URIC_EMENI
ID URIC_EMENI Reviewed; 301 AA.
AC P33282; C8V3D6; Q5AQG0;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Uricase;
DE EC=1.7.3.3 {ECO:0000269|PubMed:8226863};
DE AltName: Full=Urate oxidase;
GN Name=uaZ; ORFNames=AN9470;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=8226863; DOI=10.1016/s0021-9258(19)49474-x;
RA Oestreicher N., Scazzocchio C.;
RT "Sequence, regulation, and mutational analysis of the gene encoding urate
RT oxidase in Aspergillus nidulans.";
RL J. Biol. Chem. 268:23382-23389(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
CC -!- FUNCTION: Catalyzes the oxidation of uric acid to 5-hydroxyisourate,
CC which is further processed to form (S)-allantoin.
CC {ECO:0000269|PubMed:8226863}.
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:8226863};
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; X72210; CAA51009.1; -; Genomic_DNA.
DR EMBL; AACD01000194; EAA57588.1; -; Genomic_DNA.
DR EMBL; BN001301; CBF70468.1; -; Genomic_DNA.
DR PIR; A48879; A48879.
DR RefSeq; XP_868852.1; XM_863759.1.
DR AlphaFoldDB; P33282; -.
DR SMR; P33282; -.
DR STRING; 162425.CADANIAP00007060; -.
DR EnsemblFungi; CBF70468; CBF70468; ANIA_09470.
DR EnsemblFungi; EAA57588; EAA57588; AN9470.2.
DR GeneID; 3684067; -.
DR KEGG; ani:AN9470.2; -.
DR VEuPathDB; FungiDB:AN9470; -.
DR eggNOG; KOG1599; Eukaryota.
DR HOGENOM; CLU_048151_0_0_1; -.
DR InParanoid; P33282; -.
DR OMA; THRWTRM; -.
DR OrthoDB; 906540at2759; -.
DR UniPathway; UPA00394; UER00650.
DR Proteomes; UP000000560; Chromosome I.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IDA:AspGD.
DR GO; GO:0005777; C:peroxisome; IBA:GO_Central.
DR GO; GO:0004846; F:urate oxidase activity; IMP:AspGD.
DR GO; GO:0006145; P:purine nucleobase catabolic process; IMP:AspGD.
DR GO; GO:0019628; P:urate catabolic process; IBA:GO_Central.
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 Oxidoreductase; Peroxisome; Purine metabolism; Reference proteome.
FT CHAIN 1..301
FT /note="Uricase"
FT /id="PRO_0000165996"
FT MOTIF 299..301
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT ACT_SITE 11
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:D0VWQ1"
FT ACT_SITE 58
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:D0VWQ1"
FT ACT_SITE 257
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:D0VWQ1"
FT BINDING 58..59
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:D0VWQ1"
FT BINDING 160
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:D0VWQ1"
FT BINDING 177
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:D0VWQ1"
FT BINDING 228..229
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:D0VWQ1"
SQ SEQUENCE 301 AA; 34003 MW; BA46DD84925BCD9F CRC64;
MSTVAAARYG KDNVRVYKVH KDPKTGVQTV TEMTVCVLLE GEIDTSYTKA DNSVIVATDS
IKNTIFILAK QNPVTPPELF GSILGTHFIN KYKHIHVAHT NIITHRWTRL NIDGKPHSHS
FVRDSEETRN VQVDVTEGVG IDIKSSINKL TVLKSTGSQF WGFVRDEYTT LPEVWDRILS
TDVEATWAWK RFSGLDEVRG NVPKFDETWE AARNITLKTF AEEESASVQA TMYKMGEQIL
AYQPLLETVE YSLPNKHYFE IDLSWHKGLK NTGKDAEVFV PQTNPNGLIK CTVGRKSKAK
L
