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P04807

- HXKB_YEAST

UniProt

P04807 - HXKB_YEAST

Protein

Hexokinase-2

Gene

HXK2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 154 (01 Oct 2014)
      Sequence version 4 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Main glucose phosphorylating enzyme. May play a regulatory role in both induction and repression of gene expression by glucose.

    Catalytic activityi

    ATP + D-hexose = ADP + D-hexose 6-phosphate.

    Enzyme regulationi

    Subject to allosteric control. Substrate inhibition by ATP.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei111 – 1111ATPSequence Analysis
    Binding sitei158 – 1581Substrate; via carbonyl oxygenBy similarity
    Binding sitei237 – 2371SubstrateBy similarity
    Binding sitei269 – 2691SubstrateBy similarity
    Binding sitei302 – 3021SubstrateBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi86 – 916ATPBy similarity
    Nucleotide bindingi307 – 3082ATPBy similarity
    Nucleotide bindingi344 – 3485ATPBy similarity
    Nucleotide bindingi419 – 4235ATPBy similarity

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. hexokinase activity Source: SGD

    GO - Biological processi

    1. carbohydrate phosphorylation Source: GOC
    2. fructose import Source: SGD
    3. fructose metabolic process Source: SGD
    4. glucose import Source: SGD
    5. glucose metabolic process Source: SGD
    6. glycolytic process Source: SGD
    7. mannose metabolic process Source: SGD
    8. regulation of transcription by glucose Source: SGD
    9. replicative cell aging Source: SGD

    Keywords - Molecular functioni

    Kinase, Transferase

    Keywords - Biological processi

    Glycolysis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciYEAST:YGL253W-MONOMER.
    BRENDAi2.7.1.1. 984.
    SABIO-RKP04807.
    UniPathwayiUPA00242.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Hexokinase-2 (EC:2.7.1.1)
    Alternative name(s):
    Hexokinase PII
    Hexokinase-B
    Gene namesi
    Name:HXK2
    Synonyms:HEX1, HKB
    Ordered Locus Names:YGL253W
    ORF Names:NRB486
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome VII

    Organism-specific databases

    SGDiS000003222. HXK2.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: SGD
    2. mitochondrion Source: SGD
    3. nucleus Source: SGD

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 486485Hexokinase-2PRO_0000197602Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei15 – 151Phosphoserine3 Publications
    Modified residuei38 – 381Phosphothreonine1 Publication
    Modified residuei158 – 1581Phosphoserine2 Publications
    Modified residuei245 – 2451Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP04807.
    PaxDbiP04807.
    PeptideAtlasiP04807.

    2D gel databases

    SWISS-2DPAGEP04807.

    Expressioni

    Gene expression databases

    GenevestigatoriP04807.

    Interactioni

    Subunit structurei

    Homodimer.

    Protein-protein interaction databases

    BioGridi33026. 150 interactions.
    DIPiDIP-2380N.
    IntActiP04807. 3 interactions.
    MINTiMINT-2784874.
    STRINGi4932.YGL253W.

    Structurei

    Secondary structure

    1
    486
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi21 – 3414
    Helixi38 – 5619
    Beta strandi79 – 879
    Beta strandi89 – 10315
    Beta strandi105 – 1139
    Helixi118 – 1203
    Helixi126 – 14217
    Beta strandi152 – 1565
    Beta strandi159 – 1624
    Helixi189 – 20012
    Beta strandi203 – 2097
    Helixi211 – 22212
    Beta strandi226 – 24217
    Helixi244 – 2463
    Helixi248 – 2503
    Beta strandi254 – 2563
    Beta strandi264 – 2674
    Turni271 – 2766
    Beta strandi278 – 2803
    Helixi284 – 2929
    Beta strandi293 – 2953
    Helixi300 – 3056
    Helixi307 – 3093
    Helixi310 – 32314
    Beta strandi326 – 3305
    Turni334 – 3363
    Helixi345 – 3528
    Beta strandi355 – 3573
    Helixi359 – 36911
    Helixi375 – 39622
    Helixi398 – 40710
    Beta strandi410 – 4189
    Helixi419 – 4235
    Helixi427 – 43913
    Helixi446 – 4483
    Beta strandi449 – 4557
    Turni459 – 4613
    Helixi462 – 47110

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1IG8X-ray2.20A1-486[»]
    2YHXX-ray2.10A152-471[»]
    ProteinModelPortaliP04807.
    SMRiP04807. Positions 18-486.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP04807.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini21 – 223203Hexokinase type-1Add
    BLAST
    Domaini225 – 473249Hexokinase type-2Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni175 – 1762Substrate bindingBy similarity
    Regioni210 – 2112Substrate bindingBy similarity

    Sequence similaritiesi

    Belongs to the hexokinase family.Curated
    Contains 1 hexokinase type-1 domain.Curated
    Contains 1 hexokinase type-2 domain.Curated

    Phylogenomic databases

    eggNOGiCOG5026.
    GeneTreeiENSGT00390000017159.
    HOGENOMiHOG000162670.
    KOiK00844.
    OMAiPEMKIGC.
    OrthoDBiEOG79SF68.

