ID   URIC_CYBJA              Reviewed;         303 AA.
AC   P78609;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Uricase;
DE            EC=1.7.3.3;
DE   AltName: Full=Urate oxidase;
OS   Cyberlindnera jadinii (Torula yeast) (Pichia jadinii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Phaffomycetaceae; Cyberlindnera.
OX   NCBI_TaxID=4903;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 9950 / CBS 5609 / DSM 2361 / NBRC 0998 / NRRL Y-900;
RX   PubMed=8982864; DOI=10.1093/oxfordjournals.jbchem.a021514;
RA   Koyama Y., Ichikawa T., Nakano E.;
RT   "Cloning, sequence analysis, and expression in Escherichia coli of the gene
RT   encoding the Candida utilis urate oxidase (uricase).";
RL   J. Biochem. 120:969-973(1996).
CC   -!- FUNCTION: Catalyzes the oxidation of uric acid to 5-hydroxyisourate,
CC       which is further processed to form (S)-allantoin.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O2 + urate = 5-hydroxyisourate + H2O2;
CC         Xref=Rhea:RHEA:21368, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16240, ChEBI:CHEBI:17775, ChEBI:CHEBI:18072; EC=1.7.3.3;
CC   -!- PATHWAY: Purine metabolism; urate degradation; (S)-allantoin from
CC       urate: step 1/3.
CC   -!- SUBCELLULAR LOCATION: Peroxisome.
CC   -!- SIMILARITY: Belongs to the uricase family. {ECO:0000305}.
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DR   EMBL; D32043; BAA06804.1; -; Genomic_DNA.
DR   PIR; JC5140; JC5140.
DR   AlphaFoldDB; P78609; -.
DR   SMR; P78609; -.
DR   BRENDA; 1.7.3.3; 1148.
DR   UniPathway; UPA00394; UER00650.
DR   GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR   GO; GO:0004846; F:urate oxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006144; P:purine nucleobase metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0019628; P:urate catabolic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR002042; Uricase.
DR   InterPro; IPR019842; Uricase_CS.
DR   PANTHER; PTHR42874; PTHR42874; 1.
DR   Pfam; PF01014; Uricase; 2.
DR   PIRSF; PIRSF000241; Urate_oxidase; 1.
DR   PRINTS; PR00093; URICASE.
DR   TIGRFAMs; TIGR03383; urate_oxi; 1.
DR   PROSITE; PS00366; URICASE; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase; Peroxisome; Purine metabolism.
FT   CHAIN           1..303
FT                   /note="Uricase"
FT                   /id="PRO_0000165997"
FT   MOTIF           301..303
FT                   /note="Microbody targeting signal"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        12
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:D0VWQ1"
FT   ACT_SITE        60
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:D0VWQ1"
FT   ACT_SITE        263
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:D0VWQ1"
FT   BINDING         60..61
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:D0VWQ1"
FT   BINDING         162
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:D0VWQ1"
FT   BINDING         179
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:D0VWQ1"
FT   BINDING         234..235
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:D0VWQ1"
SQ   SEQUENCE   303 AA;  34195 MW;  0A491A4E6A39EDBF CRC64;
     MSTTLSSSTY GKDNVKFLKV KKDPQNPKKQ EVMEATVTCL LEGGFDTSYT EADNSSIVPT
     DTVKNTILVL AKTTEIWPIE RFAAKLATHF VEKYSHVSGV SVKIVQDRWV KYAVDGKPHD
     HSFIHEGGEK RITDLYYKRS GDYKLSSAIK DLTVLKSTGS MFYGYNKCDF TTLQPTTDRI
     LSTDVDATWV WDNKKIGSVY DIAKAADKGI FDNVYNQARE ITLTTFALEN SPSVQATMFN
     MATQILEKAC SVYSVSYALP NKHYFLIDLK WKGLENDNEL FYPSPHPNGL IKCTVVRKEK
     TKL