URIC_PHAVU
ID URIC_PHAVU Reviewed; 308 AA.
AC P53763; O49966;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1999, sequence version 2.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Uricase-2;
DE EC=1.7.3.3;
DE AltName: Full=Nodule-specific uricase;
DE AltName: Full=Urate oxidase;
DE AltName: Full=Uricase II;
GN Name=URIII;
OS Phaseolus vulgaris (Kidney bean) (French bean).
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; Phaseolus.
OX NCBI_TaxID=3885;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Negro Jamapa; TISSUE=Root nodule;
RX PubMed=9414545; DOI=10.1104/pp.115.4.1307;
RA Capote-Mainez N., Sanchez F.;
RT "Characterization of the common bean uricase II and its expression in
RT organs other than nodules.";
RL Plant Physiol. 115:1307-1317(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 54-308.
RC STRAIN=cv. Tendergreen; TISSUE=Root nodule;
RX PubMed=7843336; DOI=10.1007/bf01964927;
RA Papadopoulou K., Roussis A., Kuin H., Katinakis P.;
RT "Expression pattern of uricase II gene during root nodule development in
RT Phaseolus vulgaris.";
RL Experientia 51:90-94(1995).
RN [3]
RP CHARACTERIZATION, AND INDUCTION.
RC STRAIN=cv. Negro Jamapa; TISSUE=Root nodule;
RX PubMed=16665575; DOI=10.1104/pp.84.4.1143;
RA Sanchez F., Campos F., Padilla J., Bonneville J.-M., Enriquez C., Caput D.;
RT "Purification, cDNA cloning, and developmental expression of the nodule-
RT specific uricase from Phaseolus vulgaris L.";
RL Plant Physiol. 84:1143-1147(1987).
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:0000250}.
CC -!- SUBCELLULAR LOCATION: Peroxisome.
CC -!- TISSUE SPECIFICITY: Expressed predominantly in the uninfected cells of
CC the central tissue of the root nodule. Also expressed in the nodule
CC parenchyma cells and vascular tissue, in the roots, stems and leaves of
CC uninfected adult plants, and in the cotyledons, roots and hypocotyls of
CC developing seedlings. Localized to the metaxylem parenchyma cells and
CC phloem fibers of developing roots. {ECO:0000269|PubMed:9414545}.
CC -!- DEVELOPMENTAL STAGE: Detected in cotyledons and roots at 1 day
CC postimbibition, reaching a maximum at 4 days postimbibition. Hypocotyl
CC levels are constant from 3 to 10 days postimbibition.
CC {ECO:0000269|PubMed:9414545}.
CC -!- INDUCTION: In root nodules after infection by Rhizobium. Nodule uricase
CC II levels increase from 11 to around 25 days after inoculation, then
CC fall slightly. {ECO:0000269|PubMed:16665575}.
CC -!- SIMILARITY: Belongs to the uricase family. {ECO:0000305}.
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DR EMBL; U72663; AAB97726.1; -; mRNA.
DR EMBL; S75621; AAB33324.2; -; mRNA.
DR PIR; T12074; T12074.
DR AlphaFoldDB; P53763; -.
DR SMR; P53763; -.
DR STRING; 3885.XP_007145381.1; -.
DR PRIDE; P53763; -.
DR ProMEX; P53763; -.
DR eggNOG; KOG1599; Eukaryota.
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 1: Evidence at protein level;
KW Nodulation; Oxidoreductase; Peroxisome; Purine metabolism.
FT CHAIN 1..308
FT /note="Uricase-2"
FT /id="PRO_0000166002"
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"
FT CONFLICT 81
FT /note="Missing (in Ref. 2; AAB33324)"
FT /evidence="ECO:0000305"
FT CONFLICT 140
FT /note="V -> L (in Ref. 2; AAB33324)"
FT /evidence="ECO:0000305"
FT CONFLICT 144
FT /note="G -> C (in Ref. 2; AAB33324)"
FT /evidence="ECO:0000305"
FT CONFLICT 171
FT /note="N -> D (in Ref. 2; AAB33324)"
FT /evidence="ECO:0000305"
FT CONFLICT 228..230
FT /note="PNR -> TKQ (in Ref. 2; AAB33324)"
FT /evidence="ECO:0000305"
FT CONFLICT 258
FT /note="V -> C (in Ref. 2; AAB33324)"
FT /evidence="ECO:0000305"
FT CONFLICT 302..307
FT /note="SRVWSK -> LQLFYIL (in Ref. 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 308 AA; 35127 MW; EE7F6050BD8F228C CRC64;
MAQEVVEGFK FEQRHGKERV RVARVWRTPQ GRHFVVEWRV GITLFSDCVN SYLRDDNSDI
VATDTMKNTV YAKAKECSDI LSVEDFAILL AKHFVSFYKK VTGAIVNIVE KPWERVIVDG
QPHQHGFTLG SEKHTTEAIV QKSGSLQLTS GIEGLSVLKT TQSGFENFIR NKYTALPDTR
ERILATEVTA LWRYSYESLY NLPQKPLYFT DKYLEVKKVL ADTFFGPPNR GVYSPSVQNT
LYLMAKATLN RFPDIAYVHL KMPNLHFLPV NISSKDGPIV KFEDDVYLPT DEPHGSIEAS
LSRVWSKL
