G6PD_YEAST
ID G6PD_YEAST Reviewed; 505 AA.
AC P11412; D6W0V2; E9P908;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Glucose-6-phosphate 1-dehydrogenase;
DE Short=G6PD;
DE EC=1.1.1.49 {ECO:0000250|UniProtKB:P11413};
GN Name=ZWF1; Synonyms=MET19; OrderedLocusNames=YNL241C; ORFNames=N1110;
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 [GENOMIC DNA].
RX PubMed=2269430; DOI=10.1016/0378-1119(90)90248-p;
RA Nogae I., Johnston M.;
RT "Isolation and characterization of the ZWF1 gene of Saccharomyces
RT cerevisiae, encoding glucose-6-phosphate dehydrogenase.";
RL Gene 96:161-169(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2001672; DOI=10.1002/j.1460-2075.1991.tb07981.x;
RA Thomas D., Cherest H., Surdin-Kerjan Y.;
RT "Identification of the structural gene for glucose-6-phosphate
RT dehydrogenase in yeast. Inactivation leads to a nutritional requirement for
RT organic sulfur.";
RL EMBO J. 10:547-553(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8896273;
RX DOI=10.1002/(sici)1097-0061(199609)12:10b<1071::aid-yea4>3.0.co;2-s;
RA Pandolfo D., de Antoni A., Lanfranchi G., Valle G.;
RT "The DNA sequence of cosmid 14-5 from chromosome XIV reveals 21 open
RT reading frames including a novel gene encoding a globin-like domain.";
RL Yeast 12:1071-1076(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [7]
RP PROTEIN SEQUENCE OF 2-505, CLEAVAGE OF INITIATOR METHIONINE, AND
RP ACETYLATION AT SER-2.
RX PubMed=2040308; DOI=10.1111/j.1432-1033.1991.tb16039.x;
RA Persson B., Joernvall H., Wood I., Jeffery J.;
RT "Functionally important regions of glucose-6-phosphate dehydrogenase
RT defined by the Saccharomyces cerevisiae enzyme and its differences from the
RT mammalian and insect forms.";
RL Eur. J. Biochem. 198:485-491(1991).
RN [8]
RP PROTEIN SEQUENCE OF 185-195.
RX PubMed=3922403; DOI=10.1021/bi00324a019;
RA Jeffery J., Hobbs L., Joernvall H.;
RT "Glucose-6-phosphate dehydrogenase from Saccharomyces cerevisiae:
RT characterization of a reactive lysine residue labeled with acetylsalicylic
RT acid.";
RL Biochemistry 24:666-671(1985).
RN [9]
RP PROTEIN SEQUENCE OF 2-7, CLEAVAGE OF INITIATOR METHIONINE, AND ACETYLATION
RP AT SER-2.
RX PubMed=2387402; DOI=10.1016/0014-5793(90)81152-e;
RA Egestad B., Estonius M., Danielsson O., Persson B., Cederlund E.,
RA Kaiser R., Holmquist B., Vallee B., Pares X., Jefferey J., Joernvall H.;
RT "Fast atom bombardment mass spectrometry and chemical analysis in
RT determinations of acyl-blocked protein structures.";
RL FEBS Lett. 269:194-196(1990).
RN [10]
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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-142 AND TYR-145, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [12]
RP DISRUPTION PHENOTYPE.
RX PubMed=20371607; DOI=10.1074/jbc.m109.097188;
RA Castegna A., Scarcia P., Agrimi G., Palmieri L., Rottensteiner H.,
RA Spera I., Germinario L., Palmieri F.;
RT "Identification and functional characterization of a novel mitochondrial
RT carrier for citrate and oxoglutarate in Saccharomyces cerevisiae.";
RL J. Biol. Chem. 285:17359-17370(2010).
RN [13]
RP DISRUPTION PHENOTYPE.
