ID   URIC_AOTTR              Reviewed;         304 AA.
AC   Q8MKJ2;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   25-NOV-2008, entry version 35.
DE   RecName: Full=Uricase;
DE            EC=1.7.3.3;
DE   AltName: Full=Urate oxidase;
GN   Name=UOX;
OS   Aotus trivirgatus (Night monkey) (Douroucouli).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Platyrrhini; Aotidae; Aotus.
OX   NCBI_TaxID=9505;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Kidney;
RX   MEDLINE=21959327; PubMed=11961098;
RA   Oda M., Satta Y., Takenaka O., Takahata N.;
RT   "Loss of urate oxidase activity in hominoids and its evolutionary
RT   implications.";
RL   Mol. Biol. Evol. 19:640-653(2002).
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   -!- SIMILARITY: Belongs to the uricase family.
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DR   EMBL; AB074390; BAB91557.1; -; Genomic_DNA.
DR   HSSP; Q00511; 1R51.
DR   HOVERGEN; Q8MKJ2; -.
DR   GO; GO:0005777; C:peroxisome; IEA:UniProtKB-KW.
DR   GO; GO:0004846; F:urate oxidase activity; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0006144; P:purine base metabolic process; IEA:InterPro.
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   3: Inferred from homology;
KW   Acetylation; Oxidoreductase; Peroxisome; Phosphoprotein;
KW   Purine metabolism.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    304       Uricase.
FT                                /FTId=PRO_0000165981.
FT   MOTIF       302    304       Microbody targeting signal (Potential).
FT   ACT_SITE    187    187       Charge relay system (By similarity).
FT   ACT_SITE    236    236       Charge relay system (By similarity).
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES      36     36       N6-acetyllysine (By similarity).
FT   MOD_RES      39     39       Phosphoserine (By similarity).
FT   MOD_RES      55     55       N6-acetyllysine (By similarity).
FT   MOD_RES     118    118       N6-acetyllysine (By similarity).
FT   MOD_RES     122    122       N6-acetyllysine (By similarity).
FT   MOD_RES     164    164       N6-acetyllysine (By similarity).
FT   MOD_RES     185    185       N6-acetyllysine (By similarity).
FT   MOD_RES     221    221       N6-acetyllysine (By similarity).
FT   MOD_RES     228    228       N6-acetyllysine (By similarity).
FT   MOD_RES     232    232       Phosphoserine (By similarity).
FT   MOD_RES     278    278       N6-acetyllysine (By similarity).
FT   MOD_RES     291    291       N6-acetyllysine (By similarity).
FT   MOD_RES     302    302       Phosphoserine (By similarity).
SQ   SEQUENCE   304 AA;  34934 MW;  6B86C185C63CB92D CRC64;
     MAHYHNDYKK NDEVEFVRTG YGKDMVKVLH IQRDGKYHSI KEVATSVQLT LSSKKDYLHG
     DNSDIIPTDT IKNTVHALAK FKGIKSIEAF AVNICQHFLS SFNHVIRTQV YVEEIPWKRL
     EKNGVKHVHA FIHTPTGTHF CEVEQLRSGP PVIHSGIKDL KVLKTTQSGF EGFIKDQFTT
     LPEVKDRCFA AQVYCKWRYH QCRDVDFEAT WDTIRDVVLE KFAGPYDKGE YSPSVQKTLY
     DIQVVSLSQV PEIDDMEISL PNIHYFNIDM SKMGLINKEE VLLPLDNPYG KITGTVKRKL
     SSRL
//