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. Ref.11
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	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW hexokinase activity Inferred from direct assay. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.9

Chain

2 – 486

485

Hexokinase-2

PRO_0000197602

Regions

Nucleotide binding

86 – 91

6

ATP By similarity

Nucleotide binding

307 – 308

2

ATP By similarity

Nucleotide binding

344 – 348

5

ATP By similarity

Nucleotide binding

419 – 423

5

ATP By similarity

Region

175 – 176

2

Substrate binding By similarity

Region

210 – 211

2

Substrate binding By similarity

Sites

Binding site

111

1

ATP Potential

Binding site

158

1

Substrate; via carbonyl oxygen By similarity

Binding site

237

1

Substrate By similarity

Binding site

269

1

Substrate By similarity

Binding site

302

1

Substrate By similarity

Amino acid modifications

Modified residue

15

1

Phosphoserine Ref.9 Ref.7 Ref.10

Modified residue

38

1

Phosphothreonine Ref.13

Modified residue

158

1

Phosphoserine Ref.13 Ref.8

Modified residue

245

1

Phosphoserine Ref.13

Modified residue

272

1

Phosphoserine Ref.13

Modified residue

396

1

Phosphoserine Ref.12

Modified residue

419

1

Phosphoserine Ref.13

Experimental info

Sequence conflict

29

1

N → I in CAA27203. Ref.1

Sequence conflict

33

1

I → N in AAA34697. Ref.2

Sequence conflict

33

1

I → N in 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. Ref.2

Sequence conflict

421 – 422

2

YN → ST in AAA34699. Ref.2

Sequence conflict

444 – 445

2

TS → PH in AAA34697. Ref.2

Sequence conflict

444 – 445

2

TS → PH in AAA34699. Ref.2

Sequence conflict

453

1

I → V in AAA34697. Ref.2

Sequence conflict

453

1

I → V in AAA34699. Ref.2

Sequence conflict

462

1

A → P in AAA34697. Ref.2

Sequence conflict

462

1

A → P in 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-ordinates and sequence at 2.1-A resolution." Anderson C.M., Stenkamp R.E., Steitz T.A. J. Mol. Biol. 123:15-33(1978) [PubMed: 355643] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
+	Additional computationally mapped references.

Web resources

Worthington enzyme manual

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X03483 Genomic DNA. Translation: CAA27203.1.
M11181 Genomic DNA. Translation: AAA34697.1.
M14411 mRNA. Translation: AAA34699.1.
X94357 Genomic DNA. Translation: CAA64134.1.
Z72775 Genomic DNA. Translation: CAA96973.1.
X67787 Genomic DNA. Translation: CAA48003.1.

PIR

KIBYHB. S61608.

RefSeq

NP_011261.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1IG8	X-ray	2.20	A	1-486	[»]
2YHX	X-ray	2.10	A	227-462	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-2380N.

IntAct

P04807. 2 interactions.

STRING

P04807.

2-D gel databases

SWISS-2DPAGE

P04807.

Proteomic databases

PeptideAtlas

P04807.

PRIDE

P04807.

Genome annotation databases

Ensembl

YGL253W; YGL253W; YGL253W; Saccharomyces cerevisiae. [Genome view]

GeneID

852639.

KEGG

sce:YGL253W.

NMPDR

fig|4932.3.peg.2364.

Organism-specific databases

CYGD

YGL253w.

SGD

S000003222. HXK2.

Phylogenomic databases

eggNOG

fuNOG05908.

HOGENOM

HBG522186.

OMA

VMDTSYP.

OrthoDB

EOG9X0P8P.

PhylomeDB

P04807.

Enzyme and pathway databases

BRENDA

2.7.1.1. 250.

Gene expression databases

ArrayExpress

P04807.

Genevestigator

P04807.

GermOnline

YGL253W. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR001312. Hexokinase.
IPR019807. Hexokinase_CS.
[Graphical view]

PANTHER

PTHR19443. Hexokinase. 1 hit.

Pfam

PF00349. Hexokinase_1. 1 hit.
PF03727. Hexokinase_2. 1 hit.
[Graphical view]

PRINTS

PR00475. HEXOKINASE.

PROSITE

PS00378. HEXOKINASES. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

971888.

Entry information

Entry name

HXKB_YEAST

Accession

Primary (citable) accession number: P04807
Secondary accession number(s): Q05838

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 13, 1987
Last sequence update:	January 23, 2007
Last modified:	January 19, 2010
This is version 116 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)