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Conserved domains on  [gi|1370459295|ref|XP_024304258|]
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glutamine amidotransferase-like class 1 domain-containing protein 1 isoform X1 [Homo sapiens]

Protein Classification

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

type 1 glutamine amidotransferase (GATase1) family protein

CATH:  3.40.50.880
PubMed:  10387030
SCOP:  3001405

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GAT_1 super family cl00020
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 12-184 5.20e-46

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


The actual alignment was detected with superfamily member cd03141:

Pssm-ID: 469582 [Multi-domain]  Cd Length: 221  Bit Score: 152.33  E-value: 5.20e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459295  12 CLLVASGAAE-----------GVSAQSFLHCFTMAStaFNLQVATPGGK--AMEFVDVT-ESNARWVQDFRL----KAYA 73
Cdd:cd03141     1 ILIVLTSADKlggtgrptglwLEELAHPYDVFTEAG--YEVDFASPKGGkvPLDPRSLDaEDDDDASVFDNDeefkKKLA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459295  74 SPAKLESIDGARYHALLIPSCPGALTDLASSGSLARILQHFHSESKPICAVGHGVAALCCATNEDRSWVFDSYSLTGPSV 153
Cdd:cd03141    79 NTKKLSDVDPSDYDAIFIPGGHGPMFDLPDNPDLQDLLREFYENGKVVAAVCHGPAALLNVKLSDGKSLVAGKTVTGFTN 158

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1370459295 154 CELVRAPGFARLPLVVEDFVKDSGACF-SGEP 184
Cdd:cd03141   159 EEEEAAGLKKVVPFLLEDELKELGANYvKAEP 190
 
Name Accession Description Interval E-value
GATase1_Hsp31_like cd03141
Type 1 glutamine amidotransferase (GATase1)-like domain found in proteins similar to ...
 12-184 5.20e-46

Type 1 glutamine amidotransferase (GATase1)-like domain found in proteins similar to Escherichia coli Hsp31 protein; Type 1 glutamine amidotransferase (GATase1)-like domain found in proteins similar to Escherichia coli Hsp31 protein (EcHsp31). This group includes EcHsp31 and Saccharomyces cerevisiae Ydr533c protein. EcHsp31 has chaperone activity. Ydr533c is upregulated in response to various stress conditions along with the heat shock family. EcHsp31 coordinates a metal ion using a 2-His-1-carboxylate motif present in various ions that use iron as a cofactor such as Carboxypeptidase A. The catalytic triad typical of GATase1 domains is not conserved in this GATase1-like domain. However, in common with a typical GATase1 domain, a reactive Cys residue is found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For EcHsp31, this Cys together with a different His and, an Asp (rather than a Glu) residue form a different catalytic triad from the typical GATase1 domain. For Ydr533c a catalytic triad forms from the conserved Cys together with a different His and Glu from that of the typical GATase1domain. Ydr533c protein and EcHsp31 are homodimers.


Pssm-ID: 153235 [Multi-domain]  Cd Length: 221  Bit Score: 152.33  E-value: 5.20e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459295  12 CLLVASGAAE-----------GVSAQSFLHCFTMAStaFNLQVATPGGK--AMEFVDVT-ESNARWVQDFRL----KAYA 73
Cdd:cd03141     1 ILIVLTSADKlggtgrptglwLEELAHPYDVFTEAG--YEVDFASPKGGkvPLDPRSLDaEDDDDASVFDNDeefkKKLA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459295  74 SPAKLESIDGARYHALLIPSCPGALTDLASSGSLARILQHFHSESKPICAVGHGVAALCCATNEDRSWVFDSYSLTGPSV 153
Cdd:cd03141    79 NTKKLSDVDPSDYDAIFIPGGHGPMFDLPDNPDLQDLLREFYENGKVVAAVCHGPAALLNVKLSDGKSLVAGKTVTGFTN 158

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1370459295 154 CELVRAPGFARLPLVVEDFVKDSGACF-SGEP 184
Cdd:cd03141   159 EEEEAAGLKKVVPFLLEDELKELGANYvKAEP 190
YajL COG0693
Protein/nucleotide deglycase, PfpI/YajL/DJ-1 family (repair of methylglyoxal-glycated proteins ...
 43-184 1.94e-09

Protein/nucleotide deglycase, PfpI/YajL/DJ-1 family (repair of methylglyoxal-glycated proteins and nucleic acids) [Defense mechanisms];


