ID   HXKG_YEAST              Reviewed;         500 AA.
AC   P17709; D6VQX5;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
DT   27-MAR-2024, entry version 201.
DE   RecName: Full=Glucokinase-1;
DE            EC=2.7.1.2 {ECO:0000305|PubMed:3072253};
DE   AltName: Full=Glucose kinase 1;
DE            Short=GLK-1;
GN   Name=GLK1; Synonyms=HOR3; OrderedLocusNames=YCL040W;
GN   ORFNames=YCL312, YCL40W;
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], FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=3072253; DOI=10.1016/0378-1119(88)90320-4;
RA   Albig W., Entian K.-D.;
RT   "Structure of yeast glucokinase, a strongly diverged specific aldo-hexose-
RT   phosphorylating isoenzyme.";
RL   Gene 73:141-152(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1523890; DOI=10.1002/yea.320080709;
RA   Scherens B., Messenguy F., Gigot D., Dubois E.;
RT   "The complete sequence of a 9,543 bp segment on the left arm of chromosome
RT   III reveals five open reading frames including glucokinase and the protein
RT   disulfide isomerase.";
RL   Yeast 8:577-586(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=1574125; DOI=10.1038/357038a0;
RA   Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M.,
RA   Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G.,
RA   Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A.,
RA   Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M., Carcano C.,
RA   Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M.,
RA   Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C.,
RA   Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F.,
RA   Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C.,
RA   Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E.,
RA   Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P.,
RA   Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J.,
RA   Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P.,
RA   Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M.,
RA   Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P.,
RA   Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G.,
RA   Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E.,
RA   Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F.,
RA   Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L.,
RA   Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J.,
RA   Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M.,
RA   Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A.,
RA   Richterich P., Roberts A.B., Rodriguez F., Sanz E.,
RA   Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J.,
RA   Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I.,
RA   Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M.,
RA   Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M.,
RA   Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D.,
RA   Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K.,
RA   Sgouros J.G.;
RT   "The complete DNA sequence of yeast chromosome III.";
RL   Nature 357:38-46(1992).
RN   [4]
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   [5]
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   [6]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE
RP   ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE
RP   ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=YAL6B;
RX   PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA   Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA   Jensen O.N.;
RT   "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT   pathway.";
RL   Mol. Cell. Proteomics 4:310-327(2005).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-470, 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   [8]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC   -!- FUNCTION: Two isoenzymes, hexokinase-1 and hexokinase-2, can
CC       phosphorylate keto- and aldohexoses in yeast, whereas a third
CC       isoenzyme, GLK, is specific for aldohexoses. All glucose
CC       phosphorylating enzymes are involved in glucose uptake.
CC       {ECO:0000269|PubMed:3072253}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + D-glucose = ADP + D-glucose 6-phosphate + H(+);
CC         Xref=Rhea:RHEA:17825, ChEBI:CHEBI:4167, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61548, ChEBI:CHEBI:456216; EC=2.7.1.2;
CC         Evidence={ECO:0000305|PubMed:3072253};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17826;
CC         Evidence={ECO:0000305|PubMed:3072253};
CC   -!- PATHWAY: Carbohydrate metabolism; hexose metabolism.
CC       {ECO:0000269|PubMed:3072253}.
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC       phosphate and glycerone phosphate from D-glucose: step 1/4.
CC       {ECO:0000269|PubMed:3072253}.
CC   -!- SUBUNIT: Monomer.
CC   -!- MISCELLANEOUS: Present with 21100 molecules/cell in log phase SD
CC       medium. {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the hexokinase family. {ECO:0000255|PROSITE-
CC       ProRule:PRU01084, ECO:0000305}.
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DR   EMBL; M24077; AAA53536.1; -; Genomic_DNA.
DR   EMBL; X59720; CAA42376.1; -; Genomic_DNA.
DR   EMBL; BK006937; DAA07444.1; -; Genomic_DNA.
DR   PIR; JT0482; JT0482.
DR   RefSeq; NP_009890.1; NM_001178685.1.
DR   PDB; 6P4X; X-ray; 3.59 A; A/B/C/D/E/F=1-500.
DR   PDB; 6PDT; EM; 3.80 A; A/B/C/D=1-500.
DR   PDBsum; 6P4X; -.
DR   PDBsum; 6PDT; -.
DR   AlphaFoldDB; P17709; -.
DR   EMDB; EMD-20309; -.
DR   SMR; P17709; -.
DR   BioGRID; 30943; 73.
DR   DIP; DIP-525N; -.
DR   IntAct; P17709; 56.
DR   MINT; P17709; -.
DR   STRING; 4932.YCL040W; -.
DR   iPTMnet; P17709; -.
DR   MaxQB; P17709; -.
DR   PaxDb; 4932-YCL040W; -.
DR   PeptideAtlas; P17709; -.
DR   EnsemblFungi; YCL040W_mRNA; YCL040W; YCL040W.
DR   GeneID; 850317; -.
DR   KEGG; sce:YCL040W; -.
DR   AGR; SGD:S000000545; -.
DR   SGD; S000000545; GLK1.
DR   VEuPathDB; FungiDB:YCL040W; -.
DR   eggNOG; KOG1369; Eukaryota.
