ID   URIC2_CANLI             Reviewed;         301 AA.
AC   P34799;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Uricase-2 isozyme 2;
DE            EC=1.7.3.3;
DE   AltName: Full=Urate oxidase;
DE   AltName: Full=Uricase II clone pcClNUO-02;
OS   Canavalia lineata (Beach bean) (Dolichos lineatus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Canavalia.
OX   NCBI_TaxID=28957;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Root nodule;
RA   Bang K.H., An C.S.;
RT   "Nucleotide sequence and expression of cDNA clones encoding uricase II in
RT   Canavalia lineata.";
RL   Singmul Hakhoe Chi 36:415-423(1993).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X76287; CAA53905.1; -; mRNA.
DR   PIR; S38910; S38910.
DR   AlphaFoldDB; P34799; -.
DR   SMR; P34799; -.
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:0009877; P:nodulation; IEA:UniProtKB-KW.
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   2: Evidence at transcript level;
KW   Nodulation; Oxidoreductase; Peroxisome; Purine metabolism.
FT   CHAIN           1..301
FT                   /note="Uricase-2 isozyme 2"
FT                   /id="PRO_0000166001"
FT   MOTIF           299..301
FT                   /note="Microbody targeting signal"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        17
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:D0VWQ1"
FT   ACT_SITE        63
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:D0VWQ1"
FT   ACT_SITE        259
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:D0VWQ1"
FT   BINDING         63..64
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:D0VWQ1"
FT   BINDING         165
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:D0VWQ1"
FT   BINDING         182
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:D0VWQ1"
FT   BINDING         237..238
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:D0VWQ1"
SQ   SEQUENCE   301 AA;  34035 MW;  E90B96F7B5BD5294 CRC64;
     MAKEIVGGFK FDQRHGKERV RVARVWKTKK GGYFIVEWRV GISLLSDCVN SYVRDDNSDI
     VATDTMKNTV YAKAKECSEI LSVEDFAILL AKHFISFYKQ VTAAIVNIVE KPWERVSVDG
     QPHEHGFKLG SERHTAEAIV QKSGALQLTS GIEGLSLLKT TKSGFEGFIR DKYTALPETH
     ERMLATEVTA LWRYSYESLY SIPQKPLYFT DKYLEVKKVL ADTFFGPPNV GVYSPSVQNT
     LYLMAKAHSS IQLKMPNIHF LPVNISNKDG PIVKFDDDVY FPTDEPHGSI QASLSRLWSK
     L