ID   URIC_ARATH              Reviewed;         309 AA.
AC   O04420; O64848; Q94A71;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 2.
DT   16-JUN-2009, entry version 66.
DE   RecName: Full=Uricase;
DE            EC=1.7.3.3;
DE   AltName: Full=Urate oxidase;
DE   AltName: Full=Nodulin-35 homolog;
GN   OrderedLocusNames=At2g26230; ORFNames=T1D16.13;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Landsberg erecta;
RA   Marchfelder A., Binder S., Brennicke A.;
RT   "A nodulin-35 homologue is encoded in the Arabidopsis genome.";
RL   Trends Plant Sci. 2:167-168(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   MEDLINE=20083487; PubMed=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L.,
RA   Moffat K.S., Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L.,
RA   Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H.,
RA   Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D.,
RA   Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M.,
RA   Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis
RT   thaliana.";
RL   Nature 402:761-768(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   MEDLINE=22954850; PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
RA   Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA   Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA   Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA   Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA   Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA   Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA   Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA   Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA   Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA   Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA   Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA   Feldmann K.A.;
RT   "Full-length cDNA from Arabidopsis thaliana.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
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   -!- SUBCELLULAR LOCATION: Peroxisome (Potential).
CC   -!- SIMILARITY: Belongs to the uricase family.
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DR   EMBL; Y11120; CAA72005.1; -; mRNA.
DR   EMBL; AC004484; AAC14527.1; -; Genomic_DNA.
DR   EMBL; AY050318; AAK91335.1; -; mRNA.
DR   EMBL; AY101530; AAM26651.1; -; mRNA.
DR   EMBL; AY087805; AAM65341.1; -; mRNA.
DR   IPI; IPI00518603; -.
DR   PIR; H84657; H84657.
DR   RefSeq; NP_180191.1; -.
DR   UniGene; At.5406; -.
DR   HSSP; Q00511; 1UOX.
DR   PRIDE; O04420; -.
DR   ProMEX; O04420; -.
DR   GeneID; 817163; -.
DR   GenomeReviews; CT485783_GR; AT2G26230.
DR   KEGG; ath:AT2G26230; -.
DR   TAIR; At2g26230; -.
DR   OMA; O04420; KTTQSGF.
DR   BRENDA; 1.7.3.3; 302.
DR   ArrayExpress; O04420; -.
DR   GO; GO:0005777; C:peroxisome; IDA:TAIR.
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   Complete proteome; Oxidoreductase; Peroxisome; Purine metabolism.
FT   CHAIN         1    309       Uricase.
FT                                /FTId=PRO_0000165999.
FT   REGION      237    238       Substrate binding (By similarity).
FT   MOTIF       307    309       Microbody targeting signal (Potential).
FT   ACT_SITE    182    182       Charge relay system (By similarity).
FT   ACT_SITE    238    238       Charge relay system (By similarity).
FT   BINDING      63     63       Substrate (By similarity).
FT   BINDING     182    182       Substrate (By similarity).
FT   CONFLICT     11     11       D -> E (in Ref. 1; CAA72005).
SQ   SEQUENCE   309 AA;  34881 MW;  9DB8FAD58FDF1404 CRC64;
     MAQEADGIRL DQRHGKARVR VGRVWRHAHD GSHHFVEWNV SISLLSHCLS SYRLDDNSDI
     VATDTIKNTV YVKAKECGDR LSVEEFAILI GKHFCSFYPQ VFTAIVNIIE KPWERVSIDG
     KPHLHGFKLG SENHTTEARV EKSGALNLTS GIGGLALLKT TQSGFERFVR DKYTILPETR
     ERMLATEVNA SWRYSYESVA SIPTKGLYFS EKFMDVKKVL MDTFFGPPET GVYSPSVQRT
     LYLMGSAVLK RFADVSSIHL KMPNIHFLPV NLSTKENPSM VKFKDDVYLP TDEPHGSIEA
     TLSRITSKL
//