PTD012 family protein similar to Homo sapiens PTD012 (also called ester hydrolase C11orf54), a zinc-containing hydrolase fold protein which exhibits ester hydrolase activity on the substrate p-nitrophenyl acetate
proteins similar to putative ester hydrolase C11orf54/PTD012; The structure of this domain ...
14-245
3.25e-155
proteins similar to putative ester hydrolase C11orf54/PTD012; The structure of this domain displays an alpha-beta-beta-alpha four layer topology, with an HxHxxxxxxxxxH motif (x could be any residue) that coordinates a zinc ion, and an acetate anion at a site that may support the enzymatic activity of a ester. In vitro hydrolytic activity towards para-nitrophenylacetate for the human enzyme was reported. The proteins are homologous to bacterial alpha-acetolactate decarboxylase (AldB, E.C. 4.1.1.5), which converts acetolactate into acetoin.
:
Pssm-ID: 341210 Cd Length: 287 Bit Score: 433.07 E-value: 3.25e-155
proteins similar to putative ester hydrolase C11orf54/PTD012; The structure of this domain ...
14-245
3.25e-155
proteins similar to putative ester hydrolase C11orf54/PTD012; The structure of this domain displays an alpha-beta-beta-alpha four layer topology, with an HxHxxxxxxxxxH motif (x could be any residue) that coordinates a zinc ion, and an acetate anion at a site that may support the enzymatic activity of a ester. In vitro hydrolytic activity towards para-nitrophenylacetate for the human enzyme was reported. The proteins are homologous to bacterial alpha-acetolactate decarboxylase (AldB, E.C. 4.1.1.5), which converts acetolactate into acetoin.
Pssm-ID: 341210 Cd Length: 287 Bit Score: 433.07 E-value: 3.25e-155
Domain of Unknown Function (DUF1907); The structure of this domain displays an ...
21-244
1.13e-145
Domain of Unknown Function (DUF1907); The structure of this domain displays an alpha-beta-beta-alpha four layer topology, with an HxHxxxxxxxxxH motif that coordinates a zinc ion, and an acetate anion at a site that likely supports the enzymatic activity of an ester hydrolase.
Pssm-ID: 462636 Cd Length: 281 Bit Score: 408.50 E-value: 1.13e-145
proteins similar to putative ester hydrolase C11orf54/PTD012; The structure of this domain ...
14-245
3.25e-155
proteins similar to putative ester hydrolase C11orf54/PTD012; The structure of this domain displays an alpha-beta-beta-alpha four layer topology, with an HxHxxxxxxxxxH motif (x could be any residue) that coordinates a zinc ion, and an acetate anion at a site that may support the enzymatic activity of a ester. In vitro hydrolytic activity towards para-nitrophenylacetate for the human enzyme was reported. The proteins are homologous to bacterial alpha-acetolactate decarboxylase (AldB, E.C. 4.1.1.5), which converts acetolactate into acetoin.
Pssm-ID: 341210 Cd Length: 287 Bit Score: 433.07 E-value: 3.25e-155
Domain of Unknown Function (DUF1907); The structure of this domain displays an ...
21-244
1.13e-145
Domain of Unknown Function (DUF1907); The structure of this domain displays an alpha-beta-beta-alpha four layer topology, with an HxHxxxxxxxxxH motif that coordinates a zinc ion, and an acetate anion at a site that likely supports the enzymatic activity of an ester hydrolase.
Pssm-ID: 462636 Cd Length: 281 Bit Score: 408.50 E-value: 1.13e-145
proteins similar to alpha-acetolactate dehydrogenase; The structure of this domain displays an ...
56-245
3.24e-40
proteins similar to alpha-acetolactate dehydrogenase; The structure of this domain displays an alpha-beta-beta-alpha four layer topology, with an H(x)H(x)nH motif (x could be any residue, n could be 9 or 10) that coordinates a zinc ion. The proteins are homologous to bacterial alpha-acetolactate decarboxylase (AldB, E.C. 4.1.1.5), which converts acetolactate into acetoin.
Pssm-ID: 341209 Cd Length: 209 Bit Score: 137.98 E-value: 3.24e-40
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.
of the residues that compose this conserved feature have been mapped to the query sequence.
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