Reviewed, UniProtKB/Swiss-Prot P04807 (HXKB_YEAST)

Names and origin

Protein names

Recommended name:
    Hexokinase-2
    EC=2.7.1.1
Alternative name(s):
    Hexokinase-B
    Hexokinase PII

Gene names

Name:	HXK2
Synonyms:	HEX1, HKB
Ordered Locus Names:	YGL253W
ORF Names:	NRB486

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	486 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Main glucose phosphorylating enzyme. May play a regulatory role in both induction and repression of gene expression by glucose.
Catalytic activity	ATP + D-hexose = ADP + D-hexose 6-phosphate.
Enzyme regulation	Subject to allosteric control. Substrate inhibition by ATP.
Pathway	Carbohydrate metabolism; hexose metabolism.
Subunit structure	Homodimer.
Miscellaneous	In yeast there are three glucose-phosphorylating isoenzymes, designated hexokinase I, II and glucokinase. Present with 114000 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the hexokinase family.

Ontologies

Keywords
Biological process	Glycolysis
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
PTM	Phosphoprotein
Technical term	3D-structure Allosteric enzyme Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	fructose import Inferred from genetic interaction. Source: SGD fructose metabolic process Inferred from mutant phenotype. Source: SGD glucose import Inferred from genetic interaction. Source: SGD glycolysis Inferred from direct assay. Source: SGD mannose metabolic process Inferred from direct assay. Source: SGD regulation of cell size Inferred from mutant phenotype. Source: SGD regulation of transcription by glucose Inferred from direct assay. Source: SGD replicative cell aging Inferred from mutant phenotype. Source: SGD
Cellular component	cytosol Inferred from direct assay. Source: SGD mitochondrion Inferred from direct assay. Source: SGD nucleus Inferred from direct assay. Source: SGD
Molecular function	hexokinase activity Inferred from direct assay. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Molecule processing

Initiator methionine

1

1

Removed

Chain

2 – 486

485

Hexokinase-2

Regions

Region

152 – 178

27

Glucose-binding Potential

Sites

Binding site

111

1

ATP By similarity

Amino acid modifications

Modified residue

15

1

Phosphoserine

Modified residue

38

1

Phosphothreonine

Modified residue

158

1

Phosphoserine

Modified residue

245

1

Phosphoserine

Modified residue

272

1

Phosphoserine

Modified residue

396

1

Phosphoserine

Modified residue

419

1

Phosphoserine

Experimental info

Sequence conflict

29

1

N → I in CAA27203. Ref.1

Sequence conflict

33

1

I → N in AAA34697 and AAA34699. Ref.2

Sequence conflict

61

1

G → V in CAA27203. Ref.1

Sequence conflict

197

1

T → S in CAA27203. Ref.1

Sequence conflict

202

1

P → H in AAA34699. Ref.2

Sequence conflict

421 – 422

2

YN → ST in AAA34697 and AAA34699. Ref.2

Sequence conflict

444 – 445

2

TS → PH in AAA34697 and AAA34699. Ref.2

Sequence conflict

453

1

I → V in AAA34697 and AAA34699. Ref.2

Sequence conflict

462

1

A → P in AAA34697 and AAA34699. Ref.2

Secondary structure

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486

Helix Strand Turn

Details...

