ID   GUAD_YEAST              Reviewed;         489 AA.
AC   Q07729;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   16-JUN-2009, entry version 67.
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   Name=GUD1; OrderedLocusNames=YDL238C;
OS   Saccharomyces cerevisiae (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=4932;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   MEDLINE=97313263; PubMed=9169867;
RA   Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA   Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA   Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA   Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA   Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA   Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA   Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA   Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N.,
RA   Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M.,
RA   Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L.,
RA   Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M.,
RA   Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S.,
RA   Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M.,
RA   Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S.,
RA   Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K.,
RA   Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D.,
RA   Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C.,
RA   Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T.,
RA   Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E.,
RA   Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W.,
RA   Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K.,
RA   Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S.,
RA   Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A.,
RA   Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA   Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S.,
RA   Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M.,
RA   Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y.,
RA   Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M.,
RA   Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E.,
RA   Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R.,
RA   Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA   Mewes H.-W., Zollner A., Zaccaria P.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL   Nature 387:75-78(1997).
RN   [2]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   MEDLINE=22923965; PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
RA   Dephoure N., O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
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   -!- INTERACTION:
CC       P38150:-; NbExp=1; IntAct=EBI-7985, EBI-21180;
CC   -!- MISCELLANEOUS: Present with 279 molecules/cell in log phase SD
CC       medium.
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; Z74286; CAA98818.1; -; Genomic_DNA.
DR   PIR; S67802; S67802.
DR   RefSeq; NP_010043.1; -.
DR   DIP; DIP:5170N; -.
DR   IntAct; Q07729; 1.
DR   PeptideAtlas; Q07729; -.
DR   Ensembl; YDL238C; Saccharomyces cerevisiae.
DR   GeneID; 851360; -.
DR   GenomeReviews; Z71256_GR; YDL238C.
DR   KEGG; sce:YDL238C; -.
DR   NMPDR; fig|4932.3.peg.776; -.
DR   CYGD; YDL238c; -.
DR   SGD; S000002397; GUD1.
DR   HOGENOM; Q07729; -.
DR   OMA; Q07729; EDIIAKW.
DR   BRENDA; 3.5.4.3; 250.
DR   NextBio; 968462; -.
DR   ArrayExpress; Q07729; -.
DR   GermOnline; YDL238C; Saccharomyces cerevisiae.
DR   GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR   GO; GO:0008892; F:guanine deaminase activity; IDA:SGD.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
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   1: Evidence at protein level;
KW   Complete proteome; Hydrolase; Metal-binding; Zinc.
FT   CHAIN         1    489       Probable guanine deaminase.
FT                                /FTId=PRO_0000122302.
FT   METAL       100    100       Zinc; via tele nitrogen (By similarity).
FT   METAL       102    102       Zinc; via tele nitrogen (By similarity).
FT   METAL       258    258       Zinc; via tele nitrogen (By similarity).
FT   METAL       348    348       Zinc (By similarity).
FT   BINDING     105    105       Substrate (By similarity).
FT   BINDING     231    231       Substrate (By similarity).
FT   BINDING     261    261       Substrate (By similarity).
FT   BINDING     297    297       Substrate (By similarity).
SQ   SEQUENCE   489 AA;  55204 MW;  60D21F40CA23DF81 CRC64;
     MTKSDLLFDK FNDKHGKFLV FFGTFVDTPK LGELRIREKT SVGVLNGIIR FVNRNSLDPV
     KDCLDHDSSL SPEDVTVVDI IGKDKTRNNS FYFPGFVDTH NHVSQYPNVG VFGNSTLLDW
     LEKYTFPIEA ALANENIARE VYNKVISKTL SHGTTTVAYY NTIDLKSTKL LAQLSSLLGQ
     RVLVGKVCMD TNGPEYYIED TKTSFESTVK VVKYIRETIC DPLVNPIVTP RFAPSCSREL
     MQQLSKLVKD ENIHVQTHLS ENKEEIQWVQ DLFPECESYT DVYDKYGLLT EKTVLAHCIH
     LTDAEARVIK QRRCGISHCP ISNSSLTSGE CRVRWLLDQG IKVGLGTDVS AGHSCSILTT
     GRQAFAVSRH LAMRETDHAK LSVSECLFLA TMGGAQVLRM DETLGTFDVG KQFDAQMIDT
     NAPGSNVDMF HWQLKEKDQM QEQEQEQGQD PYKNPPLLTN EDIIAKWFFN GDDRNTTKVW
     VAGQQVYQI
//