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P04807 (HXKB_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 153. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Hexokinase-2

EC=2.7.1.1
Alternative name(s):
Hexokinase PII
Hexokinase-B
Gene names
Name:HXK2
Synonyms:HEX1, HKB
Ordered Locus Names:YGL253W
ORF Names:NRB486
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length486 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.

Contains 1 hexokinase type-1 domain.

Contains 1 hexokinase type-2 domain.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.10
Chain2 – 486485Hexokinase-2
PRO_0000197602

Regions

Domain21 – 223203Hexokinase type-1
Domain225 – 473249Hexokinase type-2
Nucleotide binding86 – 916ATP By similarity
Nucleotide binding307 – 3082ATP By similarity
Nucleotide binding344 – 3485ATP By similarity
Nucleotide binding419 – 4235ATP By similarity
Region175 – 1762Substrate binding By similarity
Region210 – 2112Substrate binding By similarity

Sites

Binding site1111ATP Potential
Binding site1581Substrate; via carbonyl oxygen By similarity
Binding site2371Substrate By similarity
Binding site2691Substrate By similarity
Binding site3021Substrate By similarity

Amino acid modifications

Modified residue151Phosphoserine Ref.8 Ref.10 Ref.13
Modified residue381Phosphothreonine Ref.12
Modified residue1581Phosphoserine Ref.9 Ref.12
Modified residue2451Phosphoserine Ref.13

Experimental info

Sequence conflict291N → I in CAA27203. Ref.1
Sequence conflict331I → N in AAA34697. Ref.2
Sequence conflict331I → N in AAA34699. Ref.2
Sequence conflict611G → V in CAA27203. Ref.1
Sequence conflict1971T → S in CAA27203. Ref.1
Sequence conflict2021P → H in AAA34699. Ref.2
Sequence conflict421 – 4222YN → ST in AAA34697. Ref.2
Sequence conflict421 – 4222YN → ST in AAA34699. Ref.2
Sequence conflict444 – 4452TS → PH in AAA34697. Ref.2
Sequence conflict444 – 4452TS → PH in AAA34699. Ref.2
Sequence conflict4531I → V in AAA34697. Ref.2
Sequence conflict4531I → V in AAA34699. Ref.2
Sequence conflict4621A → P in AAA34697. Ref.2
Sequence conflict4621A → P in AAA34699. Ref.2

Secondary structure

........................................................................ 486
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P04807 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: D55FF3F8992B2FEF

FASTA48653,942
        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 

« Hide

References

« Hide '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]"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] [Europe PMC] [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] [Europe PMC] [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. expand/collapse author list , 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[5]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[6]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE OF 1-247.
Strain: ATCC 200060 / W303.
[7]"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] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 119-127; 176-185 AND 304-314.
Strain: ATCC 38531 / Y41.
[8]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-15.
[9]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-158.
[10]"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] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-19, PHOSPHORYLATION AT SER-15.
[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] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[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 THR-38 AND SER-158, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15 AND SER-245, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
+Additional computationally mapped references.

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.
BK006941 Genomic DNA. Translation: DAA07866.1.
PIRKIBYHB. S61608.
RefSeqNP_011261.1. NM_001181119.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1IG8X-ray2.20A1-486[»]
2YHXX-ray2.10A152-471[»]
ProteinModelPortalP04807.
SMRP04807. Positions 18-486.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid33026. 150 interactions.
DIPDIP-2380N.
IntActP04807. 3 interactions.
MINTMINT-2784874.
STRING4932.YGL253W.

2D gel databases

SWISS-2DPAGEP04807.

Proteomic databases

MaxQBP04807.
PaxDbP04807.
PeptideAtlasP04807.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYGL253W; YGL253W; YGL253W.
GeneID852639.
KEGGsce:YGL253W.

Organism-specific databases

SGDS000003222. HXK2.

Phylogenomic databases

eggNOGCOG5026.
GeneTreeENSGT00390000017159.
HOGENOMHOG000162670.
KOK00844.
OMAPEMKIGC.
OrthoDBEOG79SF68.

Enzyme and pathway databases

BioCycYEAST:YGL253W-MONOMER.
BRENDA2.7.1.1. 984.
SABIO-RKP04807.
UniPathwayUPA00242.

Gene expression databases

GenevestigatorP04807.

Family and domain databases

InterProIPR001312. Hexokinase.
IPR022673. Hexokinase_C.
IPR019807. Hexokinase_CS.
IPR022672. Hexokinase_N.
[Graphical view]
PANTHERPTHR19443. PTHR19443. 1 hit.
PfamPF00349. Hexokinase_1. 1 hit.
PF03727. Hexokinase_2. 1 hit.
[Graphical view]
PRINTSPR00475. HEXOKINASE.
PROSITEPS00378. HEXOKINASES. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP04807.
NextBio971888.
PROP04807.

Entry information

Entry nameHXKB_YEAST
AccessionPrimary (citable) accession number: P04807
Secondary accession number(s): D6VV82, Q05838
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 153 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome VII

Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways