P04806 (HXKA_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Hexokinase-1
EC=2.7.1.1

Alternative name(s):
Hexokinase PI
Hexokinase-A

Gene names

Name:	HXK1
Synonyms:	HKA
Ordered Locus Names:	YFR053C

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	485 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

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 40800 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 Reference proteome
Gene Ontology (GO)
Biological_process	fructose import Inferred from genetic interaction PubMed 6300872. Source: SGD fructose metabolic process Inferred from mutant phenotype PubMed 6300872. Source: SGD glucose import Inferred from genetic interaction PubMed 6300872. Source: SGD glycolysis Inferred from direct assay PubMed 332086. Source: SGD mannose metabolic process Inferred from direct assay PubMed 332086. Source: SGD
Cellular_component	cytosol Inferred from direct assay PubMed 14562095. Source: SGD mitochondrion Inferred from direct assay PubMed 16962558. Source: SGD
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW hexokinase activity Inferred from direct assay PubMed 12611889PubMed 332086. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 485

485

Hexokinase-1

PRO_0000197601

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

Region

210 – 211

2

Substrate binding

Sites

Binding site

111

1

ATP Potential

Binding site

158

1

Substrate; via carbonyl oxygen

Binding site

237

1

Substrate

Binding site

269

1

Substrate

Binding site

302

1

Substrate

Amino acid modifications

Modified residue

15

1

Phosphoserine Ref.7 Ref.9 Ref.10 Ref.11 Ref.12

Modified residue

158

1

Phosphoserine Ref.12

Modified residue

245

1

Phosphoserine Ref.12

Modified residue

262

1

Phosphoserine Ref.12

Modified residue

272

1

Phosphoserine Ref.12

Modified residue

293

1

Phosphoserine Ref.12

Experimental info

Sequence conflict

61

1

G → V in CAA27202. Ref.1

Sequence conflict

103

1

H → R in CAA27202. Ref.1

Sequence conflict

194

1

N → K in CAA27202. Ref.1

Sequence conflict

244

1

V → C in CAA27202. Ref.1

Sequence conflict

356 – 357

2

EN → VF in AAA34698. Ref.2

Sequence conflict

364

1

I → M in CAA27202. Ref.1

Sequence conflict

388

1

I → T in AAA34698. Ref.2

Sequence conflict

444

1

D → EN in CAA27202. Ref.1

Sequence conflict

479 – 480

2

SL → VS in CAA27202. Ref.1

Secondary structure

1

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485

Helix Strand Turn

Details...

Helix

21 – 34

14

Helix

38 – 54

17

Beta strand

57 – 59

3

Beta strand

80 – 87

8

Beta strand

89 – 99

11

Beta strand

101 – 113

13

Helix

116 – 120

5

Helix

125 – 141

17

Beta strand

151 – 156

6

Helix

181 – 183

3

Helix

188 – 196

9

Helix

197 – 199

3

Beta strand

202 – 209

8

Helix

211 – 220

10

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 – 303

4

Helix

307 – 322

16

Turn

323 – 325

3

Beta strand

326 – 328

3

Turn

334 – 337

4

Helix

345 – 351

7

Helix

359 – 367

9

Helix

375 – 396

22

Helix

398 – 406

9

Beta strand

410 – 417

8

Helix

419 – 423

5

Helix

427 – 439

13

Turn

444 – 446

3

Beta strand

449 – 454

6

Turn

458 – 460

3

Helix

461 – 475

15

Beta strand

480 – 482

3

Sequences

	Sequence		Length	Mass (Da)
	P04806 [UniParc]. Last modified November 1, 1995. Version 2. Checksum: AF5C9DA8F17BC3D0	FASTA	485	53,738
	10 20 30 40 50 60 MVHLGPKKPQ ARKGSMADVP KELMDEIHQL EDMFTVDSET LRKVVKHFID ELNKGLTKKG 70 80 90 100 110 120 GNIPMIPGWV MEFPTGKESG NYLAIDLGGT NLRVVLVKLS GNHTFDTTQS KYKLPHDMRT 130 140 150 160 170 180 TKHQEELWSF IADSLKDFMV EQELLNTKDT LPLGFTFSYP ASQNKINEGI LQRWTKGFDI 190 200 210 220 230 240 PNVEGHDVVP LLQNEISKRE LPIEIVALIN DTVGTLIASY YTDPETKMGV IFGTGVNGAF 250 260 270 280 290 300 YDVVSDIEKL EGKLADDIPS NSPMAINCEY GSFDNEHLVL PRTKYDVAVD EQSPRPGQQA 310 320 330 340 350 360 FEKMTSGYYL GELLRLVLLE LNEKGLMLKD QDLSKLKQPY IMDTSYPARI EDDPFENLED 370 380 390 400 410 420 TDDIFQKDFG VKTTLPERKL IRRLCELIGT RAARLAVCGI AAICQKRGYK TGHIAADGSV 430 440 450 460 470 480 YNKYPGFKEA AAKGLRDIYG WTGDASKDPI TIVPAEDGSG AGAAVIAALS EKRIAEGKSL GIIGA

