URIC_ASPFL
ID URIC_ASPFL Reviewed; 302 AA.
AC Q00511;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Uricase;
DE EC=1.7.3.3;
DE AltName: Full=Urate oxidase;
GN Name=uaZ; Synonyms=uox;
OS Aspergillus flavus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=5059;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], PARTIAL PROTEIN SEQUENCE, AND
RP ACETYLATION AT SER-2.
RC STRAIN=ATCC 20047;
RX PubMed=1339455; DOI=10.1016/s0021-9258(18)42480-5;
RA Legoux R., Delpech B., Dumont X., Guillemot J.-C., Ramond P., Shire D.,
RA Caput D., Ferrara P., Loison G.;
RT "Cloning and expression in Escherichia coli of the gene encoding
RT Aspergillus flavus urate oxidase.";
RL J. Biol. Chem. 267:8565-8570(1992).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH INHIBITOR
RP 8-AZAXANTHINE, AND SUBUNIT.
RX PubMed=9360612; DOI=10.1038/nsb1197-947;
RA Colloc'h N., el Hajji M., Bachet B., L'Hermite G., Schiltz M., Prange T.,
RA Castro B., Mornon J.-P.;
RT "Crystal structure of the protein drug urate oxidase-inhibitor complex at
RT 2.05-A resolution.";
RL Nat. Struct. Biol. 4:947-952(1997).
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 -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:9360612}.
CC -!- SUBCELLULAR LOCATION: Peroxisome.
CC -!- SIMILARITY: Belongs to the uricase family. {ECO:0000305}.
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DR EMBL; X61766; CAA43896.1; -; mRNA.
DR EMBL; X61765; CAA43895.1; -; Genomic_DNA.
DR PIR; A38097; A38097.
DR PDB; 1R4S; X-ray; 1.80 A; A=2-302.
DR PDB; 1R4U; X-ray; 1.65 A; A=2-302.
DR PDB; 1R51; X-ray; 1.75 A; A=2-302.
DR PDB; 1R56; X-ray; 2.30 A; A/B/C/D/E/F/G/H=2-302.
DR PDB; 1WRR; X-ray; 1.64 A; A=2-302.
DR PDB; 1WS2; X-ray; 2.70 A; A/B/C/D=2-302.
DR PDB; 1WS3; X-ray; 3.20 A; A/B/C/D=2-302.
DR PDB; 1XT4; X-ray; 2.01 A; A=2-302.
DR PDB; 1XXJ; X-ray; 2.80 A; A/B/C/D=2-302.
DR PDB; 1XY3; X-ray; 3.20 A; A/B/C/D/E/F/G/H=2-302.
DR PDB; 2FUB; X-ray; 2.30 A; A=2-302.
DR PDB; 2FXL; X-ray; 1.76 A; A=2-302.
DR PDB; 2IBA; X-ray; 1.50 A; A=2-302.
DR PDB; 2IC0; X-ray; 1.78 A; A=2-302.
DR PDB; 2ICQ; X-ray; 1.75 A; A=2-302.
DR PDB; 2PES; X-ray; 1.60 A; A=2-296.
DR PDB; 2ZKA; X-ray; 1.61 A; A=2-302.
DR PDB; 2ZKB; X-ray; 1.61 A; A=2-302.
DR PDB; 3BJP; X-ray; 1.80 A; A=2-302.
DR PDB; 3BK8; X-ray; 1.60 A; A=2-302.
DR PDB; 3CKS; X-ray; 1.70 A; A=2-302.
DR PDB; 3CKU; X-ray; 1.70 A; A=2-302.
DR PDB; 3F2M; X-ray; 1.80 A; A=2-302.
DR PDB; 3GKO; X-ray; 1.60 A; A=2-302.
DR PDB; 3L8W; X-ray; 1.00 A; A=2-296.
DR PDB; 3L9G; X-ray; 1.75 A; A=2-296.
DR PDB; 3LBG; X-ray; 1.50 A; A=2-296.
DR PDB; 3LD4; X-ray; 1.35 A; A=2-296.
DR PDB; 3OBP; X-ray; 1.50 A; A=2-302.
