URIC1_CANLI
ID URIC1_CANLI Reviewed; 308 AA.
AC P34798;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Uricase-2 isozyme 1;
DE EC=1.7.3.3;
DE AltName: Full=Urate oxidase;
DE AltName: Full=Uricase II clone pcClNUO-01;
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}.
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DR EMBL; X76286; CAA53904.1; -; mRNA.
DR PIR; S38911; S38911.
DR AlphaFoldDB; P34798; -.
DR SMR; P34798; -.
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..308
FT /note="Uricase-2 isozyme 1"
FT /id="PRO_0000166000"
FT MOTIF 306..308
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 266
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 308 AA; 34943 MW; 2968988B6FA1993D CRC64;
MAKEIVGGFK FDQRHGKERV QVARVWKTKQ GWYFIVEWRV GNSLLSDCVN SYVRDDNSDI
VATDTMKNTV YAKAKECSEI LSVEDFAILL AKHFISFYKQ VTAAIVNIVE KPWERVSVDG
QPHEHGFKLG SERHTAEAIV QKSGALQLTS GIEGLSLLKT TKSGFEGFIR DKYTALPETH
ERMLATEVTA LWRYSYESLY SIPQKPLYFT DKYLEVKKVL ADNFFGPPNV GVYSPSVQNT
LYLMAKAALN RFPEIASIQL KMPNIHFLPV NISNKDGPIV KFEADVYLPT DEPHGSIQAS
LRRLWSKL
