ID URIC_MACFA Reviewed; 304 AA. AC Q8MHW6; DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 16-JUN-2009, entry version 38. DE RecName: Full=Uricase; DE EC=1.7.3.3; DE AltName: Full=Urate oxidase; GN Name=UOX; OS Macaca fascicularis (Crab eating macaque) (Cynomolgus monkey). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Cercopithecidae; Cercopithecinae; Macaca. OX NCBI_TaxID=9541; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC TISSUE=Liver; 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. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AB074382; BAB91556.1; -; Genomic_DNA. DR HSSP; Q00511; 1R51. DR HOVERGEN; Q8MHW6; -. DR BRENDA; 1.7.3.3; 3438. 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 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_0000165984. FT REGION 235 236 Substrate binding (By similarity). 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 BINDING 68 68 Substrate (By similarity). FT BINDING 187 187 Substrate (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; 34978 MW; D320AFF27870FAE5 CRC64; MADYHNNYKK NDELEFVRTG YGKDMVKVLH IQRDGKYHSI KEVATSVQLT LSSKKDYLHG DNSDIIPTDT IKNTVHVLAK FKGIKSIEAF GVNICEYFLS SFNHVIRAQV YVEEIPWKRL EKNGVKHVHA FIHTPTGTHF CEVEQLRSGP PVIHSGIKDL KVLKTTQSGF EGFIKDQFTT LPEVKDRCFA TQVYCKWRYH QCRDVDFEAT WGTIRDLVLE KFAGPYDKGE YSPSVQKTLY DIQVLSLSRV PEIEDMEISL PNIHYFNIDM SKMGLINKEE VLLPLDNPYG KITGTVKRKL SSRL //