URIC_DICDI
ID URIC_DICDI Reviewed; 287 AA.
AC Q54LT2;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Uricase;
DE EC=1.7.3.3;
DE AltName: Full=Urate oxidase;
GN Name=uox; ORFNames=DDB_G0286427;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: Catalyzes the oxidation of uric acid to 5-hydroxyisourate,
CC which is further processed to form (S)-allantoin. {ECO:0000250}.
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 {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the uricase family. {ECO:0000305}.
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DR EMBL; AAFI02000085; EAL64238.1; -; Genomic_DNA.
DR RefSeq; XP_637748.1; XM_632656.1.
DR AlphaFoldDB; Q54LT2; -.
DR SMR; Q54LT2; -.
DR STRING; 44689.DDB0231470; -.
DR PaxDb; Q54LT2; -.
DR PRIDE; Q54LT2; -.
DR EnsemblProtists; EAL64238; EAL64238; DDB_G0286427.
DR GeneID; 8625614; -.
DR KEGG; ddi:DDB_G0286427; -.
DR dictyBase; DDB_G0286427; uox.
DR eggNOG; KOG1599; Eukaryota.
DR HOGENOM; CLU_048151_0_0_1; -.
DR InParanoid; Q54LT2; -.
DR OMA; THRWTRM; -.
DR PhylomeDB; Q54LT2; -.
DR UniPathway; UPA00394; UER00650.
DR PRO; PR:Q54LT2; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0005777; C:peroxisome; IBA:GO_Central.
DR GO; GO:0045335; C:phagocytic vesicle; HDA:dictyBase.
DR GO; GO:0004846; F:urate oxidase activity; IBA:GO_Central.
DR GO; GO:0006145; P:purine nucleobase catabolic process; IBA:GO_Central.
DR GO; GO:0019628; P:urate catabolic process; IBA:GO_Central.
DR InterPro; IPR002042; Uricase.
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.
PE 3: Inferred from homology;
KW Oxidoreductase; Peroxisome; Purine metabolism; Reference proteome.
FT CHAIN 1..287
FT /note="Uricase"
FT /id="PRO_0000327520"
FT MOTIF 285..287
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 248
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 219..220
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:D0VWQ1"
SQ SEQUENCE 287 AA; 33031 MW; 386B01D1989EDA85 CRC64;
MATLIDNRYG KARVRVLRVF KGPNEYHKVF DFDCRVLLRG AEFSETYLTG DNSKVVATDT
MKNTVYVIAQ KEEFKSLEEY GILLGKHFLA TYSWVNGVEV VMRENQWRRI KTSNGKEQAH
SFQRDREIHS VTVTSSRDKS PVVVSGIDDL LIMKTTQSGF EGFHRDKYTS LKETKDRVFA
TVVTANWTYN TLSVDYSKVF EQFKLSVFDI FAQTYSRSVQ ETLFLIAKDV ISKVPQVEQV
HLSLPNKHAF GFDFSRLNIE NNQTVFQPVE EPSGLIEGTI KRSHSRL
