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Reviewed, UniProtKB/Swiss-Prot P25689 (URIC_PAPHA)

Last modified June 16, 2009. Version 62. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Uricase
    EC=1.7.3.3
Alternative name(s):
    Urate oxidase
Gene names
Name: UOX
OrganismPapio hamadryas (Hamadryas baboon)
Taxonomic identifier9557 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Cercopithecidae › Cercopithecinae › Papio

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Protein attributes

Sequence length304 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

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General annotation (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.

Sequence similarities

Belongs to the uricase family.

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Ontologies

Keywords
   Biological processPurine metabolism
   Cellular componentPeroxisome
   Molecular functionOxidoreductase
   PTMAcetylation
Phosphoprotein
Gene Ontology (GO)
   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

purine base metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentperoxisome

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionurate oxidase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 304303Uricase
PRO_0000165987

Regions

Region235 – 2362Substrate binding By similarity
Motif302 – 3043Microbody targeting signal Potential

Sites

Active site1871Charge relay system By similarity
Active site2361Charge relay system By similarity
Binding site681Substrate By similarity
Binding site1871Substrate By similarity

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue361N6-acetyllysine By similarity
Modified residue391Phosphoserine By similarity
Modified residue551N6-acetyllysine By similarity
Modified residue1181N6-acetyllysine By similarity
Modified residue1221N6-acetyllysine By similarity
Modified residue1641N6-acetyllysine By similarity
Modified residue1851N6-acetyllysine By similarity
Modified residue2211N6-acetyllysine By similarity
Modified residue2281N6-acetyllysine By similarity
Modified residue2321Phosphoserine By similarity
Modified residue2781N6-acetyllysine By similarity
Modified residue2911N6-acetyllysine By similarity
Modified residue3021Phosphoserine By similarity

Experimental info

Sequence conflict1541H → T in AAA35395. Ref.1

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Sequences

Sequence LengthMass (Da)Tools
P25689-1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: D320AFF27870FAE5

FASTA30434,978
        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

« Hide

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References

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

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Cross-references

Sequence databases

M27694 mRNA. Translation: AAA35395.1.
AB074366 Genomic DNA. Translation: BAB91554.1.

3D structure databases

HSSPHSSP built from PDB template 1UOX based on UniProtKB Q00511.
ModBaseSearch...

Phylogenomic databases

HOVERGENP25689.

Enzyme and pathway databases

BRENDA1.7.3.3. 39388.

Family and domain databases

InterProIPR002042. Uricase.
IPR019842. Uricase_CS.
[Graphical view]
Gene3DG3DSA:3.10.270.10. Uricase. 1 hit.
PANTHERPTHR10395:SF1. Uricase. 1 hit.
PfamPF01014. Uricase. 2 hits.
[Graphical view]
PRINTSPR00093. URICASE.
ProDomPD003367. Uricase. 2 hits.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR03383. urate_oxi. 1 hit.
PROSITEPS00366. URICASE. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameURIC_PAPHA
AccessionPrimary (citable) accession number: P25689
Secondary accession number(s): Q7JJX1
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: January 23, 2007
Last modified: June 16, 2009
This is version 62 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents