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Database: UniProt/SWISS-PROT
Entry: HXKB_YEAST
LinkDB: HXKB_YEAST
Original site: HXKB_YEAST 
ID   HXKB_YEAST              Reviewed;         486 AA.
AC   P04807; D6VV82; Q05838;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 4.
DT   05-DEC-2018, entry version 195.
DE   RecName: Full=Hexokinase-2;
DE            EC=2.7.1.1;
DE   AltName: Full=Hexokinase PII;
DE   AltName: Full=Hexokinase-B;
GN   Name=HXK2; Synonyms=HEX1, HKB; OrderedLocusNames=YGL253W;
GN   ORFNames=NRB486;
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=3905511; DOI=10.1016/0378-1119(85)90074-5;
RA   Froehlich K.-U., Entian K.-D., Mecke D.;
RT   "The primary structure of the yeast hexokinase PII gene (HXK2) which
RT   is responsible for glucose repression.";
RL   Gene 36:105-111(1985).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 96604 / S288c / FY1679;
RX   PubMed=8972578;
RX   DOI=10.1002/(SICI)1097-0061(199612)12:15<1555::AID-YEA43>3.0.CO;2-Q;
RA   Coissac E., Maillier E., Robineau S., Netter P.;
RT   "Sequence of a 39,411 bp DNA fragment covering the left end of
RT   chromosome VII of Saccharomyces cerevisiae.";
RL   Yeast 12:1555-1562(1996).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169869;
RA   Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M.,
RA   Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J.,
RA   Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E.,
RA   Clemente M.L., Coblenz A., Coglievina M., Coissac E., Defoor E.,
RA   Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B.,
RA   Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L.,
RA   Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M.,
RA   Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M.,
RA   Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B.,
RA   Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W.,
RA   Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A.,
RA   Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA   Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S.,
RA   Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L.,
RA   Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S.,
RA   Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J.,
RA   Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M.,
RA   Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B.,
RA   Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J.,
RA   Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M.,
RA   van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M.,
RA   Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H.,
RA   Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M.,
RA   Zollner A., Kleine K.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL   Nature 387:81-84(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.,
RA   Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and
RT   now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [6]
RP   NUCLEOTIDE SEQUENCE OF 1-247.
RC   STRAIN=ATCC 200060 / W303;
RX   PubMed=8322518; DOI=10.1002/yea.320090512;
RA   Breitwieser W., Price C., Schuster T.;
RT   "Identification of a gene encoding a novel zinc finger protein in
RT   Saccharomyces cerevisiae.";
RL   Yeast 9:551-556(1993).
RN   [7]
RP   PROTEIN SEQUENCE OF 119-127; 176-185 AND 304-314.
RC   STRAIN=ATCC 38531 / Y41;
RX   PubMed=7737086; DOI=10.1002/elps.1150160124;
RA   Norbeck J., Blomberg A.;
RT   "Gene linkage of two-dimensional polyacrylamide gel electrophoresis
RT   resolved proteins from isogene families in Saccharomyces cerevisiae by
RT   microsequencing of in-gel trypsin generated peptides.";
RL   Electrophoresis 16:149-156(1995).
RN   [8]
RP   PHOSPHORYLATION AT SER-15.
RX   PubMed=8286332; DOI=10.1021/bi00167a019;
RA   Kriegel T.M., Rush J., Vojtek A.B., Clifton D., Fraenkel D.G.;
RT   "In vivo phosphorylation site of hexokinase 2 in Saccharomyces
RT   cerevisiae.";
RL   Biochemistry 33:148-152(1994).
RN   [9]
RP   PHOSPHORYLATION AT SER-158.
RX   PubMed=9047292; DOI=10.1021/bi9623643;
RA   Heidrich K., Otto A., Behlke J., Rush J., Wenzel K.W., Kriegel T.;
RT   "Autophosphorylation-inactivation site of hexokinase 2 in
RT   Saccharomyces cerevisiae.";
RL   Biochemistry 36:1960-1964(1997).
RN   [10]
RP   PROTEIN SEQUENCE OF 2-19, AND PHOSPHORYLATION AT SER-15.
RX   PubMed=9718324; DOI=10.1021/bi980914m;
RA   Behlke J., Heidrich K., Naumann M., Mueller E.-C., Otto A., Reuter R.,
RA   Kriegel T.;
RT   "Hexokinase 2 from Saccharomyces cerevisiae: regulation of oligomeric
RT   structure by in vivo phosphorylation at serine-14.";
RL   Biochemistry 37:11989-11995(1998).
RN   [11]
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   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-38 AND SER-158, 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   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15 AND SER-245, AND
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   [14]
RP   X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
RX   PubMed=355643; DOI=10.1016/0022-2836(78)90374-1;
RA   Anderson C.M., Stenkamp R.E., Steitz T.A.;
RT   "Sequencing a protein by X-ray crystallography. II. Refinement of
RT   yeast hexokinase B co-ordinates and sequence at 2.1-A resolution.";
RL   J. Mol. Biol. 123:15-33(1978).
