URIC_SCHPO
ID URIC_SCHPO Reviewed; 296 AA.
AC O74409;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Uricase;
DE EC=1.7.3.3;
DE AltName: Full=Urate oxidase;
GN ORFNames=SPCC1223.09;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP CATALYTIC ACTIVITY, AND FUNCTION.
RX PubMed=4020341; DOI=10.1099/00221287-131-3-527;
RA Fluri R., Kinghorn J.R.;
RT "The all2 gene is required for the induction of the purine deamination
RT pathway in Schizosaccharomyces pombe.";
RL J. Gen. Microbiol. 131:527-532(1985).
RN [3]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- FUNCTION: Catalyzes the oxidation of uric acid to 5-hydroxyisourate,
CC which is further processed to form (S)-allantoin.
CC {ECO:0000269|PubMed:4020341}.
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 Evidence={ECO:0000269|PubMed:4020341};
CC -!- PATHWAY: Purine metabolism; urate degradation; (S)-allantoin from
CC urate: step 1/3.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000250}. Cytoplasm
CC {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the uricase family. {ECO:0000305}.
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DR EMBL; CU329672; CAA20878.1; -; Genomic_DNA.
DR PIR; T40869; T40869.
DR RefSeq; NP_588354.1; NM_001023345.2.
DR AlphaFoldDB; O74409; -.
DR SMR; O74409; -.
DR BioGRID; 275531; 1.
DR STRING; 4896.SPCC1223.09.1; -.
DR MaxQB; O74409; -.
DR PaxDb; O74409; -.
DR EnsemblFungi; SPCC1223.09.1; SPCC1223.09.1:pep; SPCC1223.09.
DR GeneID; 2538957; -.
DR KEGG; spo:SPCC1223.09; -.
DR PomBase; SPCC1223.09; -.
DR VEuPathDB; FungiDB:SPCC1223.09; -.
DR eggNOG; KOG1599; Eukaryota.
DR HOGENOM; CLU_048151_0_0_1; -.
DR InParanoid; O74409; -.
DR OMA; THRWTRM; -.
DR PhylomeDB; O74409; -.
DR UniPathway; UPA00394; UER00650.
DR PRO; PR:O74409; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0005777; C:peroxisome; IBA:GO_Central.
DR GO; GO:0004846; F:urate oxidase activity; EXP:PomBase.
DR GO; GO:0006145; P:purine nucleobase catabolic process; IBA:GO_Central.
DR GO; GO:0019628; P:urate catabolic process; IBA:GO_Central.
DR GO; GO:0019627; P:urea metabolic process; IC:PomBase.
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 1: Evidence at protein level;
KW Cytoplasm; Nucleus; Oxidoreductase; Peroxisome; Purine metabolism;
KW Reference proteome.
FT CHAIN 1..296
FT /note="Uricase"
FT /id="PRO_0000165998"
FT ACT_SITE 14
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:D0VWQ1"
FT ACT_SITE 61
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:D0VWQ1"
FT ACT_SITE 258
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:D0VWQ1"
FT BINDING 61..62
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:D0VWQ1"
FT BINDING 163
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:D0VWQ1"
FT BINDING 180
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:D0VWQ1"
FT BINDING 229..230
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:D0VWQ1"
SQ SEQUENCE 296 AA; 33610 MW; C7C8DF71A7CD1EDF CRC64;
MSETTYVKQC AYGKTLVRFM KKDICPKTKT HTVYEMDVQS LLTGELEESY TKADNSIVVP
TDTQKNTIYV FAKNNDVSVP EVFAAKLAKH FVDKYKHIHG AALDITITPW TRMEVQGKPH
SHSFIRNPGE TRKTHVVFSE GKGFDVVSSL KDVLVLKSTG SGFTNFHKCE FTTLPEVTDR
IFSTSIDCNY TFKHFDTFEE LAGFDFNSIY EKVKEITLET FALDDSESVQ ATMYKMADTI
INTYPAINEV YYALPNKHYF EINLAPFNID NLGSNCSLYQ PQAYPSGYIT CTVARK
