G6PI_YEAST
ID G6PI_YEAST Reviewed; 554 AA.
AC P12709; D6VQJ0;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 203.
DE RecName: Full=Glucose-6-phosphate isomerase;
DE Short=GPI;
DE EC=5.3.1.9 {ECO:0000250|UniProtKB:P06744};
DE AltName: Full=Phosphoglucose isomerase;
DE Short=PGI;
DE AltName: Full=Phosphohexose isomerase;
DE Short=PHI;
GN Name=PGI1; OrderedLocusNames=YBR196C; ORFNames=YBR1406;
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=3072254; DOI=10.1016/0378-1119(88)90321-6;
RA Tekamp-Olson P., Najarian R., Burke R.L.;
RT "The isolation, characterization and nucleotide sequence of the
RT phosphoglucoisomerase gene of Saccharomyces cerevisiae.";
RL Gene 73:153-161(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204510 / AB320;
RX PubMed=3071735; DOI=10.1007/bf00331310;
RA Green J.B.A., Wright A.P.H., Cheung W.Y., Lancashire W.E., Hartley B.S.;
RT "The structure and regulation of phosphoglucose isomerase in Saccharomyces
RT cerevisiae.";
RL Mol. Gen. Genet. 215:100-106(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8346681; DOI=10.1002/yea.320090611;
RA Demolis N., Mallet L., Bussereau F., Jacquet M.;
RT "RIM2, MSI1 and PGI1 are located within an 8 kb segment of Saccharomyces
RT cerevisiae chromosome II, which also contains the putative ribosomal gene
RT L21 and a new putative essential gene with a leucine zipper motif.";
RL Yeast 9:645-659(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
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] OF 424-554.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7975899; DOI=10.1002/yea.320100612;
RA Mallet L., Bussereau F., Jacquet M.;
RT "Nucleotide sequence analysis of an 11.7 kb fragment of yeast chromosome II
RT including BEM1, a new gene of the WD-40 repeat family and a new member of
RT the KRE2/MNT1 family.";
RL Yeast 10:819-831(1994).
RN [7]
RP ACETYLATION AT SER-2.
RX PubMed=9298649; DOI=10.1002/elps.1150180810;
RA Garrels J.I., McLaughlin C.S., Warner J.R., Futcher B., Latter G.I.,
RA Kobayashi R., Schwender B., Volpe T., Anderson D.S., Mesquita-Fuentes R.,
RA Payne W.E.;
RT "Proteome studies of Saccharomyces cerevisiae: identification and
RT characterization of abundant proteins.";
RL Electrophoresis 18:1347-1360(1997).
RN [8]
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 [9]
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 [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-53, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-220, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [13]
RP ACTIVITY REGULATION.
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: In the cytoplasm, catalyzes the conversion of glucose-6-
CC phosphate to fructose-6-phosphate, the second step in glycolysis, and
CC the reverse reaction during gluconeogenesis.
CC {ECO:0000250|UniProtKB:P06744}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-glucose 6-phosphate = beta-D-fructose 6-phosphate;
CC Xref=Rhea:RHEA:11816, ChEBI:CHEBI:57634, ChEBI:CHEBI:58225;
CC EC=5.3.1.9; Evidence={ECO:0000250|UniProtKB:P06744};
CC -!- ACTIVITY REGULATION: Strongly inhibited by the polyol (sugar alcohol)
CC phosphate D-glucitol 6-phosphate (D-sorbitol 6-phosphate)
CC (PubMed:30240188). Also inhibited by the polyol (sugar alcohol)
CC phosphate D-ribitol 5-phosphate (PubMed:30240188).
CC {ECO:0000269|PubMed:30240188}.
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate and glycerone phosphate from D-glucose: step 2/4.
CC {ECO:0000305}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P06744}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:P78917}.
CC -!- MISCELLANEOUS: Present with 91600 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the GPI family. {ECO:0000305}.
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DR EMBL; M37267; AAA34862.1; -; Genomic_DNA.
DR EMBL; M21696; AAA34894.1; -; Genomic_DNA.
DR EMBL; X13977; CAA32158.1; -; Genomic_DNA.
DR EMBL; Z21487; CAA79683.1; -; Genomic_DNA.
DR EMBL; Z36065; CAA85158.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07310.1; -; Genomic_DNA.
DR PIR; JT0484; NUBY.
DR RefSeq; NP_009755.1; NM_001178544.1.
DR AlphaFoldDB; P12709; -.
DR SMR; P12709; -.
DR BioGRID; 32893; 132.
DR DIP; DIP-1605N; -.
DR IntAct; P12709; 138.
DR MINT; P12709; -.
DR STRING; 4932.YBR196C; -.
DR ChEMBL; CHEMBL1075250; -.
DR iPTMnet; P12709; -.
DR MaxQB; P12709; -.
DR PaxDb; P12709; -.
DR PRIDE; P12709; -.
DR TopDownProteomics; P12709; -.
DR EnsemblFungi; YBR196C_mRNA; YBR196C; YBR196C.
