MULTISPECIES: protein deglycase HchA [Acinetobacter]
Protein Classification
protein deglycase HchA( domain architecture ID 10792339)
protein deglycase HchA deglycates cysteine, arginine and lysine residues in proteins, reactivating these proteins by reversing glycation by methylglyoxals or glyoxals and releasing lactate or glycolate, respectively
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||
| PRK04155 | PRK04155 | protein deglycase HchA; |
2-291 | 0e+00 | |||||
protein deglycase HchA; : Pssm-ID: 235228 [Multi-domain] Cd Length: 287 Bit Score: 568.09 E-value: 0e+00
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| Name | Accession | Description | Interval | E-value | |||||
| PRK04155 | PRK04155 | protein deglycase HchA; |
2-291 | 0e+00 | |||||
protein deglycase HchA; Pssm-ID: 235228 [Multi-domain] Cd Length: 287 Bit Score: 568.09 E-value: 0e+00
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| GATase1_EcHsp31_like | cd03148 | Type 1 glutamine amidotransferase (GATase1)-like domain found in Escherichia coli Hsp31 ... |
53-286 | 9.46e-125 | |||||
Type 1 glutamine amidotransferase (GATase1)-like domain found in Escherichia coli Hsp31 protein (EcHsp31); Type 1 glutamine amidotransferase (GATase1)-like domain found in Escherichia coli Hsp31 protein (EcHsp31). This group includes proteins similar to EcHsp31. EcHsp31 has chaperone activity. 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 GATase1domain, a reactive Cys residue is found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. 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. EcHsp31 is a homodimer. Pssm-ID: 153242 [Multi-domain] Cd Length: 232 Bit Score: 355.33 E-value: 9.46e-125
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| YajL | COG0693 | Protein/nucleotide deglycase, PfpI/YajL/DJ-1 family (repair of methylglyoxal-glycated proteins ... |
50-285 | 6.25e-27 | |||||
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: 103.26 E-value: 6.25e-27
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| DJ-1_PfpI | pfam01965 | DJ-1/PfpI family; The family includes the protease PfpI. This domain is also found in ... |
51-199 | 8.73e-07 | |||||
DJ-1/PfpI family; The family includes the protease PfpI. This domain is also found in transcriptional regulators. Pssm-ID: 396514 [Multi-domain] Cd Length: 165 Bit Score: 48.02 E-value: 8.73e-07
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| Name | Accession | Description | Interval | E-value | |||||
| PRK04155 | PRK04155 | protein deglycase HchA; |
2-291 | 0e+00 | |||||
protein deglycase HchA; Pssm-ID: 235228 [Multi-domain] Cd Length: 287 Bit Score: 568.09 E-value: 0e+00
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| GATase1_EcHsp31_like | cd03148 | Type 1 glutamine amidotransferase (GATase1)-like domain found in Escherichia coli Hsp31 ... |
53-286 | 9.46e-125 | |||||
Type 1 glutamine amidotransferase (GATase1)-like domain found in Escherichia coli Hsp31 protein (EcHsp31); Type 1 glutamine amidotransferase (GATase1)-like domain found in Escherichia coli Hsp31 protein (EcHsp31). This group includes proteins similar to EcHsp31. EcHsp31 has chaperone activity. 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 GATase1domain, a reactive Cys residue is found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. 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. EcHsp31 is a homodimer. Pssm-ID: 153242 [Multi-domain] Cd Length: 232 Bit Score: 355.33 E-value: 9.46e-125
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| GATase1_Hsp31_like | cd03141 | Type 1 glutamine amidotransferase (GATase1)-like domain found in proteins similar to ... |
53-285 | 3.19e-57 | |||||
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: 183.14 E-value: 3.19e-57
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| YajL | COG0693 | Protein/nucleotide deglycase, PfpI/YajL/DJ-1 family (repair of methylglyoxal-glycated proteins ... |
50-285 | 6.25e-27 | |||||
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: 103.26 E-value: 6.25e-27
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| GATase1_Ydr533c_like | cd03147 | Type 1 glutamine amidotransferase (GATase1)-like domain found in Saccharomyces cerevisiae ... |
52-218 | 1.29e-08 | |||||
Type 1 glutamine amidotransferase (GATase1)-like domain found in Saccharomyces cerevisiae Ydr533c protein; Type 1 glutamine amidotransferase (GATase1)-like domain found in Saccharomyces cerevisiae Ydr533c protein. This group includes proteins similar to S. cerevisiae Ydr533c. Ydr533c is upregulated in response to various stress conditions along with the heat shock family. The catalytic triad typical of GATase1domains is not conserved in this GATase1-like domain. However, in common with a typical GATase1domain, a reactive Cys residue is found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. This Cys together with a different His and Glu residue form a different catalytic triad from the typical GATase1domain. Ydr533c protein is a homodimer. Pssm-ID: 153241 [Multi-domain] Cd Length: 231 Bit Score: 54.25 E-value: 1.29e-08
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| DJ-1_PfpI | pfam01965 | DJ-1/PfpI family; The family includes the protease PfpI. This domain is also found in ... |
51-199 | 8.73e-07 | |||||
DJ-1/PfpI family; The family includes the protease PfpI. This domain is also found in transcriptional regulators. Pssm-ID: 396514 [Multi-domain] Cd Length: 165 Bit Score: 48.02 E-value: 8.73e-07
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| GATase1_DJ-1 | cd03135 | Type 1 glutamine amidotransferase (GATase1)-like domain found in Human DJ-1; Type 1 glutamine ... |
70-285 | 2.71e-06 | |||||
Type 1 glutamine amidotransferase (GATase1)-like domain found in Human DJ-1; Type 1 glutamine amidotransferase (GATase1)-like domain found in Human DJ-1. DJ-1 is involved in multiple physiological processes including cancer, Parkinson's disease and male fertility. It is unclear how DJ-1 functions in these. DJ-1 has been shown to possess chaperone activity. DJ-1 is preferentially expressed in the testis and moderately in other tissues; it is induced together with genes involved in oxidative stress response. The Drosophila homologue (DJ-1A) plays an essential role in oxidative stress response and neuronal maintenance. Inhibition of DJ-1A function through RNAi, results in the cellular accumulation of reactive oxygen species, organismal hypersensitivity to oxidative stress, and dysfunction and degeneration of dopaminergic and photoreceptor neurons. DJ-1 has lacks enzymatic activity and the catalytic triad of typical GATase1 domains, however it does contain the highly conserved cysteine located at the nucelophile elbow region typical of these domains. This cysteine been proposed to be a site of regulation of DJ-1 activity by oxidation. DJ-1 is a dimeric enzyme. Pssm-ID: 153229 [Multi-domain] Cd Length: 163 Bit Score: 46.39 E-value: 2.71e-06
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| GATase1 | cd01653 | Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
147-195 | 7.90e-06 | |||||
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: 44.13 E-value: 7.90e-06
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| GAT_1 | cd03128 | Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
147-194 | 1.94e-05 | |||||
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: 42.57 E-value: 1.94e-05
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| GATase1_PfpI_1 | cd03169 | Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ... |
52-198 | 1.11e-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: 41.86 E-value: 1.11e-04
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