Pssm-ID: 440457 [Multi-domain]  Cd Length: 170  Bit Score: 54.72  E-value: 1.94e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459295  43 VATPGGKAMefvdVTESNARWVQdfrlkayaSPAKLESIDGARYHALLIPSCPGALTDLASSGSLARILQHFHSESKPIC 122
Cdd:COG0693    34 VASPEGGPP----VTSKHGITVT--------ADKTLDDVDPDDYDALVLPGGHGAPDDLREDPDVVALVREFYEAGKPVA 101

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370459295 123 AVGHGVAALCcatnedRSWVFDSYSLTG-PSvcelvrapgfarlplvVEDFVKDSGACFSGEP 184
Cdd:COG0693   102 AICHGPAVLA------AAGLLKGRKVTSfPN----------------IEDDLKNAGATYVDEE 142
PRK04155 PRK04155
protein deglycase HchA;
39-148 2.45e-04

protein deglycase HchA;


Pssm-ID: 235228 [Multi-domain]  Cd Length: 287  Bit Score: 41.14  E-value: 2.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459295  39 FNLQVATPGGK-------AMEFVD--VTESNARWVQDFRlkayaSPAKLESI------DGARYHALLIPSCPGALTDLAS 103
Cdd:PRK04155   91 FEFDVATLSGNpvkfeywAMPHEDeaVMGFYEKYKSKFK-----QPKKLADVvanllaPDSDYAAVFIPGGHGALIGLPE 165

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1370459295 104 SGSLARILQHFHSESKPICAVGHGVAALCCATNEDRSWVFDSYSL 148
Cdd:PRK04155  166 SEDVAAALQWALDNDRFIITLCHGPAALLAAGVDHGDNPLNGYSI 210
 
Name Accession Description Interval E-value
GATase1_Hsp31_like cd03141
Type 1 glutamine amidotransferase (GATase1)-like domain found in proteins similar to ...
 12-184 5.20e-46

Type 1 glutamine amidotransferase (GATase1)-like domain found in proteins similar to Escherichia coli Hsp31 protein; Type 1 glutamine amidotransferase (GATase1)-like domain found in proteins similar to Escherichia coli Hsp31 protein (EcHsp31). This group includes EcHsp31 and Saccharomyces cerevisiae Ydr533c protein. EcHsp31 has chaperone activity. Ydr533c is upregulated in response to various stress conditions along with the heat shock family. EcHsp31 coordinates a metal ion using a 2-His-1-carboxylate motif present in various ions that use iron as a cofactor such as Carboxypeptidase A. The catalytic triad typical of GATase1 domains is not conserved in this GATase1-like domain. However, in common with a typical GATase1 domain, a reactive Cys residue is found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For EcHsp31, this Cys together with a different His and, an Asp (rather than a Glu) residue form a different catalytic triad from the typical GATase1 domain. For Ydr533c a catalytic triad forms from the conserved Cys together with a different His and Glu from that of the typical GATase1domain. Ydr533c protein and EcHsp31 are homodimers.


Pssm-ID: 153235 [Multi-domain]  Cd Length: 221  Bit Score: 152.33  E-value: 5.20e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459295  12 CLLVASGAAE-----------GVSAQSFLHCFTMAStaFNLQVATPGGK--AMEFVDVT-ESNARWVQDFRL----KAYA 73
Cdd:cd03141     1 ILIVLTSADKlggtgrptglwLEELAHPYDVFTEAG--YEVDFASPKGGkvPLDPRSLDaEDDDDASVFDNDeefkKKLA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459295  74 SPAKLESIDGARYHALLIPSCPGALTDLASSGSLARILQHFHSESKPICAVGHGVAALCCATNEDRSWVFDSYSLTGPSV 153
Cdd:cd03141    79 NTKKLSDVDPSDYDAIFIPGGHGPMFDLPDNPDLQDLLREFYENGKVVAAVCHGPAALLNVKLSDGKSLVAGKTVTGFTN 158

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1370459295 154 CELVRAPGFARLPLVVEDFVKDSGACF-SGEP 184
Cdd:cd03141   159 EEEEAAGLKKVVPFLLEDELKELGANYvKAEP 190
YajL COG0693
Protein/nucleotide deglycase, PfpI/YajL/DJ-1 family (repair of methylglyoxal-glycated proteins ...
 43-184 1.94e-09

