GUAD_YEAST
ID GUAD_YEAST Reviewed; 489 AA.
AC Q07729; D6VRB8;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Probable guanine deaminase;
DE Short=Guanase;
DE Short=Guanine aminase;
DE EC=3.5.4.3 {ECO:0000269|PubMed:15565584};
DE AltName: Full=Guanine aminohydrolase;
DE Short=GAH;
GN Name=GUD1; OrderedLocusNames=YDL238C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX 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., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., 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 GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [4]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [5]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND CATALYTIC ACTIVITY.
RX PubMed=15565584; DOI=10.1002/yea.1186;
RA Saint-Marc C., Daignan-Fornier B.;
RT "GUD1 (YDL238c) encodes Saccharomyces cerevisiae guanine deaminase, an
RT enzyme expressed during post-diauxic growth.";
RL Yeast 21:1359-1363(2004).
CC -!- FUNCTION: Catalyzes the hydrolytic deamination of guanine, producing
CC xanthine and ammonia. {ECO:0000269|PubMed:15565584}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=guanine + H(+) + H2O = NH4(+) + xanthine;
CC Xref=Rhea:RHEA:14665, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16235, ChEBI:CHEBI:17712, ChEBI:CHEBI:28938; EC=3.5.4.3;
CC Evidence={ECO:0000269|PubMed:15565584};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=61.5 uM for guanine {ECO:0000269|PubMed:15565584};
CC -!- PATHWAY: Purine metabolism; guanine degradation; xanthine from guanine:
CC step 1/1.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 279 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC ATZ/TRZ family. {ECO:0000305}.
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DR EMBL; Z74286; CAA98818.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11628.1; -; Genomic_DNA.
DR PIR; S67802; S67802.
DR RefSeq; NP_010043.1; NM_001180298.1.
DR PDB; 6OH9; X-ray; 1.75 A; A=1-489.
DR PDB; 6OHA; X-ray; 2.21 A; A=1-489.
DR PDBsum; 6OH9; -.
DR PDBsum; 6OHA; -.
DR AlphaFoldDB; Q07729; -.
DR SMR; Q07729; -.
DR BioGRID; 31873; 40.
DR DIP; DIP-5170N; -.
DR IntAct; Q07729; 1.
DR MINT; Q07729; -.
DR STRING; 4932.YDL238C; -.
DR MaxQB; Q07729; -.
DR PaxDb; Q07729; -.
DR PRIDE; Q07729; -.
DR EnsemblFungi; YDL238C_mRNA; YDL238C; YDL238C.
DR GeneID; 851360; -.
DR KEGG; sce:YDL238C; -.
DR SGD; S000002397; GUD1.
DR VEuPathDB; FungiDB:YDL238C; -.
DR eggNOG; KOG3968; Eukaryota.
DR GeneTree; ENSGT00390000017130; -.
DR HOGENOM; CLU_012358_0_0_1; -.
DR InParanoid; Q07729; -.
DR OMA; ALIGKVC; -.
DR BioCyc; YEAST:MON3O-12; -.
DR BRENDA; 3.5.4.3; 984.
DR Reactome; R-SCE-74259; Purine catabolism.
DR SABIO-RK; Q07729; -.
DR UniPathway; UPA00603; UER00660.
DR PRO; PR:Q07729; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q07729; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0019239; F:deaminase activity; IBA:GO_Central.
DR GO; GO:0008892; F:guanine deaminase activity; IDA:SGD.
DR GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR GO; GO:0006147; P:guanine catabolic process; IDA:SGD.
DR GO; GO:0046098; P:guanine metabolic process; IBA:GO_Central.
DR CDD; cd01303; GDEase; 1.
DR Gene3D; 2.30.40.10; -; 1.
DR InterPro; IPR006680; Amidohydro-rel.
DR InterPro; IPR014311; Guanine_deaminase.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR Pfam; PF01979; Amidohydro_1; 1.
DR SUPFAM; SSF51556; SSF51556; 1.
DR TIGRFAMs; TIGR02967; guan_deamin; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Hydrolase; Metal-binding; Reference proteome;
KW Zinc.
