELDVPILGICLGHQLIAKAFGGEVGRGEYG-EYA 97

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15234767  128 LRSITIAKDNEKLRGYFGDVEVPASlaiikcHQDEVLELPESATLLASSEVCNVEMFSIGD-HFFCIQGHPE 198
Cdd:PRK00758  98 LVEVEILDEDDILKGLPPEIRVWAS------HADEVKELPDGFEILARSDICEVEAMKHKEkPIYGVQFHPE 163
guaA_Nterm TIGR00888
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine ...
 65-204 4.42e-19

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: 81.98  E-value: 4.42e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234767    65 GFVISGSPHDAF-GDADwivklcEVCQKLDHMKKKVLGICFGHQIITRVKGGKIGRALKGaDMGLRSITIAKDNEKLRGY 143
Cdd:TIGR00888  44 GIILSGGPSSVYaENAP------RADEKIFELGVPVLGICYGMQLMAKQLGGEVGRAEKR-EYGKAELEILDEDDLFRGL 116

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15234767   144 FGDVEVPASlaiikcHQDEVLELPESATLLASSEVCNVEMFSIGDH-FFCIQGHPE-----YNKEIL 204
Cdd:TIGR00888 117 PDESTVWMS------HGDKVKELPEGFKVLATSDNCPVAAMAHEEKpIYGVQFHPEvthteYGNELL 177
PRK09065 PRK09065
glutamine amidotransferase; Provisional
 26-203 5.44e-19

glutamine amidotransferase; Provisional


Pssm-ID: 181635 [Multi-domain]  Cd Length: 237  Bit Score: 82.70  E-value: 5.44e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234767   26 YGGYFNVFVSTFGEEGEQWDLFRVIDGQ-FPDENDldkYDGFVISGSPhdAF---------GDADWIVKLCEVCQKLdhm 95
Cdd:PRK09065  20 YGDFPHWIRVALGLAEQPVVVVRVFAGEpLPAPDD---FAGVIITGSW--AMvtdrldwseRTADWLRQAAAAGMPL--- 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234767   96 kkkvLGICFGHQIITRVKGGKIGRALKGADMGLRSITI---AKDNEKLRGYfgDVEVPASLAiikcHQDEVLELPESATL 172
Cdd:PRK09065  92 ----LGICYGHQLLAHALGGEVGYNPAGRESGTVTVELhpaAADDPLFAGL--PAQFPAHLT----HLQSVLRLPPGAVV 161

                        170       180       190
                 ....*....|....*....|....*....|.
gi 15234767  173 LASSEVCNVEMFSIGDHFFCIQGHPEYNKEI 203
Cdd:PRK09065 162 LARSAQDPHQAFRYGPHAWGVQFHPEFTAHI 192
PRK07567 PRK07567
glutamine amidotransferase; Provisional
 59-198 4.97e-13

glutamine amidotransferase; Provisional


Pssm-ID: 181035 [Multi-domain]  Cd Length: 242  Bit Score: 66.50  E-value: 4.97e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234767   59 DLDKYDGFVISGSPHDAFGDAD-----------WIVKLCEVCQKLDHmkkKVLGICFGHQIITRVKGGKIGRAlKGADMG 127
Cdd:PRK07567  48 DLDDYSGVIVGGSPFNVSDPAEskspwqrrveaELSGLLDEVVARDF---PFLGACYGVGTLGHHQGGVVDRT-YGEPVG 123

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15234767  128 LRSITIAKDNEK---LRGyfgdveVPASLAIIKCHQDEVLELPESATLLASSEVCNVEMFSIGDHFFCIQGHPE 198
Cdd:PRK07567 124 AVTVSLTDAGRAdplLAG------LPDTFTAFVGHKEAVSALPPGAVLLATSPTCPVQMFRVGENVYATQFHPE 191
guaA PRK00074
GMP synthase; Reviewed
 65-204 3.77e-12

