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Q00511 (URIC_ASPFL) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 107. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Uricase

EC=1.7.3.3
Alternative name(s):
Urate oxidase
Gene names
Name:uaZ
Synonyms:uox
OrganismAspergillus flavus
Taxonomic identifier5059 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length302 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the oxidation of uric acid to 5-hydroxyisourate, which is further processed to form (S)-allantoin.

Catalytic activity

Urate + O2 + H2O = 5-hydroxyisourate + H2O2.

Pathway

Purine metabolism; urate degradation; (S)-allantoin from urate: step 1/3.

Subunit structure

Homotetramer.

Subcellular location

Peroxisome.

Sequence similarities

Belongs to the uricase family.

Ontologies

Keywords
   Biological processPurine metabolism
   Cellular componentPeroxisome
   Molecular functionOxidoreductase
   PTMAcetylation
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological_processpurine nucleobase metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

urate catabolic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentperoxisome

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionurate oxidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 302301Uricase
PRO_0000165995

Regions

Region58 – 592Substrate binding By similarity
Region228 – 2292Substrate binding By similarity
Motif300 – 3023Microbody targeting signal Potential

Sites

Active site1771Charge relay system
Active site2291Charge relay system
Binding site1771Substrate By similarity

Amino acid modifications

Modified residue21N-acetylserine

Secondary structure

................................................ 302
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q00511 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: B4FAD4ED4EC121AE

FASTA30234,241
        10         20         30         40         50         60 
MSAVKAARYG KDNVRVYKVH KDEKTGVQTV YEMTVCVLLE GEIETSYTKA DNSVIVATDS 

        70         80         90        100        110        120 
IKNTIYITAK QNPVTPPELF GSILGTHFIE KYNHIHAAHV NIVCHRWTRM DIDGKPHPHS 

       130        140        150        160        170        180 
FIRDSEEKRN VQVDVVEGKG IDIKSSLSGL TVLKSTNSQF WGFLRDEYTT LKETWDRILS 

       190        200        210        220        230        240 
TDVDATWQWK NFSGLQEVRS HVPKFDATWA TAREVTLKTF AEDNSASVQA TMYKMAEQIL 

       250        260        270        280        290        300 
ARQQLIETVE YSLPNKHYFE IDLSWHKGLQ NTGKNAEVFA PQSDPNGLIK CTVGRSSLKS 


KL 

« Hide

References

[1]"Cloning and expression in Escherichia coli of the gene encoding Aspergillus flavus urate oxidase."
Legoux R., Delpech B., Dumont X., Guillemot J.-C., Ramond P., Shire D., Caput D., Ferrara P., Loison G.
J. Biol. Chem. 267:8565-8570(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], PARTIAL PROTEIN SEQUENCE.
Strain: ATCC 20047.
[2]"Crystal structure of the protein drug urate oxidase-inhibitor complex at 2.05-A resolution."
Colloc'h N., el Hajji M., Bachet B., L'Hermite G., Schiltz M., Prange T., Castro B., Mornon J.-P.
Nat. Struct. Biol. 4:947-952(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X61766 mRNA. Translation: CAA43896.1.
X61765 Genomic DNA. Translation: CAA43895.1.
PIRA38097.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1R4SX-ray1.80A2-302[»]
1R4UX-ray1.65A2-302[»]
1R51X-ray1.75A2-302[»]
1R56X-ray2.30A/B/C/D/E/F/G/H2-302[»]
1WRRX-ray1.64A2-302[»]
1WS2X-ray2.70A/B/C/D2-302[»]
1WS3X-ray3.20A/B/C/D2-302[»]
1XT4X-ray2.01A2-302[»]
1XXJX-ray2.80A/B/C/D2-302[»]
1XY3X-ray3.20A/B/C/D/E/F/G/H2-302[»]
2FUBX-ray2.30A2-302[»]
2FXLX-ray1.76A2-302[»]
2IBAX-ray1.50A2-302[»]
2IC0X-ray1.78A2-302[»]
2ICQX-ray1.75A2-302[»]
2PESX-ray1.60A2-296[»]
2ZKAX-ray1.61A2-302[»]
2ZKBX-ray1.61A2-302[»]
3BJPX-ray1.80A2-302[»]
3BK8X-ray1.60A2-302[»]
3CKSX-ray1.70A2-302[»]
3CKUX-ray1.70A2-302[»]
3F2MX-ray1.80A2-302[»]
3GKOX-ray1.60A2-302[»]
3L8WX-ray1.00A2-296[»]
3L9GX-ray1.75A2-296[»]
3LBGX-ray1.50A2-296[»]
3LD4X-ray1.35A2-296[»]
3OBPX-ray1.50A2-302[»]
3P9FX-ray1.70A2-302[»]
3P9OX-ray1.45A2-302[»]
3PJKX-ray1.70A2-302[»]
3PK3X-ray1.65A2-302[»]
3PK4X-ray1.85A2-302[»]
3PK5X-ray1.75A2-302[»]
3PK6X-ray1.80A2-302[»]
3PK8X-ray1.65A2-302[»]
3PKFX-ray1.65A2-302[»]
3PKGX-ray1.60A2-302[»]
3PKHX-ray1.71A2-302[»]
3PKKX-ray1.73A2-302[»]
3PKLX-ray1.75A2-302[»]
3PKSX-ray1.75A2-302[»]
3PKTX-ray1.75A2-302[»]
3PKUX-ray1.75A2-302[»]
3PLEX-ray1.60A2-302[»]
3PLGX-ray1.60A2-302[»]
3PLHX-ray1.80A2-302[»]
3PLIX-ray1.68A2-302[»]
3PLJX-ray1.73A2-302[»]
3PLMX-ray1.62A2-302[»]
4FSKX-ray1.98A2-302[»]
4N3MOther1.90A2-302[»]
4N9MOther2.30A2-302[»]
4N9SX-ray1.06A2-302[»]
4N9VX-ray1.10A2-302[»]
4OP6X-ray1.65A2-302[»]
4OP9X-ray1.58A2-302[»]
ProteinModelPortalQ00511.
SMRQ00511. Positions 3-300.
ModBaseSearch...
MobiDBSearch...

Chemistry

DrugBankDB00049. Rasburicase.

Proteomic databases

PRIDEQ00511.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGCOG3648.
HOGENOMHOG000250659.

Enzyme and pathway databases

BRENDA1.7.3.3. 506.
UniPathwayUPA00394; UER00650.

Family and domain databases

InterProIPR002042. Uricase.
IPR019842. Uricase_CS.
[Graphical view]
PfamPF01014. Uricase. 2 hits.
[Graphical view]
PIRSFPIRSF000241. Urate_oxidase. 1 hit.
PRINTSPR00093. URICASE.
TIGRFAMsTIGR03383. urate_oxi. 1 hit.
PROSITEPS00366. URICASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ00511.

Entry information

Entry nameURIC_ASPFL
AccessionPrimary (citable) accession number: Q00511
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 107 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways