URAD_DANRE
ID URAD_DANRE Reviewed; 174 AA.
AC A1L259;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase;
DE Short=OHCU decarboxylase;
DE EC=4.1.1.97;
DE AltName: Full=Parahox neighbor;
DE AltName: Full=Ureidoimidazoline (2-oxo-4-hydroxy-4-carboxy-5-) decarboxylase;
GN Name=urad; Synonyms=prhoxnb; ORFNames=zgc:158663;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN
RP COMPLEXES WITH SUBSTRATE ANALOGS, FUNCTION, MUTAGENESIS OF HIS-67; GLU-87
RP AND ARG-161, AND SUBUNIT.
RX PubMed=17428786; DOI=10.1074/jbc.m701297200;
RA Cendron L., Berni R., Folli C., Ramazzina I., Percudani R., Zanotti G.;
RT "The structure of 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline
RT decarboxylase provides insights into the mechanism of uric acid
RT degradation.";
RL J. Biol. Chem. 282:18182-18189(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the stereoselective decarboxylation of 2-oxo-4-
CC hydroxy-4-carboxy-5-ureidoimidazoline (OHCU) to (S)-allantoin.
CC {ECO:0000269|PubMed:17428786}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-5-
CC carboxylate + H(+) = (S)-allantoin + CO2; Xref=Rhea:RHEA:26301,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15678, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:58639; EC=4.1.1.97;
CC -!- PATHWAY: Purine metabolism; urate degradation; (S)-allantoin from
CC urate: step 3/3.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:17428786}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the OHCU decarboxylase family. {ECO:0000305}.
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DR EMBL; EF197726; ABP04232.1; -; mRNA.
DR EMBL; BC129362; AAI29363.1; -; mRNA.
DR RefSeq; NP_001073641.1; NM_001080172.1.
DR PDB; 2O70; X-ray; 1.80 A; A/B/C/D/E/F=1-174.
DR PDB; 2O73; X-ray; 1.80 A; A/B/C/D/E/F=1-174.
DR PDB; 2O74; X-ray; 1.80 A; A/B/C/D/E/F=1-174.
DR PDBsum; 2O70; -.
DR PDBsum; 2O73; -.
DR PDBsum; 2O74; -.
DR AlphaFoldDB; A1L259; -.
DR SMR; A1L259; -.
DR STRING; 7955.ENSDARP00000096695; -.
DR PaxDb; A1L259; -.
DR PeptideAtlas; A1L259; -.
DR Ensembl; ENSDART00000105917; ENSDARP00000096695; ENSDARG00000071579.
DR Ensembl; ENSDART00000184990; ENSDARP00000148135; ENSDARG00000115541.
DR GeneID; 557735; -.
DR KEGG; dre:557735; -.
DR CTD; 646625; -.
DR ZFIN; ZDB-GENE-070112-472; urad.
DR eggNOG; KOG0848; Eukaryota.
DR GeneTree; ENSGT00390000002395; -.
DR HOGENOM; CLU_092522_1_0_1; -.
DR InParanoid; A1L259; -.
DR OMA; KICHLRL; -.
DR OrthoDB; 1547390at2759; -.
DR PhylomeDB; A1L259; -.
DR TreeFam; TF323276; -.
DR BRENDA; 4.1.1.97; 928.
DR UniPathway; UPA00394; UER00652.
DR EvolutionaryTrace; A1L259; -.
DR PRO; PR:A1L259; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 24.
DR Bgee; ENSDARG00000071579; Expressed in liver and 7 other tissues.
DR GO; GO:0005777; C:peroxisome; IBA:GO_Central.
DR GO; GO:0051997; F:2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase activity; IDA:ZFIN.
DR GO; GO:0000255; P:allantoin metabolic process; IEA:InterPro.
DR GO; GO:0006144; P:purine nucleobase metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0019628; P:urate catabolic process; IBA:GO_Central.
DR Gene3D; 1.10.3330.10; -; 1.
DR InterPro; IPR018020; OHCU_decarboxylase.
DR InterPro; IPR017580; OHCU_decarboxylase-1.
DR InterPro; IPR036778; OHCU_decarboxylase_sf.
DR Pfam; PF09349; OHCU_decarbox; 1.
DR SUPFAM; SSF158694; SSF158694; 1.
DR TIGRFAMs; TIGR03164; UHCUDC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Decarboxylase; Lyase; Peroxisome; Purine metabolism;
KW Reference proteome.
FT CHAIN 1..174
FT /note="2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline
FT decarboxylase"
FT /id="PRO_0000315243"
FT MOTIF 172..174
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT ACT_SITE 67
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 68
FT /ligand="substrate"
FT BINDING 84..88
FT /ligand="substrate"
FT BINDING 119..123
FT /ligand="substrate"
FT MUTAGEN 67
FT /note="H->N: Loss of activity."
FT /evidence="ECO:0000269|PubMed:17428786"
FT MUTAGEN 87
FT /note="E->Q: Loss of activity."
FT /evidence="ECO:0000269|PubMed:17428786"
FT MUTAGEN 161
FT /note="R->Q: Loss of activity."
FT /evidence="ECO:0000269|PubMed:17428786"
FT HELIX 3..7
FT /evidence="ECO:0007829|PDB:2O70"
FT HELIX 11..18
FT /evidence="ECO:0007829|PDB:2O70"
FT HELIX 26..32
FT /evidence="ECO:0007829|PDB:2O70"
FT HELIX 33..35
FT /evidence="ECO:0007829|PDB:2O70"
FT HELIX 41..54
FT /evidence="ECO:0007829|PDB:2O70"
FT HELIX 57..65
FT /evidence="ECO:0007829|PDB:2O70"
FT HELIX 73..77
FT /evidence="ECO:0007829|PDB:2O70"
FT HELIX 82..90
FT /evidence="ECO:0007829|PDB:2O70"
FT TURN 91..94
FT /evidence="ECO:0007829|PDB:2O73"
FT HELIX 98..115
FT /evidence="ECO:0007829|PDB:2O70"
FT HELIX 123..125
FT /evidence="ECO:0007829|PDB:2O70"
FT HELIX 128..138
FT /evidence="ECO:0007829|PDB:2O70"
FT HELIX 143..165
FT /evidence="ECO:0007829|PDB:2O70"
SQ SEQUENCE 174 AA; 19743 MW; 1B408D09F29FF4D7 CRC64;
MDINVVNALA YEDFVKLFGN VVEKCPLISA AIWSYRPFKD LADIEARISE FIHSLPDSGK
EGILRCHPDL AGRDLQSGTL TPESQEEQSQ AGMTTLDSAE IVHMYRLNSE YKERFGFPFV
ICARLNNKAD IVRQLSERLK NRRTAELECA IEEVKKICSL RLHSIVLSDI QTKL