Protein/nucleotide deglycase, PfpI/YajL/DJ-1 family (repair of methylglyoxal-glycated proteins and nucleic acids) [Defense mechanisms];


Pssm-ID: 440457 [Multi-domain]  Cd Length: 170  Bit Score: 54.72  E-value: 1.94e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459295  43 VATPGGKAMefvdVTESNARWVQdfrlkayaSPAKLESIDGARYHALLIPSCPGALTDLASSGSLARILQHFHSESKPIC 122
Cdd:COG0693    34 VASPEGGPP----VTSKHGITVT--------ADKTLDDVDPDDYDALVLPGGHGAPDDLREDPDVVALVREFYEAGKPVA 101

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370459295 123 AVGHGVAALCcatnedRSWVFDSYSLTG-PSvcelvrapgfarlplvVEDFVKDSGACFSGEP 184
Cdd:COG0693   102 AICHGPAVLA------AAGLLKGRKVTSfPN----------------IEDDLKNAGATYVDEE 142
PRK04155 PRK04155
protein deglycase HchA;
39-148 2.45e-04

protein deglycase HchA;


Pssm-ID: 235228 [Multi-domain]  Cd Length: 287  Bit Score: 41.14  E-value: 2.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459295  39 FNLQVATPGGK-------AMEFVD--VTESNARWVQDFRlkayaSPAKLESI------DGARYHALLIPSCPGALTDLAS 103
Cdd:PRK04155   91 FEFDVATLSGNpvkfeywAMPHEDeaVMGFYEKYKSKFK-----QPKKLADVvanllaPDSDYAAVFIPGGHGALIGLPE 165

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1370459295 104 SGSLARILQHFHSESKPICAVGHGVAALCCATNEDRSWVFDSYSL 148
Cdd:PRK04155  166 SEDVAAALQWALDNDRFIITLCHGPAALLAAGVDHGDNPLNGYSI 210
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 43-131 2.65e-04

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: 39.50  E-value: 2.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459295  43 VATPGGKAMEFVDVTESNARWVQDFRLKAYASPAKLESIDGARYHALLIPSCPGALTDLASSGSLARILQHFHSESKPIC 122
Cdd:cd01653     4 LLFPGFEELELASPLDALREAGAEVDVVSPDGGPVESDVDLDDYDGLILPGGPGTPDDLARDEALLALLREAAAAGKPIL 83


                  ....*....
gi 1370459295 123 AVGHGVAAL 131
Cdd:cd01653    84 GICLGAQLL 92
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 43-131 5.03e-04

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: 37.95  E-value: 5.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459295  43 VATPGGKAMEFVDVTESNARWVQDFRLKAYASPAKLESIDGARYHALLIPSCPGALTDLASSGSLARILQHFHSESKPIC 122
Cdd:cd03128     4 LLFGGSEELELASPLDALREAGAEVDVVSPDGGPVESDVDLDDYDGLILPGGPGTPDDLAWDEALLALLREAAAAGKPVL 83


                  ....*....
gi 1370459295 123 AVGHGVAAL 131
Cdd:cd03128    84 GICLGAQLL 92
GATase1_PfpI_1 cd03169
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ...
 39-134 6.03e-04

Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins similar to PfpI from Pyrococcus furiosus; Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins similar to PfpI from Pyrococcus furiosus. PfpI is an ATP-independent intracellular proteases which may hydrolyze small peptides to provide a nutritional source. Only Cys of the catalytic triad typical of GATase1 domains is conserved in this group. This Cys residue is found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow.


Pssm-ID: 153243 [Multi-domain]  Cd Length: 180  Bit Score: 39.17  E-value: 6.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459295  39 FNLQVATPGGKAMEFVdVTEsnarwVQDF------------RLKAYASPAKlesIDGARYHALLIPScpGALTD-LASSG 105
Cdd:cd03169    27 HEVDVVAPGKKKGDTV-VTA-----IHDFpgwqtytekpghRFAVTADFDE---VDPDDYDALVIPG--GRAPEyLRLDE 95

                          90       100
                  ....*....|....*....|....*....
gi 1370459295 106 SLARILQHFHSESKPICAVGHGVAALCCA 134
Cdd:cd03169    96 KVLAIVRHFAEANKPVAAICHGPQILAAA 124
 
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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