GMP synthase; Reviewed


Pssm-ID: 234614 [Multi-domain]  Cd Length: 511  Bit Score: 65.45  E-value: 3.77e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234767   65 GFVISGSPH-----DAFGDADWIVKLcevcqkldhmKKKVLGICFGHQIITRVKGGKIGRALKGaDMGLRSITIAKDNEK 139
Cdd:PRK00074  49 GIILSGGPAsvyeeGAPRADPEIFEL----------GVPVLGICYGMQLMAHQLGGKVERAGKR-EYGRAELEVDNDSPL 117

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15234767  140 LRGYFGDVEVPASlaiikcHQDEVLELPESATLLASSEVCNVEMFSIGD-HFFCIQGHPE-----YNKEIL 204
Cdd:PRK00074 118 FKGLPEEQDVWMS------HGDKVTELPEGFKVIASTENCPIAAIANEErKFYGVQFHPEvthtpQGKKLL 182
PRK07053 PRK07053
glutamine amidotransferase; Provisional
 32-198 9.50e-12

glutamine amidotransferase; Provisional


Pssm-ID: 235919 [Multi-domain]  Cd Length: 234  Bit Score: 62.65  E-value: 9.50e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234767   32 VFVSTFGEEGEQWDLFRVIDGQFPDEnDLDKYDGFVISGSPHDAFGDAD--WIVKLCE-VCQKLDHmKKKVLGICFGHQI 108
Cdd:PRK07053  18 SFEQVLGARGYRVRYVDVGVDDLETL-DALEPDLLVVLGGPIGVYDDELypFLAPEIAlLRQRLAA-GLPTLGICLGAQL 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234767  109 ITRVKGGKIgralkgADMGLRSI-------TIAKDNEKLRGYFGDVEVpaslaiIKCHQDEvLELPESATLLASSEVCNV 181
Cdd:PRK07053  96 IARALGARV------YPGGQKEIgwapltlTDAGRASPLRHLGAGTPV------LHWHGDT-FDLPEGATLLASTPACRH 162

                        170
                 ....*....|....*..
gi 15234767  182 EMFSIGDHFFCIQGHPE 198
Cdd:PRK07053 163 QAFAWGNHVLALQFHPE 179
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 37-109 8.56e-11

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


Pssm-ID: 153210 [Multi-domain]  Cd Length: 115  Bit Score: 57.61  E-value: 8.56e-11
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15234767  37 FGEEGEQWDLFRVIDGQFPDENDLDKYDGFVISGSPHDAFgDADWIVKLCEVCQKLDHMKKKVLGICFGHQII 109
Cdd:cd01653  21 LREAGAEVDVVSPDGGPVESDVDLDDYDGLILPGGPGTPD-DLARDEALLALLREAAAAGKPILGICLGAQLL 92
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 33-109 3.39e-10

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: 55.28  E-value: 3.39e-10
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15234767  33 FVSTFGEEGEQWDLFRVIDGQFPDENDLDKYDGFVISGSPHDAFgDADWIVKLCEVCQKLDHMKKKVLGICFGHQII 109
Cdd:cd03128  17 PLDALREAGAEVDVVSPDGGPVESDVDLDDYDGLILPGGPGTPD-DLAWDEALLALLREAAAAGKPVLGICLGAQLL 92
GATase pfam00117
Glutamine amidotransferase class-I;
56-205 5.43e-09

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 54.17  E-value: 5.43e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234767    56 DENDLDKYDGFVISGSPhdafGDadwiVKLCEVC----QKLDHMKKKVLGICFGHQIITRVKGGKIGRALKGADMGLRSI 131
Cdd:pfam00117  34 EEILEENPDGIILSGGP----GS----PGAAGGAieaiREARELKIPILGICLGHQLLALAFGGKVVKAKKFGHHGKNSP 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234767   132 TIAKDNEKLRGyfgdveVPASLAIIKCHQDEVLE--LPESATLLASSE--VCNVEMFSIGDHFFCIQGHPE-----YNKE 202
Cdd:pfam00117 106 VGDDGCGLFYG------LPNVFIVRRYHSYAVDPdtLPDGLEVTATSEndGTIMGIRHKKLPIFGVQFHPEsiltpHGPE 179


