ID GUAD_SCHPO Reviewed; 527 AA. AC O14057; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 1. DT 16-JUN-2009, entry version 54. DE RecName: Full=Probable guanine deaminase; DE Short=Guanase; DE Short=Guanine aminase; DE EC=3.5.4.3; DE AltName: Full=Guanine aminohydrolase; DE Short=GAH; GN ORFNames=SPCC1672.03c; OS Schizosaccharomyces pombe (Fission yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina; OC Schizosaccharomycetes; Schizosaccharomycetales; OC Schizosaccharomycetaceae; Schizosaccharomyces. OX NCBI_TaxID=4896; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 38366 / 972; RX MEDLINE=21848401; PubMed=11859360; DOI=10.1038/nature724; RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., RA Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A., RA Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., RA Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., RA James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., RA Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., RA Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., RA Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., RA Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., RA Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., RA Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., RA Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., RA Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., RA Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., RA Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., RA Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., RA Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., RA Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., RA Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., RA Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., RA Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., RA Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.; RT "The genome sequence of Schizosaccharomyces pombe."; RL Nature 415:871-880(2002). CC -!- FUNCTION: Catalyzes the hydrolytic deamination of guanine, CC producing xanthine and ammonia (By similarity). CC -!- CATALYTIC ACTIVITY: Guanine + H(2)O = xanthine + NH(3). CC -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity). CC -!- PATHWAY: Purine metabolism; guanine degradation; xanthine from CC guanine: step 1/1. CC -!- SIMILARITY: Belongs to the ATZ/TRZ 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; CU329672; CAA20441.1; -; Genomic_DNA. DR PIR; T41047; T41047. DR RefSeq; NP_587874.1; -. DR GeneID; 2539231; -. DR KEGG; spo:SPCC1672.03c; -. DR NMPDR; fig|4896.1.peg.212; -. DR GeneDB_Spombe; SPCC1672.03c; -. DR OMA; O14057; SESDWEH. DR BioCyc; SPOM-XXX-01:SPOM-XXX-01-002219-MON; -. DR BRENDA; 3.5.4.3; 653. DR ArrayExpress; O14057; -. DR GO; GO:0005829; C:cytosol; IDA:GeneDB_SPombe. DR GO; GO:0008892; F:guanine deaminase activity; IEA:EC. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW. DR InterPro; IPR006680; Amidohydro_1. DR InterPro; IPR014311; Guanine_deaminase. DR PANTHER; PTHR11271:SF6; Guanine_deaminase; 1. DR Pfam; PF01979; Amidohydro_1; 1. DR TIGRFAMs; TIGR02967; guan_deamin; 1. PE 2: Evidence at transcript level; KW Complete proteome; Hydrolase; Metal-binding; Zinc. FT CHAIN 1 527 Probable guanine deaminase. FT /FTId=PRO_0000122301. FT METAL 79 79 Zinc; via tele nitrogen (By similarity). FT METAL 81 81 Zinc; via tele nitrogen (By similarity). FT METAL 239 239 Zinc; via tele nitrogen (By similarity). FT METAL 329 329 Zinc (By similarity). FT BINDING 84 84 Substrate (By similarity). FT BINDING 212 212 Substrate (By similarity). FT BINDING 242 242 Substrate (By similarity). FT BINDING 278 278 Substrate (By similarity). SQ SEQUENCE 527 AA; 58047 MW; 23D9A3F1117601C1 CRC64; MDGHTCDVFV GKLIHTPSLG ELEITDATVG VYNGKIVFLE KSMTPKTLEE AKSHHLLKEA TIHKLKPLQF MFPGLIDTHI HAPQYPNSGI GIDVPLLQWL EKYTFPLESS LADLEEARQV YKRVVERTLS NGTTFASYFS TLHTPTSALL AEICYSYGQR AYIGKCNMNN LSPDHYCEKS AESSLEATRQ LISYMSILDP KREMVTPIIT PRFAPSCTED LLSGCGELAE KHNLPIQTHI SENTSEIELV KELFPERKSY ADVYDYYKLL TPQTILAHAI HLEDEEIELL TKRSSGISHC PTSNSILASG LANVRKLLDS GINVGLGTDV SGGYAPSILI ALRHAAMTSR SLSYVLGDPK VMLDLSELLY LATQGGAEVV SRGDQVGSFA VGKYWDALIV DLSAETHSCV DIFERDTWPV MLSKWVFTSD DRNLAQVWVN GRLVSGFEMK ANLKNSTPLT NGVTSSGHQV FKELTQAHLL PRTQCVDTPP SCCGGHCCKE ESCRTENCKG AYPANATVTV EEDSGMS //