DR PDB; 3P9F; X-ray; 1.70 A; A=2-302.
DR PDB; 3P9O; X-ray; 1.45 A; A=2-302.
DR PDB; 3PJK; X-ray; 1.70 A; A=2-302.
DR PDB; 3PK3; X-ray; 1.65 A; A=2-302.
DR PDB; 3PK4; X-ray; 1.85 A; A=2-302.
DR PDB; 3PK5; X-ray; 1.75 A; A=2-302.
DR PDB; 3PK6; X-ray; 1.80 A; A=2-302.
DR PDB; 3PK8; X-ray; 1.65 A; A=2-302.
DR PDB; 3PKF; X-ray; 1.65 A; A=2-302.
DR PDB; 3PKG; X-ray; 1.60 A; A=2-302.
DR PDB; 3PKH; X-ray; 1.71 A; A=2-302.
DR PDB; 3PKK; X-ray; 1.73 A; A=2-302.
DR PDB; 3PKL; X-ray; 1.75 A; A=2-302.
DR PDB; 3PKS; X-ray; 1.75 A; A=2-302.
DR PDB; 3PKT; X-ray; 1.75 A; A=2-302.
DR PDB; 3PKU; X-ray; 1.75 A; A=2-302.
DR PDB; 3PLE; X-ray; 1.60 A; A=2-302.
DR PDB; 3PLG; X-ray; 1.60 A; A=2-302.
DR PDB; 3PLH; X-ray; 1.80 A; A=2-302.
DR PDB; 3PLI; X-ray; 1.68 A; A=2-302.
DR PDB; 3PLJ; X-ray; 1.73 A; A=2-302.
DR PDB; 3PLM; X-ray; 1.62 A; A=2-302.
DR PDB; 4CW0; X-ray; 1.50 A; A=2-302.
DR PDB; 4CW2; X-ray; 1.32 A; A=2-302.
DR PDB; 4CW3; X-ray; 1.34 A; A=2-302.
DR PDB; 4CW6; X-ray; 1.28 A; A=2-302.
DR PDB; 4D12; X-ray; 1.40 A; A=1-302.
DR PDB; 4D13; X-ray; 1.30 A; A=1-302.
DR PDB; 4D17; X-ray; 1.30 A; A=1-302.
DR PDB; 4D19; X-ray; 1.35 A; A=1-302.
DR PDB; 4FSK; X-ray; 1.98 A; A=2-302.
DR PDB; 4N3M; Other; 1.90 A; A=2-302.
DR PDB; 4N9M; Other; 2.30 A; A=2-302.
DR PDB; 4N9S; X-ray; 1.06 A; A=2-302.
DR PDB; 4N9V; X-ray; 1.10 A; A=2-302.
DR PDB; 4OP6; X-ray; 1.65 A; A=2-302.
DR PDB; 4OP9; X-ray; 1.58 A; A=2-302.
DR PDB; 4OQC; X-ray; 1.30 A; A=2-302.
DR PDB; 4POE; X-ray; 1.07 A; A=2-302.
DR PDB; 4PR8; X-ray; 1.16 A; A=2-296.
DR PDB; 4PUV; X-ray; 1.30 A; A=2-302.
DR PDB; 5FRC; X-ray; 1.44 A; A=2-302.
DR PDB; 6I9X; X-ray; 1.60 A; A=2-302.
DR PDB; 6I9Z; X-ray; 1.60 A; A=2-302.
DR PDB; 6IA1; X-ray; 2.36 A; A=2-302.
DR PDB; 6IA3; X-ray; 1.69 A; A=2-302.
DR PDB; 6IA9; X-ray; 1.80 A; A/B=2-302.
DR PDB; 6IC1; X-ray; 1.10 A; A=2-302.
DR PDB; 6RGM; X-ray; 1.50 A; A=2-302.
DR PDB; 6RGT; X-ray; 1.60 A; A=1-302.
DR PDB; 7A0L; Other; 1.33 A; A=1-302.
DR PDB; 7P0C; X-ray; 2.15 A; A=2-302.
DR PDB; 7P0D; X-ray; 2.40 A; A=2-302.