                  ...
gi 15234767   203 ILF 205
Cdd:pfam00117 180 ILF 182
GATase1_Anthranilate_Synthase cd01743
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ...
 37-198 1.24e-08

Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase (ASase). This group contains proteins similar to para-aminobenzoate (PABA) synthase and ASase. These enzymes catalyze similar reactions and produce similar products, PABA and ortho-aminobenzoate (anthranilate). Each enzyme is composed of non-identical subunits: a glutamine amidotransferase subunit (component II) and a subunit that produces an aminobenzoate products (component I). ASase catalyses the synthesis of anthranilate from chorismate and glutamine and is a tetrameric protein comprising two copies each of components I and II. Component II of ASase belongs to the family of triad GTases which hydrolyze glutamine and transfer nascent ammonia between the active sites. In some bacteria, such as Escherichia coli, component II can be much larger than in other organisms, due to the presence of phosphoribosyl-anthranilate transferase (PRTase) activity. PRTase catalyses the second step in tryptophan biosynthesis and results in the addition of 5-phosphoribosyl-1-pyrophosphate to anthranilate to create N-5'-phosphoribosyl-anthranilate. In E.coli, the first step in the conversion of chorismate to PABA involves two proteins: PabA and PabB which co-operate to transfer the amide nitrogen of glutamine to chorismate forming 4-amino-4 deoxychorismate (ADC). PabA acts as a glutamine amidotransferase, supplying an amino group to PabB, which carries out the amination reaction. A third protein PabC then mediates elimination of pyruvate and aromatization to give PABA. Several organisms have bipartite proteins containing fused domains homologous to PabA and PabB commonly called PABA synthases. These hybrid PABA synthases may produce ADC and not PABA.


Pssm-ID: 153214 [Multi-domain]  Cd Length: 184  Bit Score: 53.31  E-value: 1.24e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234767  37 FGEEGEQWDLFRvIDGQFPDENDLDKYDGFVIS---GSPHDAfGDADWIVKlcevcqkldHMKKKV--LGICFGHQIITR 111
Cdd:cd01743  18 LRELGAEVVVVR-NDEITLEELELLNPDAIVISpgpGHPEDA-GISLEIIR---------ALAGKVpiLGVCLGHQAIAE 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234767 112 VKGGKIGRALKGadMGLRSITIAKDNEKLrgyFGDVEVPA------SLAIIKchqdevLELPESATLLASSEvCNVEMfS 185
Cdd:cd01743  87 AFGGKVVRAPEP--MHGKTSEIHHDGSGL---FKGLPQPFtvgryhSLVVDP------DPLPDLLEVTASTE-DGVIM-A 153

                       170
                ....*....|....*.
gi 15234767 186 I---GDHFFCIQGHPE 198
Cdd:cd01743 154 LrhrDLPIYGVQFHPE 169
PRK05670 PRK05670
anthranilate synthase component II; Provisional
 37-120 2.84e-08

anthranilate synthase component II; Provisional


Pssm-ID: 235552 [Multi-domain]  Cd Length: 189  Bit Score: 52.05  E-value: 2.84e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234767   37 FGEEGEQWDLFRvidgqfPDENDLD-----KYDGFVIS---GSPHDAfgdadwivklcEVCQKL-DHMKKKV--LGICFG 105
Cdd:PRK05670  19 LGELGAEVVVYR------NDEITLEeiealNPDAIVLSpgpGTPAEA-----------GISLELiREFAGKVpiLGVCLG 81

                         90
                 ....*....|....*
gi 15234767  106 HQIITRVKGGKIGRA 120
Cdd:PRK05670  82 HQAIGEAFGGKVVRA 96
PLN02347 PLN02347
GMP synthetase
 99-228 3.15e-08

