ID   URIC2_SOYBN             Reviewed;         309 AA.
AC   O04104;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Uricase-2 isozyme 2;
DE            EC=1.7.3.3;
DE   AltName: Full=Nodulin 35;
DE            Short=N-35;
DE   AltName: Full=Non-symbiotic uricase;
DE   AltName: Full=Urate oxidase;
DE   AltName: Full=Uricase II isozyme 2;
OS   Glycine max (Soybean) (Glycine hispida).
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; Glycine;
OC   Glycine subgen. Soja.
OX   NCBI_TaxID=3847;
RN   [1]
RP   NUCLEOTIDE SEQUENCE, AND PROTEIN SEQUENCE OF 245-262.
RC   STRAIN=cv. Dare;
RX   PubMed=16593585; DOI=10.1073/pnas.82.15.5040;
RA   Nguyen T., Zelechowska M., Foster V., Bergmann H., Verma D.P.S.;
RT   "Primary structure of the soybean nodulin-35 gene encoding uricase II
RT   localized in the peroxisome of uninfected cells of nodules.";
RL   Proc. Natl. Acad. Sci. U.S.A. 82:5040-5044(1985).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC   STRAIN=cv. Akisengoku; TISSUE=Root nodule;
RX   PubMed=9245835; DOI=10.1094/mpmi.1997.10.6.735;
RA   Takane K., Tajima S., Kouchi H.;
RT   "Two distinct uricase II (nodulin 35) genes are differentially expressed in
RT   soybean plants.";
RL   Mol. Plant Microbe Interact. 10:735-741(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:0000250}.
CC   -!- SUBCELLULAR LOCATION: Peroxisome.
CC   -!- SIMILARITY: Belongs to the uricase family. {ECO:0000305}.
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DR   EMBL; M10594; AAA33994.1; -; Genomic_DNA.
DR   EMBL; AB002807; BAA19670.1; -; Genomic_DNA.
DR   EMBL; AB002809; BAA19672.1; -; mRNA.
DR   RefSeq; NP_001235948.1; NM_001249019.1.
DR   AlphaFoldDB; O04104; -.
DR   SMR; O04104; -.
DR   STRING; 3847.GLYMA20G17440.1; -.
DR   GeneID; 100037445; -.
DR   KEGG; gmx:100037445; -.
DR   eggNOG; KOG1599; Eukaryota.
DR   HOGENOM; CLU_048151_1_1_1; -.
DR   InParanoid; O04104; -.
DR   OrthoDB; 906540at2759; -.
DR   UniPathway; UPA00394; UER00650.
DR   Proteomes; UP000008827; Unplaced.
DR   Genevisible; O04104; GM.
DR   GO; GO:0005777; C:peroxisome; IBA:GO_Central.
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   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   Direct protein sequencing; Oxidoreductase; Peroxisome; Purine metabolism;
KW   Reference proteome.
FT   CHAIN           1..309
FT                   /note="Uricase-2 isozyme 2"
FT                   /id="PRO_0000166004"
FT   ACT_SITE        18
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:D0VWQ1"
FT   ACT_SITE        64
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:D0VWQ1"
FT   ACT_SITE        267
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:D0VWQ1"
FT   BINDING         64..65
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:D0VWQ1"
FT   BINDING         166
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:D0VWQ1"
FT   BINDING         183
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:D0VWQ1"
FT   BINDING         238..239
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:D0VWQ1"
FT   CONFLICT        208
FT                   /note="L -> F (in Ref. 1; AAA33994)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   309 AA;  35137 MW;  81B8F8F7ACAA00A9 CRC64;
     MAQQEVVEGF KFEQRHGKER VRVARVWKTR QGQHFVVEWR VGITLFSDCV NSYLRDDNSD
     IVATDTMKNT VYAKAKECSD ILSAEDFAIL LAKHFVSFYK KVTGAIVNIV EKPWERVIVD
     GQPHEHGFKL GSEKHTTEAI VQKSGSLQLT SGIEGLSVLK TTQSGFVNFI RDKYTALPDT
     RERILATEVT ALWRYSYESQ YSLPQKPLYF TEKYQEVKKV LADTFFGPPN GGVYSPSVQN
     TLYLMAKATL NRFPDIAYVS LKMPNLHFLP VNISNKDGPI VKFEDDVYLP TDEPHGSIQA
     SLSRLWSKL