DR PDB; 7P0G; X-ray; 1.90 A; A=2-302.
DR PDB; 7PUF; X-ray; 1.86 A; A/B=2-296.
DR PDB; 7PWN; X-ray; 1.64 A; A/B=2-296.
DR PDB; 7Q09; X-ray; 2.19 A; A/B=2-296.
DR PDBsum; 1R4S; -.
DR PDBsum; 1R4U; -.
DR PDBsum; 1R51; -.
DR PDBsum; 1R56; -.
DR PDBsum; 1WRR; -.
DR PDBsum; 1WS2; -.
DR PDBsum; 1WS3; -.
DR PDBsum; 1XT4; -.
DR PDBsum; 1XXJ; -.
DR PDBsum; 1XY3; -.
DR PDBsum; 2FUB; -.
DR PDBsum; 2FXL; -.
DR PDBsum; 2IBA; -.
DR PDBsum; 2IC0; -.
DR PDBsum; 2ICQ; -.
DR PDBsum; 2PES; -.
DR PDBsum; 2ZKA; -.
DR PDBsum; 2ZKB; -.
DR PDBsum; 3BJP; -.
DR PDBsum; 3BK8; -.
DR PDBsum; 3CKS; -.
DR PDBsum; 3CKU; -.
DR PDBsum; 3F2M; -.
DR PDBsum; 3GKO; -.
DR PDBsum; 3L8W; -.
DR PDBsum; 3L9G; -.
DR PDBsum; 3LBG; -.
DR PDBsum; 3LD4; -.
DR PDBsum; 3OBP; -.
DR PDBsum; 3P9F; -.
DR PDBsum; 3P9O; -.
DR PDBsum; 3PJK; -.
DR PDBsum; 3PK3; -.
DR PDBsum; 3PK4; -.
DR PDBsum; 3PK5; -.
DR PDBsum; 3PK6; -.
DR PDBsum; 3PK8; -.
DR PDBsum; 3PKF; -.
DR PDBsum; 3PKG; -.
DR PDBsum; 3PKH; -.
DR PDBsum; 3PKK; -.
DR PDBsum; 3PKL; -.
DR PDBsum; 3PKS; -.
DR PDBsum; 3PKT; -.
DR PDBsum; 3PKU; -.
DR PDBsum; 3PLE; -.
DR PDBsum; 3PLG; -.
DR PDBsum; 3PLH; -.
DR PDBsum; 3PLI; -.
DR PDBsum; 3PLJ; -.
DR PDBsum; 3PLM; -.
DR PDBsum; 4CW0; -.
DR PDBsum; 4CW2; -.
DR PDBsum; 4CW3; -.
DR PDBsum; 4CW6; -.
DR PDBsum; 4D12; -.
DR PDBsum; 4D13; -.
DR PDBsum; 4D17; -.
DR PDBsum; 4D19; -.
DR PDBsum; 4FSK; -.
DR PDBsum; 4N3M; -.
DR PDBsum; 4N9M; -.
DR PDBsum; 4N9S; -.
DR PDBsum; 4N9V; -.
DR PDBsum; 4OP6; -.
DR PDBsum; 4OP9; -.
DR PDBsum; 4OQC; -.
DR PDBsum; 4POE; -.
DR PDBsum; 4PR8; -.
DR PDBsum; 4PUV; -.
DR PDBsum; 5FRC; -.
DR PDBsum; 6I9X; -.
DR PDBsum; 6I9Z; -.
DR PDBsum; 6IA1; -.
DR PDBsum; 6IA3; -.
DR PDBsum; 6IA9; -.
DR PDBsum; 6IC1; -.
DR PDBsum; 6RGM; -.
DR PDBsum; 6RGT; -.
DR PDBsum; 7A0L; -.
DR PDBsum; 7P0C; -.
DR PDBsum; 7P0D; -.
DR PDBsum; 7P0G; -.
DR PDBsum; 7PUF; -.
DR PDBsum; 7PWN; -.
DR PDBsum; 7Q09; -.
DR AlphaFoldDB; Q00511; -.
DR SASBDB; Q00511; -.