GMP synthetase


Pssm-ID: 215197 [Multi-domain]  Cd Length: 536  Bit Score: 53.53  E-value: 3.15e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234767   99 VLGICFGHQIITRVKGGKIGRALKGaDMGLRSITIAKDNeklrGYFGDVEVPASLAIIKCHQDEVLELPESATLLASSEV 178
Cdd:PLN02347  89 VLGICYGMQLIVQKLGGEVKPGEKQ-EYGRMEIRVVCGS----QLFGDLPSGETQTVWMSHGDEAVKLPEGFEVVAKSVQ 163

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15234767  179 CNV-EMFSIGDHFFCIQGHPEYN---------KEILFEI--VDRVLNMKLMEQEFADKAKST 228
Cdd:PLN02347 164 GAVvAIENRERRIYGLQYHPEVThspkgmetlRHFLFDVcgVTADWKMQDVLEEQIELIKAT 225
PabA COG0512
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ...
 56-120 1.06e-07

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: 50.42  E-value: 1.06e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15234767  56 DENDLD-----KYDGFVIS---GSPHDAfGDADWIVKLCevcqkldHMKKKVLGICFGHQIITRVKGGKIGRA 120
Cdd:COG0512  31 DEITLEeiealAPDGIVLSpgpGTPEEA-GISLEVIRAF-------AGKIPILGVCLGHQAIGEAFGGKVVRA 95
PRK06490 PRK06490
glutamine amidotransferase; Provisional
 39-198 3.78e-07

glutamine amidotransferase; Provisional


Pssm-ID: 180590 [Multi-domain]  Cd Length: 239  Bit Score: 49.57  E-value: 3.78e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234767   39 EEGEQWDLFRVIDGQfPDENDLDKYDGFVISGSP-----HDAF--GDADWI-VKLCEvcqkldhmKKKVLGICFGHQIIT 110
Cdd:PRK06490  30 ERGYPLDIRRPRLGD-PLPDTLEDHAGAVIFGGPmsandPDDFirREIDWIsVPLKE--------NKPFLGICLGAQMLA 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234767  111 RVKGGKIgralKGADMGLRSItiakdneklrGYFGDVEVPASLAIIKCHQ------DEVLELPESATLLASSEVCNVEMF 184
Cdd:PRK06490 101 RHLGARV----APHPDGRVEI----------GYYPLRPTEAGRALMHWPEmvyhwhREGFDLPAGAELLATGDDFPNQAF 166

                        170
                 ....*....|....
gi 15234767  185 SIGDHFFCIQGHPE 198
Cdd:PRK06490 167 RYGDNAWGLQFHPE 180
GATase1_CPSase cd01744
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ...
 61-117 2.49e-05

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: 43.64  E-value: 2.49e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15234767  61 DKYDGFVISGSPHDAfGDADWIVKLC-EVCQKldhmKKKVLGICFGHQIITRVKGGKI 117
Cdd:cd01744  38 LDPDGIFLSNGPGDP-ALLDEAIKTVrKLLGK----KIPIFGICLGHQLLALALGAKT 90
PRK12564 PRK12564
carbamoyl-phosphate synthase small subunit;
62-117 5.04e-03

carbamoyl-phosphate synthase small subunit;


Pssm-ID: 237139 [Multi-domain]  Cd Length: 360  Bit Score: 37.75  E-value: 5.04e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 15234767   62 KYDGFVIS---GSPHDAfgdaDWIVklcEVCQKLDHMKKKVLGICFGHQIITRVKGGKI 117
Cdd:PRK12564 218 NPDGVFLSngpGDPAAL----DYAI---EMIRELLEKKIPIFGICLGHQLLALALGAKT 269
CPSaseIIsmall TIGR01368
carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small ...
 56-116 5.66e-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: 37.61  E-value: 5.66e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15234767    56 DENDLDKY--DGFVISGSPhdafGDADWIVKLCEVCQKLdhMKKK-VLGICFGHQIITRVKGGK 116
Cdd:TIGR01368 205 DAEEIKKYnpDGIFLSNGP----GDPAAVEPAIETIRKL--LEKIpIFGICLGHQLLALAFGAK 262
 
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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