CC   -!- FUNCTION: Main glucose phosphorylating enzyme. May play a
CC       regulatory role in both induction and repression of gene
CC       expression by glucose.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + D-hexose = ADP + D-hexose 6-phosphate + H(+);
CC         Xref=Rhea:RHEA:22740, ChEBI:CHEBI:4194, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61567, ChEBI:CHEBI:456216;
CC         EC=2.7.1.1;
CC   -!- ACTIVITY 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 114000 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; X03483; CAA27203.1; -; Genomic_DNA.
DR   EMBL; M11181; AAA34697.1; -; Genomic_DNA.
DR   EMBL; M14411; AAA34699.1; -; mRNA.
DR   EMBL; X94357; CAA64134.1; -; Genomic_DNA.
DR   EMBL; Z72775; CAA96973.1; -; Genomic_DNA.
DR   EMBL; X67787; CAA48003.1; -; Genomic_DNA.
DR   EMBL; BK006941; DAA07866.1; -; Genomic_DNA.
DR   PIR; S61608; KIBYHB.
DR   RefSeq; NP_011261.1; NM_001181119.1.
DR   PDB; 1IG8; X-ray; 2.20 A; A=1-486.
DR   PDB; 2YHX; X-ray; 2.10 A; A=152-471.
DR   PDB; 5UWT; X-ray; 2.34 A; D=14-36.
DR   PDBsum; 1IG8; -.
DR   PDBsum; 2YHX; -.
DR   PDBsum; 5UWT; -.
DR   ProteinModelPortal; P04807; -.
DR   SMR; P04807; -.
DR   BioGrid; 33026; 281.
DR   DIP; DIP-2380N; -.
DR   IntAct; P04807; 16.
DR   MINT; P04807; -.
DR   STRING; 4932.YGL253W; -.
DR   MoonProt; P04807; -.
DR   CarbonylDB; P04807; -.
DR   iPTMnet; P04807; -.
DR   SWISS-2DPAGE; P04807; -.
DR   MaxQB; P04807; -.
DR   PaxDb; P04807; -.
DR   PRIDE; P04807; -.
DR   TopDownProteomics; P04807; -.
DR   EnsemblFungi; YGL253W_mRNA; YGL253W_mRNA; YGL253W.
DR   GeneID; 852639; -.
DR   KEGG; sce:YGL253W; -.
DR   SGD; S000003222; HXK2.
DR   GeneTree; ENSGT00940000153555; -.
DR   HOGENOM; HOG000162670; -.
DR   InParanoid; P04807; -.
DR   KO; K00844; -.
DR   OMA; ASHYVNP; -.
DR   OrthoDB; EOG092C2JW4; -.
DR   BioCyc; YEAST:YGL253W-MONOMER; -.
DR   BRENDA; 2.7.1.1; 984.
DR   SABIO-RK; P04807; -.
DR   UniPathway; UPA00242; -.
DR   EvolutionaryTrace; P04807; -.
DR   PRO; PR:P04807; -.
DR   Proteomes; UP000002311; Chromosome VII.
DR   GO; GO:0005829; C:cytosol; IDA:SGD.
DR   GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR   GO; GO:0005634; C:nucleus; 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   GO; GO:0046015; P:regulation of transcription by glucose; IDA:SGD.
DR   GO; GO:0001302; P:replicative cell aging; IMP: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   INIT_MET      1      1       Removed. {ECO:0000269|PubMed:9718324}.
FT   CHAIN         2    486       Hexokinase-2.
FT                                /FTId=PRO_0000197602.
FT   DOMAIN       21    469       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. {ECO:0000250}.
FT   REGION      210    458       Hexokinase large subdomain.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01084}.
FT   REGION      210    211       Substrate binding. {ECO:0000250}.
FT   BINDING     111    111       ATP. {ECO:0000255}.
FT   BINDING     158    158       Substrate; via carbonyl oxygen.
FT                                {ECO:0000250}.
FT   BINDING     237    237       Substrate. {ECO:0000250}.
FT   BINDING     269    269       Substrate. {ECO:0000250}.
FT   BINDING     302    302       Substrate. {ECO:0000250}.
FT   MOD_RES      15     15       Phosphoserine.
FT                                {ECO:0000244|PubMed:19779198,
FT                                ECO:0000269|PubMed:8286332,
FT                                ECO:0000269|PubMed:9718324}.
FT   MOD_RES      38     38       Phosphothreonine.
FT                                {ECO:0000244|PubMed:18407956}.
FT   MOD_RES     158    158       Phosphoserine.
FT                                {ECO:0000244|PubMed:18407956,
FT                                ECO:0000269|PubMed:9047292}.
FT   MOD_RES     245    245       Phosphoserine.
FT                                {ECO:0000244|PubMed:19779198}.
FT   MOD_RES     272    272       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P04806}.
FT   CONFLICT     29     29       N -> I (in Ref. 1; CAA27203).
FT                                {ECO:0000305}.
FT   CONFLICT     33     33       I -> N (in Ref. 2; AAA34697/AAA34699).
FT                                {ECO:0000305}.
FT   CONFLICT     61     61       G -> V (in Ref. 1; CAA27203).
FT                                {ECO:0000305}.
FT   CONFLICT    197    197       T -> S (in Ref. 1; CAA27203).
FT                                {ECO:0000305}.
FT   CONFLICT    202    202       P -> H (in Ref. 2; AAA34699).
FT                                {ECO:0000305}.
FT   CONFLICT    421    422       YN -> ST (in Ref. 2; AAA34697/AAA34699).
FT                                {ECO:0000305}.
FT   CONFLICT    444    445       TS -> PH (in Ref. 2; AAA34697/AAA34699).
FT                                {ECO:0000305}.
FT   CONFLICT    453    453       I -> V (in Ref. 2; AAA34697/AAA34699).
FT                                {ECO:0000305}.
FT   CONFLICT    462    462       A -> P (in Ref. 2; AAA34697/AAA34699).
FT                                {ECO:0000305}.
FT   HELIX        27     34       {ECO:0000244|PDB:2YHX}.
FT   HELIX        38     54       {ECO:0000244|PDB:2YHX}.
FT   STRAND       58     60       {ECO:0000244|PDB:2YHX}.
FT   STRAND       80     87       {ECO:0000244|PDB:2YHX}.
FT   STRAND       89    100       {ECO:0000244|PDB:2YHX}.
FT   STRAND      104    113       {ECO:0000244|PDB:2YHX}.
FT   TURN        116    119       {ECO:0000244|PDB:2YHX}.
FT   HELIX       125    142       {ECO:0000244|PDB:2YHX}.
FT   STRAND      151    156       {ECO:0000244|PDB:2YHX}.
FT   STRAND      159    162       {ECO:0000244|PDB:1IG8}.
FT   HELIX       189    200       {ECO:0000244|PDB:2YHX}.
FT   STRAND      203    209       {ECO:0000244|PDB:2YHX}.
FT   HELIX       211    222       {ECO:0000244|PDB:2YHX}.
FT   STRAND      226    241       {ECO:0000244|PDB:2YHX}.
FT   HELIX       246    248       {ECO:0000244|PDB:2YHX}.
FT   STRAND      256    258       {ECO:0000244|PDB:2YHX}.
FT   STRAND      264    267       {ECO:0000244|PDB:2YHX}.
FT   TURN        271    276       {ECO:0000244|PDB:2YHX}.
FT   STRAND      278    280       {ECO:0000244|PDB:2YHX}.
FT   HELIX       284    292       {ECO:0000244|PDB:2YHX}.
FT   STRAND      293    295       {ECO:0000244|PDB:1IG8}.
FT   HELIX       300    305       {ECO:0000244|PDB:2YHX}.
FT   HELIX       307    309       {ECO:0000244|PDB:2YHX}.
FT   HELIX       310    323       {ECO:0000244|PDB:2YHX}.
FT   STRAND      326    330       {ECO:0000244|PDB:2YHX}.
FT   TURN        334    336       {ECO:0000244|PDB:1IG8}.
FT   HELIX       345    352       {ECO:0000244|PDB:2YHX}.
FT   STRAND      355    357       {ECO:0000244|PDB:2YHX}.
FT   HELIX       359    369       {ECO:0000244|PDB:2YHX}.
FT   HELIX       375    396       {ECO:0000244|PDB:2YHX}.
FT   HELIX       398    407       {ECO:0000244|PDB:2YHX}.
FT   STRAND      410    418       {ECO:0000244|PDB:2YHX}.
FT   TURN        419    422       {ECO:0000244|PDB:2YHX}.
FT   HELIX       427    439       {ECO:0000244|PDB:2YHX}.
FT   HELIX       446    448       {ECO:0000244|PDB:2YHX}.
FT   STRAND      449    455       {ECO:0000244|PDB:2YHX}.
FT   TURN        459    461       {ECO:0000244|PDB:2YHX}.
FT   HELIX       462    471       {ECO:0000244|PDB:2YHX}.
SQ   SEQUENCE   486 AA;  53942 MW;  D55FF3F8992B2FEF CRC64;
     MVHLGPKKPQ ARKGSMADVP KELMQQIENF EKIFTVPTET LQAVTKHFIS ELEKGLSKKG
     GNIPMIPGWV MDFPTGKESG DFLAIDLGGT NLRVVLVKLG GDRTFDTTQS KYRLPDAMRT
     TQNPDELWEF IADSLKAFID EQFPQGISEP IPLGFTFSFP ASQNKINEGI LQRWTKGFDI
     PNIENHDVVP MLQKQITKRN IPIEVVALIN DTTGTLVASY YTDPETKMGV IFGTGVNGAY
     YDVCSDIEKL QGKLSDDIPP SAPMAINCEY GSFDNEHVVL PRTKYDITID EESPRPGQQT
     FEKMSSGYYL GEILRLALMD MYKQGFIFKN QDLSKFDKPF VMDTSYPARI EEDPFENLED
     TDDLFQNEFG INTTVQERKL IRRLSELIGA RAARLSVCGI AAICQKRGYK TGHIAADGSV
     YNRYPGFKEK AANALKDIYG WTQTSLDDYP IKIVPAEDGS GAGAAVIAAL AQKRIAEGKS
     VGIIGA
//
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