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   16-JUN-2009, entry version 58.
DE   RecName: Full=Uricase-2 isozyme 2;
DE            EC=1.7.3.3;
DE   AltName: Full=Uricase II isozyme 2;
DE   AltName: Full=Urate oxidase;
DE   AltName: Full=Nodulin 35;
DE            Short=N-35;
DE   AltName: Full=Non-symbiotic uricase;
OS   Glycine max (Soybean).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   rosids; eurosids I; Fabales; Fabaceae; Papilionoideae; Phaseoleae;
OC   Glycine.
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
RT   expressed in soybean plants.";
RL   Mol. Plant Microbe Interact. 10:735-741(1997).
CC   -!- FUNCTION: Catalyzes the oxidation of uric acid to 5-
CC       hydroxyisourate, which spontaneously decomposes to form allantoin.
CC   -!- CATALYTIC ACTIVITY: Urate + O(2) + H(2)O = 5-hydroxyisourate +
CC       H(2)O(2).
CC   -!- PATHWAY: Purine metabolism; uric acid degradation; (S)-allantoin
CC       from uric acid: step 1/3.
CC   -!- SUBUNIT: Homotetramer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Peroxisome.
CC   -!- SIMILARITY: Belongs to the uricase family.
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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   UniGene; Gma.29861; -.
DR   HSSP; Q00511; 1UOX.
DR   BRENDA; 1.7.3.3; 299.
DR   GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR   GO; GO:0004846; F:urate oxidase activity; IEA:EC.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0006144; P:purine base metabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR002042; Uricase.
DR   InterPro; IPR019842; Uricase_CS.
DR   Gene3D; G3DSA:3.10.270.10; Uricase; 1.
DR   PANTHER; PTHR10395:SF1; Uricase; 1.
DR   Pfam; PF01014; Uricase; 2.
DR   PRINTS; PR00093; URICASE.
DR   ProDom; PD003367; Uricase; 2.
DR   TIGRFAMs; TIGR03383; urate_oxi; 1.
DR   PROSITE; PS00366; URICASE; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Oxidoreductase; Peroxisome;
KW   Purine metabolism.
FT   CHAIN         1    309       Uricase-2 isozyme 2.
FT                                /FTId=PRO_0000166004.
FT   REGION      238    239       Substrate binding (By similarity).
FT   ACT_SITE    183    183       Charge relay system (By similarity).
FT   ACT_SITE    239    239       Charge relay system (By similarity).
FT   BINDING      64     64       Substrate (By similarity).
FT   BINDING     183    183       Substrate (By similarity).
FT   CONFLICT    208    208       L -> F (in Ref. 1; AAA33994).
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
//