DR GeneID; 852495; -.
DR KEGG; sce:YBR196C; -.
DR SGD; S000000400; PGI1.
DR VEuPathDB; FungiDB:YBR196C; -.
DR eggNOG; KOG2446; Eukaryota.
DR GeneTree; ENSGT00390000000707; -.
DR HOGENOM; CLU_017947_3_1_1; -.
DR InParanoid; P12709; -.
DR OMA; IGVWYIN; -.
DR BioCyc; MetaCyc:YBR196C-MON; -.
DR BioCyc; YEAST:YBR196C-MON; -.
DR Reactome; R-SCE-5628897; TP53 Regulates Metabolic Genes.
DR Reactome; R-SCE-6798695; Neutrophil degranulation.
DR Reactome; R-SCE-70171; Glycolysis.
DR Reactome; R-SCE-70263; Gluconeogenesis.
DR SABIO-RK; P12709; -.
DR UniPathway; UPA00109; UER00181.
DR PRO; PR:P12709; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P12709; protein.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR GO; GO:0005886; C:plasma membrane; HDA:SGD.
DR GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR GO; GO:0004347; F:glucose-6-phosphate isomerase activity; IMP:SGD.
DR GO; GO:0048029; F:monosaccharide binding; IBA:GO_Central.
DR GO; GO:0006094; P:gluconeogenesis; IMP:SGD.
DR GO; GO:0051156; P:glucose 6-phosphate metabolic process; IBA:GO_Central.
DR GO; GO:0006096; P:glycolytic process; IMP:SGD.
DR CDD; cd05015; SIS_PGI_1; 1.
DR CDD; cd05016; SIS_PGI_2; 1.
DR Gene3D; 1.10.1390.10; -; 1.
DR HAMAP; MF_00473; G6P_isomerase; 1.
DR InterPro; IPR001672; G6P_Isomerase.
DR InterPro; IPR023096; G6P_Isomerase_C.
DR InterPro; IPR018189; Phosphoglucose_isomerase_CS.
DR InterPro; IPR046348; SIS_dom_sf.
DR InterPro; IPR035476; SIS_PGI_1.
DR InterPro; IPR035482; SIS_PGI_2.
DR PANTHER; PTHR11469; PTHR11469; 1.
DR Pfam; PF00342; PGI; 1.
DR PRINTS; PR00662; G6PISOMERASE.
DR SUPFAM; SSF53697; SSF53697; 1.
DR PROSITE; PS00765; P_GLUCOSE_ISOMERASE_1; 1.
DR PROSITE; PS00174; P_GLUCOSE_ISOMERASE_2; 1.
DR PROSITE; PS51463; P_GLUCOSE_ISOMERASE_3; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Gluconeogenesis; Glycolysis; Isomerase;
KW Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9298649"
FT CHAIN 2..554
FT /note="Glucose-6-phosphate isomerase"
FT /id="PRO_0000180578"
FT ACT_SITE 367
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P06744"
FT ACT_SITE 398
FT /evidence="ECO:0000250|UniProtKB:P06744"
FT ACT_SITE 520
FT /evidence="ECO:0000250|UniProtKB:P06744"
FT BINDING 168..169
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000250|UniProtKB:P06745"
FT BINDING 218..223
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000250|UniProtKB:P06745"
FT BINDING 363
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000250|UniProtKB:P06745"
FT BINDING 367
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000250|UniProtKB:P06745"
FT BINDING 398
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000250|UniProtKB:P06745"
FT BINDING 520
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000250|UniProtKB:P06745"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:9298649"
FT MOD_RES 53
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 220
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
SQ SEQUENCE 554 AA; 61299 MW; 556D3D3B77EED052 CRC64;
MSNNSFTNFK LATELPAWSK LQKIYESQGK TLSVKQEFQK DAKRFEKLNK TFTNYDGSKI
LFDYSKNLVN DEIIAALIEL AKEANVTGLR DAMFKGEHIN STEDRAVYHV ALRNRANKPM
YVDGVNVAPE VDSVLKHMKE FSEQVRSGEW KGYTGKKITD VVNIGIGGSD LGPVMVTEAL
KHYAGVLDVH FVSNIDGTHI AETLKVVDPE TTLFLIASKT FTTAETITNA NTAKNWFLSK
TGNDPSHIAK HFAALSTNET EVAKFGIDTK NMFGFESWVG GRYSVWSAIG LSVALYIGYD
NFEAFLKGAE AVDNHFTQTP LEDNIPLLGG LLSVWYNNFF GAQTHLVAPF DQYLHRFPAY
LQQLSMESNG KSVTRGNVFT DYSTGSILFG EPATNAQHSF FQLVHQGTKL IPSDFILAAQ
SHNPIENKLH QKMLASNFFA QAEALMVGKD EEQVKAEGAT GGLVPHKVFS GNRPTTSILA
QKITPATLGA LIAYYEHVTF TEGAIWNINS FDQWGVELGK VLAKVIGKEL DNSSTISTHD
ASTNGLINQF KEWM
