Urate oxidase (UO, uricase) is a peroxisomal enzyme that catalyzes the oxidation of uric acid ...
26-302
4.57e-156
Urate oxidase (UO, uricase) is a peroxisomal enzyme that catalyzes the oxidation of uric acid to allantoin in most fish, amphibian, and mammalian species. The enzymatic process involves catalyzing the oxidative opening of the purine ring during the purine degradation pathway. In humans and certain other primates, however, the enzyme has been lost by some unknown mechanism. Each monomer contains two instances of this domain. Its functional form is a homotetramer for most species, though there are reports that some may form heterotetramers based on a few biochemical studies.
Pssm-ID: 238251 Cd Length: 286 Bit Score: 437.18 E-value: 4.57e-156
urate oxidase; Members of this protein family are urate oxidase, also called uricase. This ...
31-302
2.27e-134
urate oxidase; Members of this protein family are urate oxidase, also called uricase. This protein contains two copies of the domain described by the uricase model pfam01014. In animals, this enzyme has been lost from primates and birds. [Central intermediary metabolism, Other]
Pssm-ID: 274554 Cd Length: 282 Bit Score: 382.31 E-value: 2.27e-134
Urate oxidase (UO, uricase) is a peroxisomal enzyme that catalyzes the oxidation of uric acid ...
26-302
4.57e-156
Urate oxidase (UO, uricase) is a peroxisomal enzyme that catalyzes the oxidation of uric acid to allantoin in most fish, amphibian, and mammalian species. The enzymatic process involves catalyzing the oxidative opening of the purine ring during the purine degradation pathway. In humans and certain other primates, however, the enzyme has been lost by some unknown mechanism. Each monomer contains two instances of this domain. Its functional form is a homotetramer for most species, though there are reports that some may form heterotetramers based on a few biochemical studies.
Pssm-ID: 238251 Cd Length: 286 Bit Score: 437.18 E-value: 4.57e-156
urate oxidase; Members of this protein family are urate oxidase, also called uricase. This ...
31-302
2.27e-134
urate oxidase; Members of this protein family are urate oxidase, also called uricase. This protein contains two copies of the domain described by the uricase model pfam01014. In animals, this enzyme has been lost from primates and birds. [Central intermediary metabolism, Other]
Pssm-ID: 274554 Cd Length: 282 Bit Score: 382.31 E-value: 2.27e-134
Tunnelling fold (T-fold). The five known T-folds are found in five different enzymes with ...
147-299
3.65e-14
Tunnelling fold (T-fold). The five known T-folds are found in five different enzymes with different functions: dihydroneopterin-triphosphate epimerase (DHNTPE), dihydroneopterin aldolase (DHNA) , GTP cyclohydrolase I (GTPCH-1), 6-pyrovoyl tetrahydropterin synthetase (PTPS), and uricase (UO,uroate/urate oxidase). They bind to substrates belonging to the purine or pterin families, and share a fold-related binding site with a glutamate or glutamine residue anchoring the substrate and a lot of conserved interactions. They also share a similar oligomerization mode: several T-folds join together to form a beta(2n)alpha(n) barrel, then two barrels join together in a head-to-head fashion to made up the native enzymes. The functional enzyme is a tetramer for UO, a hexamer for PTPS, an octamer for DHNA/DHNTPE and a decamer for GTPCH-1. The substrate is located in a deep and narrow pocket at the interface between monomers. In PTPS, the active site is located at the interface of three monomers, two from one trimer and one from the other trimer. In GTPCH-1, it is also located at the interface of three subunits, two from one pentamer and one from the other pentamer. There are four equivalent active sites in UO, six in PTPS, eight in DHNA/DHNTPE and ten in GTPCH-1. Each globular multimeric enzyme encloses a tunnel which is lined with charged residues for DHNA and UO, and with basic residues in PTPS. The N and C-terminal ends are located on one side of the T-fold while the residues involved in the catalytic activity are located at the opposite side. In PTPS, UO and DHNA/DHNTPE, the N and C-terminal extremities of the enzyme are located on the exterior side of the functional multimeric enzyme. In GTPCH-1, the extra C-terminal helix places the extremity inside the tunnel.
Pssm-ID: 238351 Cd Length: 122 Bit Score: 67.85 E-value: 3.65e-14
Tunnelling fold (T-fold). The five known T-folds are found in five different enzymes with ...
31-136
2.12e-09
Tunnelling fold (T-fold). The five known T-folds are found in five different enzymes with different functions: dihydroneopterin-triphosphate epimerase (DHNTPE), dihydroneopterin aldolase (DHNA) , GTP cyclohydrolase I (GTPCH-1), 6-pyrovoyl tetrahydropterin synthetase (PTPS), and uricase (UO,uroate/urate oxidase). They bind to substrates belonging to the purine or pterin families, and share a fold-related binding site with a glutamate or glutamine residue anchoring the substrate and a lot of conserved interactions. They also share a similar oligomerization mode: several T-folds join together to form a beta(2n)alpha(n) barrel, then two barrels join together in a head-to-head fashion to made up the native enzymes. The functional enzyme is a tetramer for UO, a hexamer for PTPS, an octamer for DHNA/DHNTPE and a decamer for GTPCH-1. The substrate is located in a deep and narrow pocket at the interface between monomers. In PTPS, the active site is located at the interface of three monomers, two from one trimer and one from the other trimer. In GTPCH-1, it is also located at the interface of three subunits, two from one pentamer and one from the other pentamer. There are four equivalent active sites in UO, six in PTPS, eight in DHNA/DHNTPE and ten in GTPCH-1. Each globular multimeric enzyme encloses a tunnel which is lined with charged residues for DHNA and UO, and with basic residues in PTPS. The N and C-terminal ends are located on one side of the T-fold while the residues involved in the catalytic activity are located at the opposite side. In PTPS, UO and DHNA/DHNTPE, the N and C-terminal extremities of the enzyme are located on the exterior side of the functional multimeric enzyme. In GTPCH-1, the extra C-terminal helix places the extremity inside the tunnel.
Pssm-ID: 238351 Cd Length: 122 Bit Score: 54.37 E-value: 2.12e-09
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.
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