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Q9NFT9

- HXK1_DROME

UniProt

Q9NFT9 - HXK1_DROME

Protein

Hexokinase type 1

Gene

Hex-t1

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 101 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      Previous versions | rss
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    Functioni

    Catalytic activityi

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

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei88 – 881ATPBy similarity

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. fructokinase activity Source: RefGenome
    3. glucokinase activity Source: RefGenome
    4. mannokinase activity Source: RefGenome

    GO - Biological processi

    1. carbohydrate phosphorylation Source: GOC
    2. cellular glucose homeostasis Source: RefGenome
    3. glucose 6-phosphate metabolic process Source: GOC
    4. glycolytic process Source: UniProtKB-KW
    5. hexose metabolic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Kinase, Transferase

    Keywords - Biological processi

    Glycolysis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_218382. Glucose transport.
    REACT_80959. Regulation of Glucokinase by Glucokinase Regulatory Protein.
    UniPathwayiUPA00242.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Hexokinase type 1 (EC:2.7.1.1)
    Gene namesi
    Name:Hex-t1
    Synonyms:Hex
    ORF Names:CG33102
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 3R

    Organism-specific databases

    FlyBaseiFBgn0042711. Hex-t1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: RefGenome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 465465Hexokinase type 1PRO_0000197596Add
    BLAST

    Proteomic databases

    PRIDEiQ9NFT9.

    Expressioni

    Gene expression databases

    BgeeiQ9NFT9.

    Interactioni

    Protein-protein interaction databases

    STRINGi7227.FBpp0084382.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9NFT9.
    SMRiQ9NFT9. Positions 21-449.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini13 – 209197Hexokinase type-1Add
    BLAST
    Domaini214 – 449236Hexokinase type-2Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni139 – 16527Glucose-bindingSequence AnalysisAdd
    BLAST

    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.
    InParanoidiQ9NFT9.
    KOiK00844.
    OMAiPTNCRIM.
    OrthoDBiEOG7TBC24.
    PhylomeDBiQ9NFT9.

    Family and domain databases

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

    Sequencei

    Sequence statusi: Complete.

    Q9NFT9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MANTFNPEED FPEVYKVCKL FNPSIDDLEK IKNAMDREIT MGLSRDHHDR    50
    STVPCHLSYV QDLPTGRERG QFLALEMMPT NCRIMLVKFS SERDIYTSSK 100
    CVIMPHTVAA GRGTEVFTFL ATSIANFVKE KKVDKDNLPL GIAFAFTLKK 150
    LALDVGILVS WTKEFGAQGA IGKDVVQLLR DALAKFPEIS VDVMGIINVG 200
    AGSLLALCWA QPDTRIGLIM GSIANSCYVE RVERCETYEG DEYRKLMIIN 250
    SDWAHFGDTG QLDFIRNEYD RQLDTESINP GTRIYEKFSG ALCMGELVRI 300
    IVLRLMKSGA IFAEDRRDYI GIQWKLDMVS LIEIVSDPPG VYTKAQEVMD 350
    KFRIRHCKER DLAALKYICD TVTNRAAMLV ASGVSCLIDR MRLPQISIAV 400
    DGGIYRLHPT FSTVLNKYTR LLADPNYNFE FVITQDSCGV GAAIMAGMAH 450
    ANKYKTDAKL FTMDY 465
    Length:465
    Mass (Da):52,260
    Last modified:October 1, 2000 - v1
    Checksum:i67B611920D56B6DD
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti33 – 331N → H in strain: HFL97e3_12 and ZIM(S)e3_24. 1 Publication
    Natural varianti243 – 2431Y → F in strain: DPF96e3_3.0, DPF96e3_4.2, DPF96e3_23.1, DPF96e3_74.2, VT97e3_41, SC96e3_12.3, HFL97e3_8, HFL97e3_12, HFL97e3_15, ZIM(S)e3_24 and ZIM(S)e3_35. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF257590 Genomic DNA. Translation: AAG22891.1.
    AF257591 Genomic DNA. Translation: AAG22893.1.
    AF257592 Genomic DNA. Translation: AAG22895.1.
    AF257593 Genomic DNA. Translation: AAG22897.1.
    AF257594 Genomic DNA. Translation: AAG22899.1.
    AF257595 Genomic DNA. Translation: AAG22901.1.
    AF257596 Genomic DNA. Translation: AAG22903.1.
    AF257597 Genomic DNA. Translation: AAG22905.1.
    AF257598 Genomic DNA. Translation: AAG22907.1.
    AF257599 Genomic DNA. Translation: AAG22909.1.
    AF257600 Genomic DNA. Translation: AAG22911.1.
    AF257601 Genomic DNA. Translation: AAG22913.1.
    AF257602 Genomic DNA. Translation: AAG22915.1.
    AF257603 Genomic DNA. Translation: AAG22917.1.
    AF257604 Genomic DNA. Translation: AAG22919.1.
    AF257605 Genomic DNA. Translation: AAG22921.1.
    AF257606 Genomic DNA. Translation: AAG22923.1.
    AF257607 Genomic DNA. Translation: AAG22925.1.
    AF257608 Genomic DNA. Translation: AAG22927.1.
    AJ271350 Genomic DNA. Translation: CAB72131.1.
    AE014297 Genomic DNA. Translation: AAF56591.2.
    BT015307 mRNA. Translation: AAT94535.1.
    RefSeqiNP_788744.1. NM_176567.2.
    UniGeneiDm.21469.

