[1]	NUCLEOTIDE SEQUENCE [MRNA]. PubMed=2594778 [NCBI, ExPASy, EBI, Israel, Japan] Wu X., Lee C.C., Muzny D.M., Caskey C.T.; "Urate oxidase: primary structure and evolutionary implications."; Proc. Natl. Acad. Sci. U.S.A. 86:9412-9416(1989).
[2]	NUCLEOTIDE SEQUENCE. PubMed=11961098 [NCBI, ExPASy, EBI, Israel, Japan] Oda M., Satta Y., Takenaka O., Takahata N.; "Loss of urate oxidase activity in hominoids and its evolutionary implications."; Mol. Biol. Evol. 19:640-653(2002).

Comments

FUNCTION: Catalyzes the oxidation of uric acid to 5-hydroxyisourate, which spontaneously decomposes to form allantoin.
CATALYTIC ACTIVITY: Urate + O₂ + H₂O = 5-hydroxyisourate + H₂O₂.
PATHWAY: Purine metabolism; uric acid degradation; (S)-allantoin from uric acid: step 1/3 .
SUBCELLULAR LOCATION: Peroxisome.
SIMILARITY: Belongs to the uricase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M27694; AAA35395.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AB074366; BAB91554.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

Q00511; 1UOX. [HSSP ENTRY / PDB]

ModBase

P25689.

Ontologies

GO:0005777;	Cellular component: peroxisome (inferred from electronic annotation from UniProtKB-KW).
GO:0004846;	Molecular function: urate oxidase activity (inferred from electronic annotation from InterPro).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0006144;	Biological process: purine base metabolic process (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR002042; Uricase.
Graphical view of domain structure.

Gene3D

G3DSA:3.10.270.10; Uricase; 1.

PANTHER

PTHR10395:SF1; Uricase; 1.

Pfam

PF01014; Uricase; 2.
Pfam graphical view of domain structure.

PRINTS

PR00093; URICASE.

ProDom

PD003367; Uricase; 2.
[Domain structure / List of seq. sharing at least 1 domain]

TIGRFAMs

TIGR03383; urate_oxi; 1.

PROSITE

PS00366; URICASE; 1.

ProtoNet

P25689.

Phylogenomic databases

HOVERGEN

P25689; -.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Acetylation; Oxidoreductase; Peroxisome; Phosphoprotein; Purine metabolism.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed (By similarity).`
`CHAIN`	`2 304`	`303`	`Uricase.`	`PRO_0000165987`
`MOTIF`	`302 304`	`3`	`Microbody targeting signal (Potential).`
`ACT_SITE`	`187 187`		`Charge relay system (By similarity).`
`ACT_SITE`	`236 236`		`Charge relay system (By similarity).`
`MOD_RES`	`2 2`		`N-acetylalanine (By similarity).`
`MOD_RES`	`36 36`		`N6-acetyllysine (By similarity).`
`MOD_RES`	`39 39`		`Phosphoserine (By similarity).`
`MOD_RES`	`55 55`		`N6-acetyllysine (By similarity).`
`MOD_RES`	`118 118`		`N6-acetyllysine (By similarity).`
`MOD_RES`	`122 122`		`N6-acetyllysine (By similarity).`
`MOD_RES`	`164 164`		`N6-acetyllysine (By similarity).`
`MOD_RES`	`185 185`		`N6-acetyllysine (By similarity).`
`MOD_RES`	`221 221`		`N6-acetyllysine (By similarity).`
`MOD_RES`	`228 228`		`N6-acetyllysine (By similarity).`
`MOD_RES`	`232 232`		`Phosphoserine (By similarity).`
`MOD_RES`	`278 278`		`N6-acetyllysine (By similarity).`
`MOD_RES`	`291 291`		`N6-acetyllysine (By similarity).`
`MOD_RES`	`302 302`		`Phosphoserine (By similarity).`
`CONFLICT`	`154 154`		`H -> T (in Ref. 1; AAA35395).`

Sequence information

Length: 304 AA [This is the length of the unprocessed precursor]

Molecular weight: 34978 Da [This is the MW of the unprocessed precursor]

CRC64: D320AFF27870FAE5 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MADYHNNYKK NDELEFVRTG YGKDMVKVLH IQRDGKYHSI KEVATSVQLT LSSKKDYLHG 

        70         80         90        100        110        120 
DNSDIIPTDT IKNTVHVLAK FKGIKSIEAF GVNICEYFLS SFNHVIRAQV YVEEIPWKRL 

       130        140        150        160        170        180 
EKNGVKHVHA FIHTPTGTHF CEVEQLRSGP PVIHSGIKDL KVLKTTQSGF EGFIKDQFTT 

       190        200        210        220        230        240 
LPEVKDRCFA TQVYCKWRYH QCRDVDFEAT WGTIRDLVLE KFAGPYDKGE YSPSVQKTLY 

       250        260        270        280        290        300 
DIQVLSLSRV PEIEDMEISL PNIHYFNIDM SKMGLINKEE VLLPLDNPYG KITGTVKRKL 


SSRL

P25689 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools