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Database: UniProt/SWISS-PROT
Entry: HXKA_YEAST
LinkDB: HXKA_YEAST
Original site: HXKA_YEAST 
ID   HXKA_YEAST              Reviewed;         485 AA.
AC   P04806; D6VTT6;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 2.
DT   25-OCT-2017, entry version 187.
DE   RecName: Full=Hexokinase-1;
DE            EC=2.7.1.1;
DE   AltName: Full=Hexokinase PI;
DE   AltName: Full=Hexokinase-A;
GN   Name=HXK1; Synonyms=HKA; OrderedLocusNames=YFR053C;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3003701; DOI=10.1093/nar/14.2.945;
RA   Stachelek C., Stachelek J., Swan J., Botstein D., Konigsberg W.;
RT   "Identification, cloning and sequence determination of the genes
RT   specifying hexokinase A and B from yeast.";
RL   Nucleic Acids Res. 14:945-963(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=3908224; DOI=10.1016/0378-1119(85)90113-1;
RA   Kopetzki E., Entian K.-D., Mecke D.;
RT   "Complete nucleotide sequence of the hexokinase PI gene (HXK1) of
RT   Saccharomyces cerevisiae.";
RL   Gene 39:95-102(1985).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=7670463; DOI=10.1038/ng0795-261;
RA   Murakami Y., Naitou M., Hagiwara H., Shibata T., Ozawa M.,
RA   Sasanuma S., Sasanuma M., Tsuchiya Y., Soeda E., Yokoyama K.,
RA   Yamazaki M., Tashiro H., Eki T.;
RT   "Analysis of the nucleotide sequence of chromosome VI from
RT   Saccharomyces cerevisiae.";
RL   Nat. Genet. 10:261-268(1995).
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.,
RA   Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and
RT   now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204511 / S288c / AB972;
RX   PubMed=8686379;
RX   DOI=10.1002/(SICI)1097-0061(199602)12:2<149::AID-YEA893>3.0.CO;2-G;
RA   Eki T., Naitou M., Hagiwara H., Ozawa M., Sasanuma S., Sasanuma M.,
RA   Tsuchiya Y., Shibata T., Hanaoka F., Murakami Y.;
RT   "Analysis of a 36.2 kb DNA sequence including the right telomere of
RT   chromosome VI from Saccharomyces cerevisiae.";
RL   Yeast 12:149-167(1996).
RN   [6]
RP   ATP-BINDING, AND PROTEIN SEQUENCE OF 104-112.
RX   PubMed=3131329;
RA   Tamura J.K., Ladime J.R., Cross R.L.;
RT   "The adenine nucleotide binding site on yeast hexokinase PII. Affinity
RT   labeling of Lys-111 by pyridoxal 5'-diphospho-5'-adenosine.";
RL   J. Biol. Chem. 263:7907-7912(1988).
RN   [7]
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.,
RA   Dephoure N., O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-245 AND SER-272, AND
RP   IDENTIFICATION BY 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
RT   phosphoproteome analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
RN   [9]
RP   IDENTIFICATION BY 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
RT   insights into evolution.";
RL   Science 325:1682-1686(2009).
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS).
RX   PubMed=7001031; DOI=10.1016/0022-2836(80)90102-3;
RA   Bennett W.S. Jr., Steitz T.A.;
RT   "Structure of a complex between yeast hexokinase A and glucose. I.
RT   Structure determination and refinement at 3.5-A resolution.";
RL   J. Mol. Biol. 140:183-210(1980).
CC   -!- CATALYTIC ACTIVITY: ATP + D-hexose = ADP + D-hexose 6-phosphate.
CC   -!- ENZYME REGULATION: Subject to allosteric control. Substrate
CC       inhibition by ATP.
CC   -!- PATHWAY: Carbohydrate metabolism; hexose metabolism.
CC   -!- SUBUNIT: Homodimer.
CC   -!- MISCELLANEOUS: In yeast there are three glucose-phosphorylating
CC       isoenzymes, designated hexokinase I, II and glucokinase.
CC   -!- MISCELLANEOUS: Present with 40800 molecules/cell in log phase SD
CC       medium. {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the hexokinase family.
CC       {ECO:0000255|PROSITE-ProRule:PRU01084, ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Worthington enzyme manual;
CC       URL="http://www.worthington-biochem.com/HK/";
DR   EMBL; M14410; AAA34698.1; -; mRNA.
DR   EMBL; X03482; CAA27202.1; -; Genomic_DNA.
DR   EMBL; D50617; BAA09292.1; -; Genomic_DNA.
DR   EMBL; BK006940; DAA12496.1; -; Genomic_DNA.
DR   PIR; S56308; KIBYHA.
DR   RefSeq; NP_116711.3; NM_001180018.3.
DR   PDB; 1HKG; X-ray; 3.50 A; A=152-466.
DR   PDB; 3B8A; X-ray; 2.95 A; X=1-485.
DR   PDBsum; 1HKG; -.
DR   PDBsum; 3B8A; -.
DR   ProteinModelPortal; P04806; -.
DR   SMR; P04806; -.
DR   BioGrid; 31211; 86.
DR   DIP; DIP-5377N; -.
DR   IntAct; P04806; 95.
DR   MINT; MINT-561285; -.
DR   STRING; 4932.YFR053C; -.
DR   BindingDB; P04806; -.
DR   iPTMnet; P04806; -.
DR   SWISS-2DPAGE; P04806; -.
DR   MaxQB; P04806; -.
DR   PRIDE; P04806; -.
DR   TopDownProteomics; P04806; -.
DR   EnsemblFungi; BAA09292; BAA09292; BAA09292.
DR   EnsemblFungi; YFR053C; YFR053C; YFR053C.
DR   GeneID; 850614; -.
DR   KEGG; sce:YFR053C; -.
DR   EuPathDB; FungiDB:YFR053C; -.
DR   SGD; S000001949; HXK1.
DR   GeneTree; ENSGT00900000142519; -.
DR   HOGENOM; HOG000162670; -.
DR   InParanoid; P04806; -.
DR   KO; K00844; -.
DR   OMA; LMSCAFY; -.
DR   OrthoDB; EOG092C2JW4; -.
DR   BioCyc; YEAST:YFR053C-MONOMER; -.
DR   BRENDA; 2.7.1.1; 984.
DR   SABIO-RK; P04806; -.
DR   UniPathway; UPA00242; -.
DR   EvolutionaryTrace; P04806; -.
DR   PRO; PR:P04806; -.
DR   Proteomes; UP000002311; Chromosome VI.
DR   GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR   GO; GO:0005739; C:mitochondrion; IDA: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; IBA:GO_Central.
DR   GO; GO:0005536; F:glucose binding; IEA:InterPro.
DR   GO; GO:0004396; F:hexokinase activity; IDA:SGD.
DR   GO; GO:0019158; F:mannokinase activity; IBA:GO_Central.
DR   GO; GO:0001678; P:cellular glucose homeostasis; IBA:GO_Central.
DR   GO; GO:0032445; P:fructose import; IGI:SGD.
DR   GO; GO:0006000; P:fructose metabolic process; IMP:SGD.
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; 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   PROSITE; PS00378; HEXOKINASE_1; 1.
DR   PROSITE; PS51748; HEXOKINASE_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Allosteric enzyme; ATP-binding; Complete proteome;
KW   Direct protein sequencing; Glycolysis; Kinase; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome; Transferase.
FT   CHAIN         1    485       Hexokinase-1.
FT                                /FTId=PRO_0000197601.
FT   DOMAIN       21    468       Hexokinase. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01084}.
FT   NP_BIND      86     91       ATP. {ECO:0000250}.
FT   NP_BIND     307    308       ATP. {ECO:0000250}.
FT   NP_BIND     344    348       ATP. {ECO:0000250}.
FT   NP_BIND     419    423       ATP. {ECO:0000250}.
FT   REGION       75    209       Hexokinase small subdomain.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01084}.
FT   REGION      175    176       Substrate binding.
FT   REGION      210    457       Hexokinase large subdomain.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01084}.
FT   REGION      210    211       Substrate binding.
FT   BINDING     111    111       ATP. {ECO:0000255}.
FT   BINDING     158    158       Substrate; via carbonyl oxygen.
FT   BINDING     237    237       Substrate.
FT   BINDING     269    269       Substrate.
FT   BINDING     302    302       Substrate.
FT   MOD_RES     245    245       Phosphoserine.
FT                                {ECO:0000244|PubMed:18407956}.
FT   MOD_RES     272    272       Phosphoserine.
FT                                {ECO:0000244|PubMed:18407956}.
FT   CONFLICT     61     61       G -> V (in Ref. 1; CAA27202).
FT                                {ECO:0000305}.
FT   CONFLICT    103    103       H -> R (in Ref. 1; CAA27202).
FT                                {ECO:0000305}.
FT   CONFLICT    194    194       N -> K (in Ref. 1; CAA27202).
FT                                {ECO:0000305}.
FT   CONFLICT    244    244       V -> C (in Ref. 1; CAA27202).
FT                                {ECO:0000305}.
FT   CONFLICT    356    357       EN -> VF (in Ref. 2; AAA34698).
FT                                {ECO:0000305}.
FT   CONFLICT    364    364       I -> M (in Ref. 1; CAA27202).
FT                                {ECO:0000305}.
FT   CONFLICT    388    388       I -> T (in Ref. 2; AAA34698).
FT                                {ECO:0000305}.
FT   CONFLICT    444    444       D -> EN (in Ref. 1; CAA27202).
FT                                {ECO:0000305}.
FT   CONFLICT    479    480       SL -> VS (in Ref. 1; CAA27202).
FT                                {ECO:0000305}.
FT   HELIX        21     34       {ECO:0000244|PDB:3B8A}.
FT   HELIX        38     54       {ECO:0000244|PDB:3B8A}.
FT   STRAND       57     59       {ECO:0000244|PDB:3B8A}.
FT   STRAND       80     87       {ECO:0000244|PDB:3B8A}.
FT   STRAND       89     99       {ECO:0000244|PDB:3B8A}.
FT   STRAND      101    113       {ECO:0000244|PDB:3B8A}.
FT   HELIX       116    120       {ECO:0000244|PDB:3B8A}.
FT   HELIX       125    141       {ECO:0000244|PDB:3B8A}.
FT   STRAND      151    156       {ECO:0000244|PDB:3B8A}.
FT   HELIX       181    183       {ECO:0000244|PDB:3B8A}.
FT   HELIX       188    196       {ECO:0000244|PDB:3B8A}.
FT   HELIX       197    199       {ECO:0000244|PDB:3B8A}.
FT   STRAND      202    209       {ECO:0000244|PDB:3B8A}.
FT   HELIX       211    220       {ECO:0000244|PDB:3B8A}.
FT   STRAND      226    243       {ECO:0000244|PDB:3B8A}.
FT   HELIX       244    246       {ECO:0000244|PDB:3B8A}.
FT   HELIX       248    250       {ECO:0000244|PDB:3B8A}.
FT   STRAND      263    267       {ECO:0000244|PDB:3B8A}.
FT   HELIX       270    272       {ECO:0000244|PDB:3B8A}.
FT   TURN        273    276       {ECO:0000244|PDB:3B8A}.
FT   STRAND      278    280       {ECO:0000244|PDB:3B8A}.
FT   HELIX       284    292       {ECO:0000244|PDB:3B8A}.
FT   STRAND      293    295       {ECO:0000244|PDB:3B8A}.
FT   HELIX       300    303       {ECO:0000244|PDB:3B8A}.
FT   HELIX       307    322       {ECO:0000244|PDB:3B8A}.
FT   TURN        323    325       {ECO:0000244|PDB:3B8A}.
FT   STRAND      326    328       {ECO:0000244|PDB:3B8A}.
FT   TURN        334    337       {ECO:0000244|PDB:3B8A}.
FT   HELIX       345    351       {ECO:0000244|PDB:3B8A}.
FT   HELIX       359    367       {ECO:0000244|PDB:3B8A}.
FT   HELIX       375    396       {ECO:0000244|PDB:3B8A}.
FT   HELIX       398    406       {ECO:0000244|PDB:3B8A}.
FT   STRAND      410    417       {ECO:0000244|PDB:3B8A}.
FT   HELIX       419    423       {ECO:0000244|PDB:3B8A}.
FT   HELIX       427    439       {ECO:0000244|PDB:3B8A}.
FT   TURN        444    446       {ECO:0000244|PDB:3B8A}.
FT   STRAND      449    454       {ECO:0000244|PDB:3B8A}.
FT   TURN        458    460       {ECO:0000244|PDB:3B8A}.
FT   HELIX       461    475       {ECO:0000244|PDB:3B8A}.
FT   STRAND      480    482       {ECO:0000244|PDB:3B8A}.
SQ   SEQUENCE   485 AA;  53738 MW;  AF5C9DA8F17BC3D0 CRC64;
     MVHLGPKKPQ ARKGSMADVP KELMDEIHQL EDMFTVDSET LRKVVKHFID ELNKGLTKKG
     GNIPMIPGWV MEFPTGKESG NYLAIDLGGT NLRVVLVKLS GNHTFDTTQS KYKLPHDMRT
     TKHQEELWSF IADSLKDFMV EQELLNTKDT LPLGFTFSYP ASQNKINEGI LQRWTKGFDI
     PNVEGHDVVP LLQNEISKRE LPIEIVALIN DTVGTLIASY YTDPETKMGV IFGTGVNGAF
     YDVVSDIEKL EGKLADDIPS NSPMAINCEY GSFDNEHLVL PRTKYDVAVD EQSPRPGQQA
     FEKMTSGYYL GELLRLVLLE LNEKGLMLKD QDLSKLKQPY IMDTSYPARI EDDPFENLED
     TDDIFQKDFG VKTTLPERKL IRRLCELIGT RAARLAVCGI AAICQKRGYK TGHIAADGSV
     YNKYPGFKEA AAKGLRDIYG WTGDASKDPI TIVPAEDGSG AGAAVIAALS EKRIAEGKSL
     GIIGA
//
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