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Protein

2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase

Gene

urad

Organism
Danio rerio (Zebrafish) (Brachydanio rerio)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the stereoselective decarboxylation of 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline (OHCU) to (S)-allantoin.1 Publication

Catalytic activityi

5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-5-carboxylate = (S)-allantoin + CO2.

Pathwayi: urate degradation

This protein is involved in step 3 of the subpathway that synthesizes (S)-allantoin from urate.
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. Uricase (uox)
  2. 5-hydroxyisourate hydrolase (urah)
  3. 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase (urad)
This subpathway is part of the pathway urate degradation, which is itself part of Purine metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes (S)-allantoin from urate, the pathway urate degradation and in Purine metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei67 – 671Proton donorBy similarity
Binding sitei68 – 681Substrate; via carbonyl oxygen

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Decarboxylase, Lyase

Keywords - Biological processi

Purine metabolism

Enzyme and pathway databases

BRENDAi4.1.1.97. 928.
UniPathwayiUPA00394; UER00652.

Names & Taxonomyi

Protein namesi
Recommended name:
2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase (EC:4.1.1.97)
Short name:
OHCU decarboxylase
Alternative name(s):
Parahox neighbor
Ureidoimidazoline (2-oxo-4-hydroxy-4-carboxy-5-) decarboxylase
Gene namesi
Name:urad
Synonyms:prhoxnb
ORF Names:zgc:158663
OrganismiDanio rerio (Zebrafish) (Brachydanio rerio)
Taxonomic identifieri7955 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiOstariophysiCypriniformesCyprinidaeDanio
Proteomesi
  • UP000000437 Componenti: Chromosome 24

Organism-specific databases

ZFINiZDB-GENE-070112-472. urad.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Peroxisome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi67 – 671H → N: Loss of activity. 1 Publication
Mutagenesisi87 – 871E → Q: Loss of activity. 1 Publication
Mutagenesisi161 – 1611R → Q: Loss of activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 1741742-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylasePRO_0000315243Add
BLAST

Proteomic databases

PaxDbiA1L259.

Expressioni

Gene expression databases

BgeeiA1L259.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

STRINGi7955.ENSDARP00000096695.

Structurei

Secondary structure

1
174
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 75Combined sources
Helixi11 – 188Combined sources
Helixi26 – 327Combined sources
Helixi33 – 353Combined sources
Helixi41 – 5414Combined sources
Helixi57 – 659Combined sources
Helixi73 – 775Combined sources
Helixi82 – 909Combined sources
Turni91 – 944Combined sources
Helixi98 – 11518Combined sources
Helixi123 – 1253Combined sources
Helixi128 – 13811Combined sources
Helixi143 – 16523Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2O70X-ray1.80A/B/C/D/E/F1-174[»]
2O73X-ray1.80A/B/C/D/E/F1-174[»]
2O74X-ray1.80A/B/C/D/E/F1-174[»]
ProteinModelPortaliA1L259.
SMRiA1L259. Positions 1-168.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiA1L259.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni84 – 885Substrate binding
Regioni119 – 1235Substrate binding

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi172 – 1743Microbody targeting signalSequence analysis

Sequence similaritiesi

Belongs to the OHCU decarboxylase family.Curated

Phylogenomic databases

eggNOGiENOG410IX4N. Eukaryota.
COG3195. LUCA.
GeneTreeiENSGT00390000002395.
HOGENOMiHOG000251764.
HOVERGENiHBG108651.
InParanoidiA1L259.
KOiK13485.
OMAiHRIAQFR.
OrthoDBiEOG7GFB6D.
PhylomeDBiA1L259.
TreeFamiTF323276.

Family and domain databases

Gene3Di1.10.3330.10. 1 hit.
InterProiIPR018020. OHCU_decarboxylase.
IPR017580. OHCU_decarboxylase-1.
[Graphical view]
PfamiPF09349. OHCU_decarbox. 1 hit.
[Graphical view]
TIGRFAMsiTIGR03164. UHCUDC. 1 hit.

Sequencei

Sequence statusi: Complete.

A1L259-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDINVVNALA YEDFVKLFGN VVEKCPLISA AIWSYRPFKD LADIEARISE
60 70 80 90 100
FIHSLPDSGK EGILRCHPDL AGRDLQSGTL TPESQEEQSQ AGMTTLDSAE
110 120 130 140 150
IVHMYRLNSE YKERFGFPFV ICARLNNKAD IVRQLSERLK NRRTAELECA
160 170
IEEVKKICSL RLHSIVLSDI QTKL
Length:174
Mass (Da):19,743
Last modified:February 6, 2007 - v1
Checksum:i1B408D09F29FF4D7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EF197726 mRNA. Translation: ABP04232.1.
BC129362 mRNA. Translation: AAI29363.1.
RefSeqiNP_001073641.1. NM_001080172.1.
UniGeneiDr.87169.

Genome annotation databases

EnsembliENSDART00000105917; ENSDARP00000096695; ENSDARG00000071579.
GeneIDi557735.
KEGGidre:557735.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EF197726 mRNA. Translation: ABP04232.1.
BC129362 mRNA. Translation: AAI29363.1.
RefSeqiNP_001073641.1. NM_001080172.1.
UniGeneiDr.87169.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2O70X-ray1.80A/B/C/D/E/F1-174[»]
2O73X-ray1.80A/B/C/D/E/F1-174[»]
2O74X-ray1.80A/B/C/D/E/F1-174[»]
ProteinModelPortaliA1L259.
SMRiA1L259. Positions 1-168.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi7955.ENSDARP00000096695.

Proteomic databases

PaxDbiA1L259.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSDART00000105917; ENSDARP00000096695; ENSDARG00000071579.
GeneIDi557735.
KEGGidre:557735.

Organism-specific databases

CTDi646625.
ZFINiZDB-GENE-070112-472. urad.

Phylogenomic databases

eggNOGiENOG410IX4N. Eukaryota.
COG3195. LUCA.
GeneTreeiENSGT00390000002395.
HOGENOMiHOG000251764.
HOVERGENiHBG108651.
InParanoidiA1L259.
KOiK13485.
OMAiHRIAQFR.
OrthoDBiEOG7GFB6D.
PhylomeDBiA1L259.
TreeFamiTF323276.

Enzyme and pathway databases

UniPathwayiUPA00394; UER00652.
BRENDAi4.1.1.97. 928.

Miscellaneous databases

EvolutionaryTraceiA1L259.
NextBioi20882132.
PROiA1L259.

Gene expression databases

BgeeiA1L259.

Family and domain databases

Gene3Di1.10.3330.10. 1 hit.
InterProiIPR018020. OHCU_decarboxylase.
IPR017580. OHCU_decarboxylase-1.
[Graphical view]
PfamiPF09349. OHCU_decarbox. 1 hit.
[Graphical view]
TIGRFAMsiTIGR03164. UHCUDC. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The structure of 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase provides insights into the mechanism of uric acid degradation."
    Cendron L., Berni R., Folli C., Ramazzina I., Percudani R., Zanotti G.
    J. Biol. Chem. 282:18182-18189(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEXES WITH SUBSTRATE ANALOGS, FUNCTION, MUTAGENESIS OF HIS-67; GLU-87 AND ARG-161, SUBUNIT.
  2. NIH - Zebrafish Gene Collection (ZGC) project
    Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Liver.

Entry informationi

Entry nameiURAD_DANRE
AccessioniPrimary (citable) accession number: A1L259
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: February 6, 2007
Last modified: December 9, 2015
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.