RX PubMed=30240188; DOI=10.1021/acschembio.8b00804;
RA Xu Y.F., Lu W., Chen J.C., Johnson S.A., Gibney P.A., Thomas D.G.,
RA Brown G., May A.L., Campagna S.R., Yakunin A.F., Botstein D.,
RA Rabinowitz J.D.;
RT "Discovery and Functional Characterization of a Yeast Sugar Alcohol
RT Phosphatase.";
RL ACS Chem. Biol. 13:3011-3020(2018).
CC -!- FUNCTION: Catalyzes the rate-limiting step of the oxidative pentose-
CC phosphate pathway, which represents a route for the dissimilation of
CC carbohydrates besides glycolysis. The main function of this enzyme is
CC to provide reducing power (NADPH) and pentose phosphates for fatty acid
CC and nucleic acid synthesis (By similarity).
CC {ECO:0000250|UniProtKB:P11413}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glucose 6-phosphate + NADP(+) = 6-phospho-D-glucono-1,5-
CC lactone + H(+) + NADPH; Xref=Rhea:RHEA:15841, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:57955, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:61548; EC=1.1.1.49;
CC Evidence={ECO:0000250|UniProtKB:P11413};
CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-
CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step
CC 1/3. {ECO:0000250|UniProtKB:P11413}.
CC -!- DISRUPTION PHENOTYPE: Shows growth defects in acetate-supplemented
CC medium; the phenotype is enhanced by addition of hydrogen peroxide
CC (increased oxidative stress) and/or double knockout of ZWF1 and YHM2
CC (PubMed:20371607). Decreases the cytosolic NADPH/NADP(+) ratio; this
CC effect is enhanced in the presence of hydrogen peroxide
CC (PubMed:20371607). Ribitol-5P absent from cell (PubMed:30240188).
CC Decreases cellular levels of ribose-5P and ribulose-5P
CC (PubMed:30240188). Decreases cytosolic levels of citrate and
CC oxoglutarate in the presence of hydrogen peroxide (PubMed:20371607).
CC Double knockouts of ZWF1 and YHM2 show an increased mitochondrial
CC NADPH/NADP(+) ratio in the presence of hydrogen peroxide
CC (PubMed:20371607). Reactive oxygen species (ROS) levels are moderately
CC increased following hydrogen peroxide treatment; in double knockouts of
CC YHM2 and ZWF1 there is a larger increase (PubMed:20371607).
CC {ECO:0000269|PubMed:20371607, ECO:0000269|PubMed:30240188}.
CC -!- MISCELLANEOUS: Present with 15000 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the glucose-6-phosphate dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; M34709; AAA34619.1; -; Genomic_DNA.
DR EMBL; X57336; CAA40611.1; -; Genomic_DNA.
DR EMBL; Z69381; CAA93357.1; -; Genomic_DNA.
DR EMBL; Z71517; CAA96146.1; -; Genomic_DNA.
DR EMBL; AY692998; AAT93017.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10318.1; -; Genomic_DNA.
DR PIR; S13744; S13744.
DR RefSeq; NP_014158.1; NM_001183079.1.
DR AlphaFoldDB; P11412; -.
DR SMR; P11412; -.
DR BioGRID; 35598; 244.
DR DIP; DIP-5061N; -.
DR IntAct; P11412; 4.
DR MINT; P11412; -.
DR STRING; 4932.YNL241C; -.
DR BindingDB; P11412; -.
DR ChEMBL; CHEMBL1075249; -.
DR iPTMnet; P11412; -.
DR SWISS-2DPAGE; P11412; -.
DR MaxQB; P11412; -.
DR PaxDb; P11412; -.
DR PRIDE; P11412; -.
DR EnsemblFungi; YNL241C_mRNA; YNL241C; YNL241C.
DR GeneID; 855480; -.
DR KEGG; sce:YNL241C; -.
DR SGD; S000005185; ZWF1.
DR VEuPathDB; FungiDB:YNL241C; -.
DR eggNOG; KOG0563; Eukaryota.
DR GeneTree; ENSGT00530000063435; -.
DR HOGENOM; CLU_013524_2_3_1; -.
DR InParanoid; P11412; -.