DR SMR; Q00511; -.
DR iPTMnet; Q00511; -.
DR PRIDE; Q00511; -.
DR EnsemblFungi; EED52707; EED52707; AFLA_044090.
DR VEuPathDB; FungiDB:AFLA_044090; -.
DR VEuPathDB; FungiDB:F9C07_2229599; -.
DR OMA; THRWTRM; -.
DR BRENDA; 1.7.3.3; 506.
DR UniPathway; UPA00394; UER00650.
DR EvolutionaryTrace; Q00511; -.
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 1: Evidence at protein level;
KW 3D-structure; Acetylation; Direct protein sequencing; Oxidoreductase;
KW Peroxisome; Purine metabolism.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..302
FT /note="Uricase"
FT /id="PRO_0000165995"
FT MOTIF 300..302
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:0000305|PubMed:9360612"
FT BINDING 160
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:9360612"
FT BINDING 177
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:9360612"
FT BINDING 228..229
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:9360612"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000305|PubMed:1339455"
FT STRAND 9..21
FT /evidence="ECO:0007829|PDB:3L8W"
FT TURN 23..25
FT /evidence="ECO:0007829|PDB:3L8W"
FT STRAND 28..42
FT /evidence="ECO:0007829|PDB:3L8W"
FT HELIX 44..48
FT /evidence="ECO:0007829|PDB:3L8W"
FT HELIX 52..54
FT /evidence="ECO:0007829|PDB:3L8W"
FT HELIX 58..71
FT /evidence="ECO:0007829|PDB:3L8W"
FT HELIX 77..91
FT /evidence="ECO:0007829|PDB:3L8W"
FT STRAND 95..105
FT /evidence="ECO:0007829|PDB:3L8W"
FT STRAND 108..112
FT /evidence="ECO:0007829|PDB:3L8W"
FT STRAND 115..122
FT /evidence="ECO:0007829|PDB:3L8W"
FT STRAND 128..136
FT /evidence="ECO:0007829|PDB:3L8W"
FT TURN 137..139
FT /evidence="ECO:0007829|PDB:3L8W"
FT STRAND 140..158
FT /evidence="ECO:0007829|PDB:3L8W"
FT STRAND 174..176
FT /evidence="ECO:0007829|PDB:3L8W"
FT STRAND 179..189
FT /evidence="ECO:0007829|PDB:3L8W"
FT STRAND 192..194
FT /evidence="ECO:0007829|PDB:3L8W"
FT HELIX 195..200
FT /evidence="ECO:0007829|PDB:3L8W"
FT HELIX 202..222
FT /evidence="ECO:0007829|PDB:3L8W"
FT HELIX 228..242
FT /evidence="ECO:0007829|PDB:3L8W"
FT STRAND 246..255
FT /evidence="ECO:0007829|PDB:3L8W"
FT STRAND 258..260
FT /evidence="ECO:0007829|PDB:3L8W"
FT TURN 264..268
FT /evidence="ECO:0007829|PDB:3L8W"
FT HELIX 273..275
FT /evidence="ECO:0007829|PDB:3L8W"
FT STRAND 279..281
FT /evidence="ECO:0007829|PDB:3L8W"
FT STRAND 287..294
FT /evidence="ECO:0007829|PDB:3L8W"
SQ SEQUENCE 302 AA; 34241 MW; B4FAD4ED4EC121AE CRC64;
MSAVKAARYG KDNVRVYKVH KDEKTGVQTV YEMTVCVLLE GEIETSYTKA DNSVIVATDS
IKNTIYITAK QNPVTPPELF GSILGTHFIE KYNHIHAAHV NIVCHRWTRM DIDGKPHPHS
FIRDSEEKRN VQVDVVEGKG IDIKSSLSGL TVLKSTNSQF WGFLRDEYTT LKETWDRILS
TDVDATWQWK NFSGLQEVRS HVPKFDATWA TAREVTLKTF AEDNSASVQA TMYKMAEQIL
ARQQLIETVE YSLPNKHYFE IDLSWHKGLQ NTGKNAEVFA PQSDPNGLIK CTVGRSSLKS
KL