Helix

21 – 34

14

Helix

38 – 56

19

Beta strand

79 – 87

9

Beta strand

89 – 103

15

Beta strand

105 – 113

9

Helix

118 – 120

3

Helix

126 – 142

17

Beta strand

151 – 156

6

Beta strand

159 – 162

4

Helix

188 – 198

11

Beta strand

203 – 209

7

Helix

211 – 222

12

Beta strand

226 – 243

18

Helix

244 – 246

3

Helix

248 – 250

3

Beta strand

263 – 267

5

Helix

270 – 272

3

Turn

273 – 276

4

Beta strand

278 – 280

3

Helix

284 – 292

9

Beta strand

293 – 295

3

Helix

300 – 305

6

Helix

307 – 309

3

Helix

310 – 323

14

Beta strand

326 – 328

3

Turn

334 – 336

3

Helix

345 – 352

8

Helix

359 – 369

11

Helix

375 – 396

22

Helix

398 – 407

10

Beta strand

410 – 418

9

Helix

419 – 423

5

Helix

427 – 439

13

Helix

446 – 448

3

Beta strand

450 – 455

6

Turn

459 – 461

3

Helix

462 – 476

15

Sequences

	Sequence		Length	Mass (Da)
	P04807-1 [UniParc]. Last modified January 23, 2007. Version 4. Checksum: D55FF3F8992B2FEF	FASTA	486	53,942
	10 20 30 40 50 60 MVHLGPKKPQ ARKGSMADVP KELMQQIENF EKIFTVPTET LQAVTKHFIS ELEKGLSKKG 70 80 90 100 110 120 GNIPMIPGWV MDFPTGKESG DFLAIDLGGT NLRVVLVKLG GDRTFDTTQS KYRLPDAMRT 130 140 150 160 170 180 TQNPDELWEF IADSLKAFID EQFPQGISEP IPLGFTFSFP ASQNKINEGI LQRWTKGFDI 190 200 210 220 230 240 PNIENHDVVP MLQKQITKRN IPIEVVALIN DTTGTLVASY YTDPETKMGV IFGTGVNGAY 250 260 270 280 290 300 YDVCSDIEKL QGKLSDDIPP SAPMAINCEY GSFDNEHVVL PRTKYDITID EESPRPGQQT 310 320 330 340 350 360 FEKMSSGYYL GEILRLALMD MYKQGFIFKN QDLSKFDKPF VMDTSYPARI EEDPFENLED 370 380 390 400 410 420 TDDLFQNEFG INTTVQERKL IRRLSELIGA RAARLSVCGI AAICQKRGYK TGHIAADGSV 430 440 450 460 470 480 YNRYPGFKEK AANALKDIYG WTQTSLDDYP IKIVPAEDGS GAGAAVIAAL AQKRIAEGKS VGIIGA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification, cloning and sequence determination of the genes specifying hexokinase A and B from yeast." Stachelek C., Stachelek J., Swan J., Botstein D., Konigsberg W. Nucleic Acids Res. 14:945-963(1986) [PubMed: 3003701] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The primary structure of the yeast hexokinase PII gene (HXK2) which is responsible for glucose repression." Froehlich K.-U., Entian K.-D., Mecke D. Gene 36:105-111(1985) [PubMed: 3905511] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"Sequence of a 39,411 bp DNA fragment covering the left end of chromosome VII of Saccharomyces cerevisiae." Coissac E., Maillier E., Robineau S., Netter P. Yeast 12:1555-1562(1996) [PubMed: 8972578] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[4]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome VII." Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E. , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K. Nature 387:81-84(1997) [PubMed: 9169869] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[5]	"Identification of a gene encoding a novel zinc finger protein in Saccharomyces cerevisiae." Breitwieser W., Price C., Schuster T. Yeast 9:551-556(1993) [PubMed: 8322518] [Abstract] Cited for: NUCLEOTIDE SEQUENCE OF 1-247. Strain: ATCC 200060 / W303.
[6]	"Gene linkage of two-dimensional polyacrylamide gel electrophoresis resolved proteins from isogene families in Saccharomyces cerevisiae by microsequencing of in-gel trypsin generated peptides." Norbeck J., Blomberg A. Electrophoresis 16:149-156(1995) [PubMed: 7737086] [Abstract] Cited for: PROTEIN SEQUENCE OF 119-127; 176-185 AND 304-314. Strain: ATCC 38531 / Y41.
[7]	"In vivo phosphorylation site of hexokinase 2 in Saccharomyces cerevisiae." Kriegel T.M., Rush J., Vojtek A.B., Clifton D., Fraenkel D.G. Biochemistry 33:148-152(1994) [PubMed: 8286332] [Abstract] Cited for: PHOSPHORYLATION AT SER-15.
[8]	"Autophosphorylation-inactivation site of hexokinase 2 in Saccharomyces cerevisiae." Heidrich K., Otto A., Behlke J., Rush J., Wenzel K.W., Kriegel T. Biochemistry 36:1960-1964(1997) [PubMed: 9047292] [Abstract] Cited for: PHOSPHORYLATION AT SER-158.
[9]	"Hexokinase 2 from Saccharomyces cerevisiae: regulation of oligomeric structure by in vivo phosphorylation at serine-14." Behlke J., Heidrich K., Naumann M., Mueller E.-C., Otto A., Reuter R., Kriegel T. Biochemistry 37:11989-11995(1998) [PubMed: 9718324] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-19, PHOSPHORYLATION AT SER-15.
[10]	"Phosphoproteome analysis by mass spectrometry and its application to Saccharomyces cerevisiae." Ficarro S.B., McCleland M.L., Stukenberg P.T., Burke D.J., Ross M.M., Shabanowitz J., Hunt D.F., White F.M. Nat. Biotechnol. 20:301-305(2002) [PubMed: 11875433] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15, MASS SPECTROMETRY.
[11]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[12]	"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry." Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F. Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed: 17287358] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-396, MASS SPECTROMETRY.
[13]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-38; SER-158; SER-245; SER-272 AND SER-419, MASS SPECTROMETRY.
[14]	"Sequencing a protein by X-ray crystallography. II. Refinement of yeast hexokinase B co-