DR   GeneTree; ENSGT00950000182787; -.
DR   HOGENOM; CLU_014393_5_0_1; -.
DR   InParanoid; P17709; -.
DR   OMA; YPNFEGY; -.
DR   OrthoDB; 5481886at2759; -.
DR   BioCyc; MetaCyc:YCL040W-MONOMER; -.
DR   BioCyc; YEAST:YCL040W-MONOMER; -.
DR   BRENDA; 2.7.1.2; 984.
DR   Reactome; R-SCE-170822; Regulation of Glucokinase by Glucokinase Regulatory Protein.
DR   Reactome; R-SCE-6798695; Neutrophil degranulation.
DR   Reactome; R-SCE-70171; Glycolysis.
DR   SABIO-RK; P17709; -.
DR   UniPathway; UPA00109; UER00180.
DR   UniPathway; UPA00242; -.
DR   BioGRID-ORCS; 850317; 6 hits in 10 CRISPR screens.
DR   PRO; PR:P17709; -.
DR   Proteomes; UP000002311; Chromosome III.
DR   RNAct; P17709; Protein.
DR   GO; GO:0005829; C:cytosol; HDA:SGD.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; HDA:SGD.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008865; F:fructokinase activity; IBA:GO_Central.
DR   GO; GO:0004340; F:glucokinase activity; IDA:SGD.
DR   GO; GO:0005536; F:glucose binding; IEA:InterPro.
DR   GO; GO:0046835; P:carbohydrate phosphorylation; IBA:GO_Central.
DR   GO; GO:0051156; P:glucose 6-phosphate metabolic process; IBA:GO_Central.
DR   GO; GO:0046323; P:glucose import; IGI:SGD.
DR   GO; GO:0006006; P:glucose metabolic process; IMP:SGD.
DR   GO; GO:0006096; P:glycolytic process; IDA:SGD.
DR   GO; GO:0001678; P:intracellular glucose homeostasis; IBA:GO_Central.
DR   GO; GO:0006013; P:mannose metabolic process; IDA:SGD.
DR   CDD; cd00012; NBD_sugar-kinase_HSP70_actin; 1.
DR   Gene3D; 3.30.420.40; -; 1.
DR   Gene3D; 3.40.367.20; -; 1.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR001312; Hexokinase.
DR   InterPro; IPR019807; Hexokinase_BS.
DR   InterPro; IPR022673; Hexokinase_C.
DR   InterPro; IPR022672; Hexokinase_N.
DR   PANTHER; PTHR19443:SF30; GLUCOKINASE-1-RELATED; 1.
DR   PANTHER; PTHR19443; HEXOKINASE; 1.
DR   Pfam; PF00349; Hexokinase_1; 1.
DR   Pfam; PF03727; Hexokinase_2; 1.
DR   PRINTS; PR00475; HEXOKINASE.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR   PROSITE; PS00378; HEXOKINASE_1; 1.
DR   PROSITE; PS51748; HEXOKINASE_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; ATP-binding; Glycolysis; Kinase;
KW   Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:15665377,
FT                   ECO:0007744|PubMed:22814378"
FT   CHAIN           2..500
FT                   /note="Glucokinase-1"
FT                   /id="PRO_0000197603"
FT   DOMAIN          12..498
FT                   /note="Hexokinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01084"
FT   REGION          74..216
FT                   /note="Hexokinase small subdomain"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01084"
FT   REGION          158..184
FT                   /note="Glucose-binding"
FT                   /evidence="ECO:0000255"
FT   REGION          217..487
FT                   /note="Hexokinase large subdomain"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01084"
FT   BINDING         110
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   BINDING         487..492
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0007744|PubMed:15665377,
FT                   ECO:0007744|PubMed:22814378"
FT   MOD_RES         2
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:15665377"
FT   MOD_RES         470
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
SQ   SEQUENCE   500 AA;  55377 MW;  A7A417041D7A961F CRC64;
     MSFDDLHKAT ERAVIQAVDQ ICDDFEVTPE KLDELTAYFI EQMEKGLAPP KEGHTLASDK
     GLPMIPAFVT GSPNGTERGV LLAADLGGTN FRICSVNLHG DHTFSMEQMK SKIPDDLLDD
     ENVTSDDLFG FLARRTLAFM KKYHPDELAK GKDAKPMKLG FTFSYPVDQT SLNSGTLIRW
     TKGFRIADTV GKDVVQLYQE QLSAQGMPMI KVVALTNDTV GTYLSHCYTS DNTDSMTSGE
     ISEPVIGCIF GTGTNGCYME EINKITKLPQ ELRDKLIKEG KTHMIINVEW GSFDNELKHL
     PTTKYDVVID QKLSTNPGFH LFEKRVSGMF LGEVLRNILV DLHSQGLLLQ QYRSKEQLPR
     HLTTPFQLSS EVLSHIEIDD STGLRETELS LLQSLRLPTT PTERVQIQKL VRAISRRSAY
     LAAVPLAAIL IKTNALNKRY HGEVEIGCDG SVVEYYPGFR SMLRHALALS PLGAEGERKV
     HLKIAKDGSG VGAALCALVA
//