Homogentisate 1,2-dioxygenase N-terminal; Homogentisate dioxygenase cleaves the aromatic ring ...
5-279
0e+00
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: 533.47 E-value: 0e+00
homogentisate 1,2-dioxygenase and related proteins, N-terminal cupin domain; This family ...
95-205
5.72e-71
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: 219.32 E-value: 5.72e-71
Homogentisate 1,2-dioxygenase N-terminal; Homogentisate dioxygenase cleaves the aromatic ring ...
5-279
0e+00
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: 533.47 E-value: 0e+00
Homogentisate 1,2-dioxygenase C-terminal; Homogentisate dioxygenase cleaves the aromatic ring ...
280-434
1.30e-108
Homogentisate 1,2-dioxygenase C-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 C-terminal active site domain.
Pssm-ID: 461227 [Multi-domain] Cd Length: 153 Bit Score: 317.40 E-value: 1.30e-108
homogentisate 1,2-dioxygenase and related proteins, N-terminal cupin domain; This family ...
95-205
5.72e-71
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: 219.32 E-value: 5.72e-71
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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This image shows a graphical summary of conserved domains identified on the query sequence.
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if a domain or superfamily has been annotated with functional sites (conserved features),
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click on the bars or triangles to view your query sequence embedded in a multiple sequence alignment of the proteins used to develop the corresponding domain model.
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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To view your query sequence embedded in that multiple sequence alignment, click on the colored bars in the Graphical Summary portion of the search results page,
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Concise Display shows only the best scoring domain model, in each hit category listed below except non-specific hits, for each region on the query sequence.
(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.
(labeled illustration) Full Display shows all domain models, in each hit category below, that meet or exceed the RPS-BLAST threshold for statistical significance.
(labeled illustration) Four types of hits can be shown, as available,
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specific hits meet or exceed a domain-specific e-value threshold
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and represent a very high confidence that the query sequence belongs to the same protein family as the sequences use to create the domain model
non-specific hits
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the domain superfamily to which the specific and non-specific hits belong
multi-domain models that were computationally detected and are likely to contain multiple single domains
Retrieve proteins that contain one or more of the domains present in the query sequence, using the Conserved Domain Architecture Retrieval Tool
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