HXKG_YEAST
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 03-AUG-2022, entry version 194.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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 SMR; P17709; -.
DR BioGRID; 30943; 64.
DR DIP; DIP-525N; -.
DR IntAct; P17709; 56.
DR MINT; P17709; -.
DR STRING; 4932.YCL040W; -.
DR iPTMnet; P17709; -.
DR MaxQB; P17709; -.
DR PaxDb; P17709; -.
DR PRIDE; P17709; -.
DR EnsemblFungi; YCL040W_mRNA; YCL040W; YCL040W.
DR GeneID; 850317; -.
DR KEGG; sce:YCL040W; -.
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; VCSIDLH; -.
DR BioCyc; MetaCyc:YCL040W-MON; -.
DR BioCyc; YEAST:YCL040W-MON; -.
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 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:0001678; P:cellular glucose homeostasis; 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:0006013; P:mannose metabolic process; IDA:SGD.
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; PTHR19443; 1.
DR Pfam; PF00349; Hexokinase_1; 1.
DR Pfam; PF03727; Hexokinase_2; 1.
DR SUPFAM; SSF53067; SSF53067; 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