    Genome annotation databases

    EnsemblMetazoaiFBtr0085010; FBpp0084382; FBgn0042711.
    GeneIDi117364.
    KEGGidme:Dmel_CG33102.
    UCSCiCG33102-RA. d. melanogaster.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF257590 Genomic DNA. Translation: AAG22891.1 .
    AF257591 Genomic DNA. Translation: AAG22893.1 .
    AF257592 Genomic DNA. Translation: AAG22895.1 .
    AF257593 Genomic DNA. Translation: AAG22897.1 .
    AF257594 Genomic DNA. Translation: AAG22899.1 .
    AF257595 Genomic DNA. Translation: AAG22901.1 .
    AF257596 Genomic DNA. Translation: AAG22903.1 .
    AF257597 Genomic DNA. Translation: AAG22905.1 .
    AF257598 Genomic DNA. Translation: AAG22907.1 .
    AF257599 Genomic DNA. Translation: AAG22909.1 .
    AF257600 Genomic DNA. Translation: AAG22911.1 .
    AF257601 Genomic DNA. Translation: AAG22913.1 .
    AF257602 Genomic DNA. Translation: AAG22915.1 .
    AF257603 Genomic DNA. Translation: AAG22917.1 .
    AF257604 Genomic DNA. Translation: AAG22919.1 .
    AF257605 Genomic DNA. Translation: AAG22921.1 .
    AF257606 Genomic DNA. Translation: AAG22923.1 .
    AF257607 Genomic DNA. Translation: AAG22925.1 .
    AF257608 Genomic DNA. Translation: AAG22927.1 .
    AJ271350 Genomic DNA. Translation: CAB72131.1 .
    AE014297 Genomic DNA. Translation: AAF56591.2 .
    BT015307 mRNA. Translation: AAT94535.1 .
    RefSeqi NP_788744.1. NM_176567.2.
    UniGenei Dm.21469.

    3D structure databases

    ProteinModelPortali Q9NFT9.
    SMRi Q9NFT9. Positions 21-449.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 7227.FBpp0084382.

    Proteomic databases

    PRIDEi Q9NFT9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0085010 ; FBpp0084382 ; FBgn0042711 .
    GeneIDi 117364.
    KEGGi dme:Dmel_CG33102.
    UCSCi CG33102-RA. d. melanogaster.

    Organism-specific databases

    CTDi 117364.
    FlyBasei FBgn0042711. Hex-t1.

    Phylogenomic databases

    eggNOGi COG5026.
    GeneTreei ENSGT00390000017159.
    InParanoidi Q9NFT9.
    KOi K00844.
    OMAi PTNCRIM.
    OrthoDBi EOG7TBC24.
    PhylomeDBi Q9NFT9.

    Enzyme and pathway databases

    UniPathwayi UPA00242 .
    Reactomei REACT_218382. Glucose transport.
    REACT_80959. Regulation of Glucokinase by Glucokinase Regulatory Protein.

    Miscellaneous databases

    GenomeRNAii 117364.
    NextBioi 841931.

    Gene expression databases

    Bgeei Q9NFT9.

    Family and domain databases

    InterProi IPR001312. Hexokinase.
    IPR022673. Hexokinase_C.
    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.
    ProtoNeti Search...

    Publicationsi

    1. "Contrasting molecular population genetics of four hexokinases in Drosophila melanogaster, D. simulans and D. yakuba."
      Duvernell D.D., Eanes W.F.
      Genetics 156:1191-1201(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS HIS-33 AND PHE-243.
      Strain: DPF96e3_23.1, DPF96e3_3.0, DPF96e3_4.2, DPF96e3_74.2, DPF96e3_84.3, HFL97e3_12, HFL97e3_13, HFL97e3_15, HFL97e3_16, HFL97e3_8, SC96e3_12.3, SC96e3_19.4, VT97e3_1, VT97e3_39, VT97e3_41, ZIM(H)e3_38.4, ZIM(H)e3_39, ZIM(S)e3_24 and ZIM(S)e3_35.
    2. Deobagkar D.D., Kulkarni G.V., Deobagkar D.N.
      Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: Oregon-K.
    3. "The genome sequence of Drosophila melanogaster."
      Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
      , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
      Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Berkeley.
    4. Cited for: GENOME REANNOTATION.
      Strain: Berkeley.
    5. Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M., Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.
      Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Berkeley.
      Tissue: Testis.

    Entry informationi

    Entry nameiHXK1_DROME
    AccessioniPrimary (citable) accession number: Q9NFT9
    Secondary accession number(s): Q6AWE1, Q9VBF1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 21, 2001
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 101 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programDrosophila annotation project

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Drosophila
      Drosophila: entries, gene names and cross-references to FlyBase
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3