    Family and domain databases

    InterProiIPR001312. Hexokinase.
    IPR022673. Hexokinase_C.
    IPR019807. Hexokinase_CS.
    IPR022672. Hexokinase_N.
    [Graphical view]
    PANTHERiPTHR19443. PTHR19443. 1 hit.
    PfamiPF00349. Hexokinase_1. 1 hit.
    PF03727. Hexokinase_2. 1 hit.
    [Graphical view]
    PRINTSiPR00475. HEXOKINASE.
    PROSITEiPS00378. HEXOKINASES. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P04807-1 [UniParc]FASTAAdd to Basket

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    MVHLGPKKPQ ARKGSMADVP KELMQQIENF EKIFTVPTET LQAVTKHFIS    50
    ELEKGLSKKG GNIPMIPGWV MDFPTGKESG DFLAIDLGGT NLRVVLVKLG 100
    GDRTFDTTQS KYRLPDAMRT TQNPDELWEF IADSLKAFID EQFPQGISEP 150
    IPLGFTFSFP ASQNKINEGI LQRWTKGFDI PNIENHDVVP MLQKQITKRN 200
    IPIEVVALIN DTTGTLVASY YTDPETKMGV IFGTGVNGAY YDVCSDIEKL 250
    QGKLSDDIPP SAPMAINCEY GSFDNEHVVL PRTKYDITID EESPRPGQQT 300
    FEKMSSGYYL GEILRLALMD MYKQGFIFKN QDLSKFDKPF VMDTSYPARI 350
    EEDPFENLED TDDLFQNEFG INTTVQERKL IRRLSELIGA RAARLSVCGI 400
    AAICQKRGYK TGHIAADGSV YNRYPGFKEK AANALKDIYG WTQTSLDDYP 450
    IKIVPAEDGS GAGAAVIAAL AQKRIAEGKS VGIIGA 486
    Length:486
    Mass (Da):53,942
    Last modified:January 23, 2007 - v4
    Checksum:iD55FF3F8992B2FEF
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti29 – 291N → I in CAA27203. (PubMed:3003701)Curated
    Sequence conflicti33 – 331I → N in AAA34697. (PubMed:3905511)Curated
    Sequence conflicti33 – 331I → N in AAA34699. (PubMed:3905511)Curated
    Sequence conflicti61 – 611G → V in CAA27203. (PubMed:3003701)Curated
    Sequence conflicti197 – 1971T → S in CAA27203. (PubMed:3003701)Curated
    Sequence conflicti202 – 2021P → H in AAA34699. (PubMed:3905511)Curated
    Sequence conflicti421 – 4222YN → ST in AAA34697. (PubMed:3905511)Curated
    Sequence conflicti421 – 4222YN → ST in AAA34699. (PubMed:3905511)Curated
    Sequence conflicti444 – 4452TS → PH in AAA34697. (PubMed:3905511)Curated
    Sequence conflicti444 – 4452TS → PH in AAA34699. (PubMed:3905511)Curated
    Sequence conflicti453 – 4531I → V in AAA34697. (PubMed:3905511)Curated
    Sequence conflicti453 – 4531I → V in AAA34699. (PubMed:3905511)Curated
    Sequence conflicti462 – 4621A → P in AAA34697. (PubMed:3905511)Curated
    Sequence conflicti462 – 4621A → P in AAA34699. (PubMed:3905511)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    PIRiS61608. KIBYHB.
    RefSeqiNP_011261.1. NM_001181119.1.

    Genome annotation databases

    EnsemblFungiiYGL253W; YGL253W; YGL253W.
    GeneIDi852639.
    KEGGisce:YGL253W.

    Cross-referencesi

    Web resourcesi

    Worthington enzyme manual

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    PIRi S61608. KIBYHB.
    RefSeqi NP_011261.1. NM_001181119.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1IG8 X-ray 2.20 A 1-486 [» ]
    2YHX X-ray 2.10 A 152-471 [» ]
    ProteinModelPortali P04807.
    SMRi P04807. Positions 18-486.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 33026. 150 interactions.
    DIPi DIP-2380N.
    IntActi P04807. 3 interactions.
    MINTi MINT-2784874.
    STRINGi 4932.YGL253W.

    2D gel databases

    SWISS-2DPAGE P04807.

    Proteomic databases

    MaxQBi P04807.
    PaxDbi P04807.
    PeptideAtlasi P04807.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YGL253W ; YGL253W ; YGL253W .
    GeneIDi 852639.
    KEGGi sce:YGL253W.

    Organism-specific databases

    SGDi S000003222. HXK2.

    Phylogenomic databases

    eggNOGi COG5026.
    GeneTreei ENSGT00390000017159.
    HOGENOMi HOG000162670.
    KOi K00844.
    OMAi PEMKIGC.
    OrthoDBi EOG79SF68.

    Enzyme and pathway databases

    UniPathwayi UPA00242 .
    BioCyci YEAST:YGL253W-MONOMER.
    BRENDAi 2.7.1.1. 984.
    SABIO-RK P04807.

    Miscellaneous databases

    EvolutionaryTracei P04807.
    NextBioi 971888.
    PROi P04807.

    Gene expression databases

    Genevestigatori P04807.

    Family and domain databases

    InterProi IPR001312. Hexokinase.
    IPR022673. Hexokinase_C.
    IPR019807. Hexokinase_CS.
    IPR022672. Hexokinase_N.
    [Graphical view ]
    PANTHERi PTHR19443. PTHR19443. 1 hit.
    Pfami PF00349. Hexokinase_1. 1 hit.
    PF03727. Hexokinase_2. 1 hit.
    [Graphical view ]
    PRINTSi PR00475. HEXOKINASE.
    PROSITEi PS00378. HEXOKINASES. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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. 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. 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).

    Entry informationi

    Entry nameiHXKB_YEAST
    AccessioniPrimary (citable) accession number: P04807
    Secondary accession number(s): D6VV82, Q05838
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 13, 1987
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 154 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    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.1 Publication

    Keywords - Technical termi

    3D-structure, Allosteric enzyme, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families
    4. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    5. Yeast chromosome VII
      Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

    External Data

    Dasty 3