ID   URIC_DROSU              Reviewed;         339 AA.
AC   O44111;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   16-JUN-2009, entry version 51.
DE   RecName: Full=Uricase;
DE            EC=1.7.3.3;
DE   AltName: Full=Urate oxidase;
DE   Flags: Fragment;
GN   Name=Uro; Synonyms=UO;
OS   Drosophila subobscura (Fruit fly).
OC   Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha;
OC   Ephydroidea; Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7241;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=98386758; PubMed=9720289; DOI=10.1023/A:1017035109224;
RA   Zeng L.-W., Comeron J.M., Chen B., Kreitman M.;
RT   "The molecular clock revisited: the rate of synonymous vs. replacement
RT   change in Drosophila.";
RL   Genetica 102:369-382(1998).
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.
CC   -!- DEVELOPMENTAL STAGE: Third instar larvae and adult.
CC   -!- SIMILARITY: Belongs to the uricase family.
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DR   EMBL; AF025816; AAB87901.1; -; mRNA.
DR   HSSP; Q00511; 1UOX.
DR   FlyBase; FBgn0021077; Dsub\Uro.
DR   BRENDA; 1.7.3.3; 270690.
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   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   2: Evidence at transcript level;
KW   Oxidoreductase; Peroxisome; Purine metabolism.
FT   CHAIN        <1    339       Uricase.
FT                                /FTId=PRO_0000165993.
FT   REGION      266    267       Substrate binding (By similarity).
FT   MOTIF       337    339       Microbody targeting signal (Potential).
FT   ACT_SITE    218    218       Charge relay system (By similarity).
FT   ACT_SITE    267    267       Charge relay system (By similarity).
FT   BINDING      78     78       Substrate (By similarity).
FT   BINDING     218    218       Substrate (By similarity).
FT   NON_TER       1      1
SQ   SEQUENCE   339 AA;  38437 MW;  34439F6B6078DC6E CRC64;
     LRQPSSASNR TAASLDGQET PFQYEITDHG YGKDAVKVLH VSRKGPVHTI QEFEVGTHLK
     LYSKKDYYQG NNSDIVATDS QKNTVYLLAK KYGIESPEKF ALLLGQHFLN KYSHVEEAHV
     HVETYPWQRV CQEETKASTT VGQGSCNFSS IDNRSLHNHA FIFTPTALHY CDVVIXRQDP
     KQTVITGIKG LRVLKTTQSS FVNFVNDEXR SLPDQYDRIF STVVDCSWEY SDTDTVNFSR
     AWQQVKNIIL RNFAGDPQVG VSSPSVQHTL YLSEKQVLDV IPQVSVISMT MPNKHYFNFD
     TKPFQQIVPG DNNEVFIPVD KPHGTIYAQL ARKNLNSHL
//