Summary: OHCU decarboxylase
This is the Wikipedia entry entitled "2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase". More...
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2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase Edit Wikipedia article
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In molecular biology 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase (OHCU decarboxylase) EC 4.1.1.n1 is an enzyme involved in purine catabolism. It catalyses the decarboxylation of 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline (OHCU) into S(+)-allantoin. It is the third step of the conversion of uric acid (a purine derivative) to allantoin. Step one is catalysed by urate oxidase and step two is catalysed by hydroxyisourate hydrolase.
- Ramazzina I, Folli C, Secchi A, Berni R, Percudani R (March 2006). "Completing the uric acid degradation pathway through phylogenetic comparison of whole genomes". Nat. Chem. Biol. 2 (3): 144–8. doi:10.1038/nchembio768. PMID 16462750.
- Cendron L, Berni R, Folli C, Ramazzina I, Percudani R, Zanotti G (2007). "The structure of 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase provides insights into the mechanism of uric acid degradation.". J Biol Chem 282 (25): 18182–9. doi:10.1074/jbc.M701297200. PMID 17428786.
- Kim K, Park J, Rhee S (2007). "Structural and functional basis for (S)-allantoin formation in the ureide pathway.". J Biol Chem 282 (32): 23457–64. doi:10.1074/jbc.M703211200. PMID 17567580.
- Todd CD, Tipton PA, Blevins DG, Piedras P, Pineda M, Polacco JC (2006). "Update on ureide degradation in legumes.". J Exp Bot 57 (1): 5–12. doi:10.1093/jxb/erj013. PMID 16317038.
OHCU decarboxylase Provide feedback
The proteins in this family are OHCU decarboxylase - enzymes of the purine catabolism that catalyse the conversion of OHCU into S(+)-allantoin . This is the third step of the conversion of uric acid (a purine derivative) to allantoin. Step one is catalysed by urate oxidase (PF01014) and step two is catalysed by HIUases (PF00576).
Ramazzina I, Folli C, Secchi A, Berni R, Percudani R; , Nat Chem Biol. 2006;2:144-148.: Completing the uric acid degradation pathway through phylogenetic comparison of whole genomes. PUBMED:16462750 EPMC:16462750
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR018020
The proteins in this entry are OHCU decarboxylase, an enzyme of the purine catabolism that catalyses the conversion of OHCU into S(+)-allantoin [PUBMED:16462750]; it is the third step of the conversion of uric acid (a purine derivative) to allantoin. Step one is catalysed by urate oxidase (INTERPRO) and step two is catalysed by hydroxyisourate hydrolase (INTERPRO).
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This example describes an architecture with one
Gladomain, followed by two consecutive
EGFdomains, and finally a single
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Curation and family details
|Seed source:||PSI2 target BIG_237|
|Author:||Bateman A, Percudani R|
|Number in seed:||369|
|Number in full:||3590|
|Average length of the domain:||154.80 aa|
|Average identity of full alignment:||31 %|
|Average coverage of the sequence by the domain:||61.79 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 80369284 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||6|
|Download:||download the raw HMM for this family|
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There is 1 interaction for this family. More...
We determine these interactions using iPfam, which considers the interactions between residues in three-dimensional protein structures and maps those interactions back to Pfam families. You can find more information about the iPfam algorithm in the journal article that accompanies the website.
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the OHCU_decarbox domain has been found. There are 26 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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