FT CHAIN 1..489
FT /note="Probable guanine deaminase"
FT /id="PRO_0000122302"
FT BINDING 100
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2T3"
FT BINDING 102..105
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2T3"
FT BINDING 102
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2T3"
FT BINDING 231..232
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2T3"
FT BINDING 258..261
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2T3"
FT BINDING 258
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2T3"
FT BINDING 348
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2T3"
FT BINDING 348
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2T3"
FT STRAND 18..27
FT /evidence="ECO:0007829|PDB:6OH9"
FT STRAND 35..45
FT /evidence="ECO:0007829|PDB:6OH9"
FT STRAND 48..53
FT /evidence="ECO:0007829|PDB:6OH9"
FT HELIX 59..66
FT /evidence="ECO:0007829|PDB:6OH9"
FT HELIX 72..74
FT /evidence="ECO:0007829|PDB:6OH9"
FT STRAND 75..79
FT /evidence="ECO:0007829|PDB:6OH9"
FT STRAND 90..94
FT /evidence="ECO:0007829|PDB:6OH9"
FT STRAND 96..102
FT /evidence="ECO:0007829|PDB:6OH9"
FT HELIX 103..108
FT /evidence="ECO:0007829|PDB:6OH9"
FT HELIX 117..123
FT /evidence="ECO:0007829|PDB:6OH9"
FT HELIX 125..131
FT /evidence="ECO:0007829|PDB:6OH9"
FT HELIX 135..151
FT /evidence="ECO:0007829|PDB:6OH9"
FT STRAND 154..160
FT /evidence="ECO:0007829|PDB:6OH9"
FT HELIX 165..178
FT /evidence="ECO:0007829|PDB:6OH9"
FT STRAND 181..185
FT /evidence="ECO:0007829|PDB:6OH9"
FT STRAND 191..193
FT /evidence="ECO:0007829|PDB:6OH9"
FT HELIX 201..217
FT /evidence="ECO:0007829|PDB:6OH9"
FT STRAND 224..230
FT /evidence="ECO:0007829|PDB:6OH9"
FT HELIX 233..235
FT /evidence="ECO:0007829|PDB:6OH9"
FT HELIX 238..251
FT /evidence="ECO:0007829|PDB:6OH9"
FT STRAND 254..260
FT /evidence="ECO:0007829|PDB:6OH9"
FT HELIX 263..272
FT /evidence="ECO:0007829|PDB:6OH9"
FT STRAND 276..278
FT /evidence="ECO:0007829|PDB:6OH9"
FT HELIX 279..285
FT /evidence="ECO:0007829|PDB:6OH9"
FT STRAND 293..297
FT /evidence="ECO:0007829|PDB:6OH9"
FT HELIX 303..312
FT /evidence="ECO:0007829|PDB:6OH9"
FT STRAND 315..318
FT /evidence="ECO:0007829|PDB:6OH9"
FT HELIX 320..325
FT /evidence="ECO:0007829|PDB:6OH9"
FT HELIX 333..338
FT /evidence="ECO:0007829|PDB:6OH9"
FT STRAND 342..345
FT /evidence="ECO:0007829|PDB:6OH9"
FT TURN 349..351
FT /evidence="ECO:0007829|PDB:6OH9"
FT HELIX 357..375
FT /evidence="ECO:0007829|PDB:6OH9"
FT HELIX 377..379
FT /evidence="ECO:0007829|PDB:6OH9"
FT HELIX 383..390
FT /evidence="ECO:0007829|PDB:6OH9"
FT HELIX 392..397
FT /evidence="ECO:0007829|PDB:6OH9"
FT TURN 401..403
FT /evidence="ECO:0007829|PDB:6OH9"
FT STRAND 404..407
FT /evidence="ECO:0007829|PDB:6OH9"
FT STRAND 415..419
FT /evidence="ECO:0007829|PDB:6OH9"
FT HELIX 431..433
FT /evidence="ECO:0007829|PDB:6OH9"
FT HELIX 460..470
FT /evidence="ECO:0007829|PDB:6OH9"
FT HELIX 473..475
FT /evidence="ECO:0007829|PDB:6OH9"
FT STRAND 476..481
FT /evidence="ECO:0007829|PDB:6OH9"
FT STRAND 484..488
FT /evidence="ECO:0007829|PDB:6OH9"
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
