cupin domain-containing protein, part of a functionally diverse superfamily with the active site generally located at the center of a conserved domain forming a beta-barrel fold
Homogentisate 1,2-dioxygenase N-terminal; Homogentisate dioxygenase cleaves the aromatic ring ...
5-227
1.40e-146
Homogentisate 1,2-dioxygenase N-terminal; Homogentisate dioxygenase cleaves the aromatic ring during the metabolic degradation of Phe and Tyr. Homogentisate dioxygenase deficiency causes alkaptonuria. The structure of homogentisate dioxygenase shows that the enzyme forms a hexamer arrangement comprised of a dimer of trimers. The active site iron ion is coordinated near the interface between the trimers. This entry represents the N-terminal domain which forms a jelly roll of beta-strands.
The actual alignment was detected with superfamily member pfam20510:
Pssm-ID: 466659 Cd Length: 271 Bit Score: 409.43 E-value: 1.40e-146
Homogentisate 1,2-dioxygenase N-terminal; Homogentisate dioxygenase cleaves the aromatic ring ...
5-227
1.40e-146
Homogentisate 1,2-dioxygenase N-terminal; Homogentisate dioxygenase cleaves the aromatic ring during the metabolic degradation of Phe and Tyr. Homogentisate dioxygenase deficiency causes alkaptonuria. The structure of homogentisate dioxygenase shows that the enzyme forms a hexamer arrangement comprised of a dimer of trimers. The active site iron ion is coordinated near the interface between the trimers. This entry represents the N-terminal domain which forms a jelly roll of beta-strands.
Pssm-ID: 466659 Cd Length: 271 Bit Score: 409.43 E-value: 1.40e-146
homogentisate 1,2-dioxygenase and related proteins, N-terminal cupin domain; This family ...
95-205
5.20e-74
homogentisate 1,2-dioxygenase and related proteins, N-terminal cupin domain; This family includes homogentisate 1,2-dioxygenase (also known as homogentisate oxygenase, homogentisic acid oxidase, homogentisicase, HGO, HGD, HGDO, or HmgA; EC 1.13.11.5), which is involved in the metabolic degradation of phenylalanine and tyrosine. It catalyzes the crucial aromatic ring opening reaction, utilizing nonheme Fe2+ to incorporate both atoms of molecular oxygen into homogentisate (2,5-dihydroxyphenylacetate) to yield 4-maleylacetoacetate as part of the homogentisate pathway. HGO deficiency caused by critical mutations and polymorphic sites, causes the metabolic disease alkaptonuria (AKU), a rare disorder of autosomal recessive inheritance. Homogentisate accumulation causes insoluble ochronotic pigments to deposit in connective tissues, resulting in degenerative arthritis. These enzymes are found in prokaryotes, eukaryotes, and archaea. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.
Pssm-ID: 380404 [Multi-domain] Cd Length: 109 Bit Score: 219.70 E-value: 5.20e-74
Homogentisate 1,2-dioxygenase N-terminal; Homogentisate dioxygenase cleaves the aromatic ring ...
5-227
1.40e-146
Homogentisate 1,2-dioxygenase N-terminal; Homogentisate dioxygenase cleaves the aromatic ring during the metabolic degradation of Phe and Tyr. Homogentisate dioxygenase deficiency causes alkaptonuria. The structure of homogentisate dioxygenase shows that the enzyme forms a hexamer arrangement comprised of a dimer of trimers. The active site iron ion is coordinated near the interface between the trimers. This entry represents the N-terminal domain which forms a jelly roll of beta-strands.
Pssm-ID: 466659 Cd Length: 271 Bit Score: 409.43 E-value: 1.40e-146
homogentisate 1,2-dioxygenase and related proteins, N-terminal cupin domain; This family ...
95-205
5.20e-74
homogentisate 1,2-dioxygenase and related proteins, N-terminal cupin domain; This family includes homogentisate 1,2-dioxygenase (also known as homogentisate oxygenase, homogentisic acid oxidase, homogentisicase, HGO, HGD, HGDO, or HmgA; EC 1.13.11.5), which is involved in the metabolic degradation of phenylalanine and tyrosine. It catalyzes the crucial aromatic ring opening reaction, utilizing nonheme Fe2+ to incorporate both atoms of molecular oxygen into homogentisate (2,5-dihydroxyphenylacetate) to yield 4-maleylacetoacetate as part of the homogentisate pathway. HGO deficiency caused by critical mutations and polymorphic sites, causes the metabolic disease alkaptonuria (AKU), a rare disorder of autosomal recessive inheritance. Homogentisate accumulation causes insoluble ochronotic pigments to deposit in connective tissues, resulting in degenerative arthritis. These enzymes are found in prokaryotes, eukaryotes, and archaea. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.
Pssm-ID: 380404 [Multi-domain] Cd Length: 109 Bit Score: 219.70 E-value: 5.20e-74
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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Functional characterization of the conserved domain architecture found on the query.
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if a domain or superfamily has been annotated with functional sites (conserved features),
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The table lists conserved domains identified on the query sequence. Click on the plus sign (+) on the left to display full descriptions, alignments, and scores.
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(labeled illustration) Standard Display shows only the best scoring domain model from each source, in each hit category listed below for each region on the query sequence.
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