DR OMA; VEICVYE; -.
DR BioCyc; MetaCyc:YNL241C-MON; -.
DR BioCyc; YEAST:YNL241C-MON; -.
DR BRENDA; 1.1.1.49; 984.
DR Reactome; R-SCE-5628897; TP53 Regulates Metabolic Genes.
DR Reactome; R-SCE-71336; Pentose phosphate pathway.
DR SABIO-RK; P11412; -.
DR UniPathway; UPA00115; UER00408.
DR PRO; PR:P11412; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P11412; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004345; F:glucose-6-phosphate dehydrogenase activity; IMP:SGD.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0006006; P:glucose metabolic process; IBA:GO_Central.
DR GO; GO:0006740; P:NADPH regeneration; IMP:SGD.
DR GO; GO:0009051; P:pentose-phosphate shunt, oxidative branch; IMP:SGD.
DR GO; GO:0042542; P:response to hydrogen peroxide; IMP:SGD.
DR HAMAP; MF_00966; G6PD; 1.
DR InterPro; IPR001282; G6P_DH.
DR InterPro; IPR019796; G6P_DH_AS.
DR InterPro; IPR022675; G6P_DH_C.
DR InterPro; IPR022674; G6P_DH_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR23429; PTHR23429; 1.
DR Pfam; PF02781; G6PD_C; 1.
DR Pfam; PF00479; G6PD_N; 1.
DR PIRSF; PIRSF000110; G6PD; 1.
DR PRINTS; PR00079; G6PDHDRGNASE.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR00871; zwf; 1.
DR PROSITE; PS00069; G6P_DEHYDROGENASE; 1.
PE 1: Evidence at protein level;
KW Acetylation; Carbohydrate metabolism; Direct protein sequencing;
KW Glucose metabolism; NADP; Oxidoreductase; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2040308,
FT ECO:0000269|PubMed:2387402"
FT CHAIN 2..505
FT /note="Glucose-6-phosphate 1-dehydrogenase"
FT /id="PRO_0000068107"
FT ACT_SITE 249
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P11411"
FT BINDING 18..25
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT BINDING 52
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT BINDING 157
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT BINDING 157
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT BINDING 187..191
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT BINDING 225
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT BINDING 244
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT BINDING 343
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT BINDING 377
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11413"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:2040308,
FT ECO:0000269|PubMed:2387402"
FT MOD_RES 142
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 145
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT CONFLICT 59
FT /note="Missing (in Ref. 7; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 80
FT /note="K -> N (in Ref. 6; AAT93017)"
FT /evidence="ECO:0000305"
FT CONFLICT 175
FT /note="P -> A (in Ref. 1; AAA34619)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 505 AA; 57522 MW; 9FC23E6CE599454E CRC64;
MSEGPVKFEK NTVISVFGAS GDLAKKKTFP ALFGLFREGY LDPSTKIFGY ARSKLSMEED
LKSRVLPHLK KPHGEADDSK VEQFFKMVSY ISGNYDTDEG FDELRTQIEK FEKSANVDVP
HRLFYLALPP SVFLTVAKQI KSRVYAENGI TRVIVEKPFG HDLASARELQ KNLGPLFKEE
ELYRIDHYLG KELVKNLLVL RFGNQFLNAS WNRDNIQSVQ ISFKERFGTE GRGGYFDSIG
IIRDVMQNHL LQIMTLLTME RPVSFDPESI RDEKVKVLKA VAPIDTDDVL LGQYGKSEDG
SKPAYVDDDT VDKDSKCVTF AAMTFNIENE RWEGVPIMMR AGKALNESKV EIRLQYKAVA
SGVFKDIPNN ELVIRVQPDA AVYLKFNAKT PGLSNATQVT DLNLTYASRY QDFWIPEAYE
VLIRDALLGD HSNFVRDDEL DISWGIFTPL LKHIERPDGP TPEIYPYGSR GPKGLKEYMQ
KHKYVMPEKH PYAWPVTKPE DTKDN