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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Complete nucleotide sequence of the hexokinase PI gene (HXK1) of Saccharomyces cerevisiae." Kopetzki E., Entian K.-D., Mecke D. Gene 39:95-102(1985) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"Analysis of the nucleotide sequence of chromosome VI from Saccharomyces cerevisiae." Murakami Y., Naitou M., Hagiwara H., Shibata T., Ozawa M., Sasanuma S., Sasanuma M., Tsuchiya Y., Soeda E., Yokoyama K., Yamazaki M., Tashiro H., Eki T. Nat. Genet. 10:261-268(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[4]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[5]	"Analysis of a 36.2 kb DNA sequence including the right telomere of chromosome VI from Saccharomyces cerevisiae." Eki T., Naitou M., Hagiwara H., Ozawa M., Sasanuma S., Sasanuma M., Tsuchiya Y., Shibata T., Hanaoka F., Murakami Y. Yeast 12:149-167(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[6]	"The adenine nucleotide binding site on yeast hexokinase PII. Affinity labeling of Lys-111 by pyridoxal 5'-diphospho-5'-adenosine." Tamura J.K., Ladime J.R., Cross R.L. J. Biol. Chem. 263:7907-7912(1988) [PubMed] [Europe PMC] [Abstract] Cited for: ATP-BINDING, PROTEIN SEQUENCE OF 104-112.
[7]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15, MASS SPECTROMETRY. Strain: 2124.
[8]	"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] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[9]	"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae." Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P. J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15, MASS SPECTROMETRY. Strain: ADR376.
[10]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15, MASS SPECTROMETRY.
[11]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15, MASS SPECTROMETRY.
[12]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15; SER-158; SER-245; SER-262; SER-272 AND SER-293, MASS SPECTROMETRY.
[13]	"Structure of a complex between yeast hexokinase A and glucose. I. Structure determination and refinement at 3.5-A resolution." Bennett W.S. Jr., Steitz T.A. J. Mol. Biol. 140:183-210(1980) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS).
+	Additional computationally mapped references.

Web resources

Worthington enzyme manual

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M14410 mRNA. Translation: AAA34698.1.
X03482 Genomic DNA. Translation: CAA27202.1.
D50617 Genomic DNA. Translation: BAA09292.1.
BK006940 Genomic DNA. Translation: DAA12496.1.

PIR

KIBYHA. S56308.

RefSeq

NP_116711.3. NM_001180018.3.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1HKG	X-ray	3.50	A	227-461	[»]
3B8A	X-ray	2.95	X	1-485	[»]

ProteinModelPortal

P04806.

SMR

P04806. Positions 15-485.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-5377N.

IntAct

P04806. 2 interactions.

MINT

MINT-561285.

STRING

4932.YFR053C.

2D gel databases

SWISS-2DPAGE

P04806.

Proteomic databases

PaxDb

P04806.

PeptideAtlas

P04806.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YFR053C; YFR053C; YFR053C.

GeneID

850614.

KEGG

sce:YFR053C.
sce:YFR057W.

Organism-specific databases

CYGD

YFR053c.

SGD

S000001949. HXK1.

Phylogenomic databases

eggNOG

COG5026.

GeneTree

ENSGT00390000017159.

HOGENOM

HOG000162670.

KO

K00844.

OMA

FDIPNVE.

OrthoDB

EOG4F21BM.

Enzyme and pathway databases

BRENDA

2.7.1.1. 984.

SABIO-RK

P04806.

UniPathway

UPA00242.

Gene expression databases

ArrayExpress

P04806.

Genevestigator

P04806.

GermOnline

YFR053C. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR001312. Hexokinase.
IPR022673. Hexokinase_C.
IPR019807. Hexokinase_CS.
IPR022672. Hexokinase_N.
[Graphical view]

PANTHER

PTHR19443. PTHR19443. 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

ChEMBL

CHEMBL4291.

EvolutionaryTrace

P04806.

NextBio

966508.

Entry information

Entry name

HXKA_YEAST

Accession

Primary (citable) accession number: P04806
Secondary accession number(s): D6VTT6

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 13, 1987
Last sequence update:	November 1, 1995
Last modified:	April 3, 2013
This is version 146 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program