Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P33284

- HXK_KLULA

UniProt

P33284 - HXK_KLULA

Protein

Hexokinase

Gene

RAG5

Organism
Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 107 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Catalytic activityi

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

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei111 – 1111ATPBy similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. glycolytic process Source: UniProtKB-KW
    2. 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

    BRENDAi2.7.1.1. 2825.
    SABIO-RKP33284.
    UniPathwayiUPA00242.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Hexokinase (EC:2.7.1.1)
    Gene namesi
    Name:RAG5
    Ordered Locus Names:KLLA0D11352g
    OrganismiKluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica)
    Taxonomic identifieri284590 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeKluyveromyces
    ProteomesiUP000000598: Chromosome D

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 485484HexokinasePRO_0000197608Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei15 – 151Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Interactioni

    Subunit structurei

    Monomer and homodimer. The monomeric form is active, the homodimeric form inactive.1 Publication

    Protein-protein interaction databases

    STRINGi28985.P33284.

    Structurei

    Secondary structure

    1
    485
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi21 – 3414
    Helixi38 – 5619
    Beta strandi57 – 593
    Beta strandi61 – 633
    Beta strandi79 – 10325
    Beta strandi105 – 1139
    Helixi118 – 1203
    Helixi123 – 14119
    Beta strandi150 – 1567
    Beta strandi158 – 1614
    Beta strandi163 – 1664
    Helixi187 – 19711
    Beta strandi202 – 2087
    Helixi210 – 22112
    Beta strandi225 – 24218
    Helixi243 – 2453
    Helixi247 – 2493
    Turni250 – 2523
    Beta strandi262 – 2665
    Helixi269 – 2713
    Turni272 – 2754
    Beta strandi277 – 2793
    Helixi283 – 2919
    Beta strandi292 – 2943
    Helixi299 – 3046
    Turni306 – 3083
    Helixi309 – 32214
    Beta strandi325 – 3273
    Helixi333 – 3364
    Helixi344 – 3518
    Helixi358 – 36811
    Helixi374 – 40633
    Beta strandi409 – 4179
    Helixi418 – 4225
    Helixi426 – 43813
    Helixi445 – 4473
    Beta strandi449 – 4546
    Turni458 – 4603
    Helixi461 – 47616
    Beta strandi480 – 4823

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3O08X-ray2.00A/B1-485[»]
    3O1BX-ray2.80A1-485[»]
    3O1WX-ray1.66A/B1-485[»]
    3O4WX-ray1.61A/B1-485[»]
    3O5BX-ray1.97A/B1-485[»]
    3O6WX-ray1.48A/B1-485[»]
    3O80X-ray2.18A1-485[»]
    3O8MX-ray1.42A1-485[»]
    4JAXX-ray2.26A/B/C/D/E/F1-485[»]
    ProteinModelPortaliP33284.
    SMRiP33284. Positions 18-484.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP33284.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini22 – 222201Hexokinase type-1Add
    BLAST
    Domaini224 – 472249Hexokinase type-2Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni151 – 17727Glucose-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.
    HOGENOMiHOG000162670.
    KOiK00844.
    OMAiARISACG.
    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.

    P33284-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVRLGPKKPP ARKGSMADVP ANLMEQIHGL ETLFTVSSEK MRSIVKHFIS    50
    ELDKGLSKKG GNIPMIPGWV VEYPTGKETG DFLALDLGGT NLRVVLVKLG 100
    GNHDFDTTQN KYRLPDHLRT GTSEQLWSFI AKCLKEFVDE WYPDGVSEPL 150
    PLGFTFSYPA SQKKINSGVL QRWTKGFDIE GVEGHDVVPM LQEQIEKLNI 200
    PINVVALIND TTGTLVASLY TDPQTKMGII IGTGVNGAYY DVVSGIEKLE 250
    GLLPEDIGPD SPMAINCEYG SFDNEHLVLP RTKYDVIIDE ESPRPGQQAF 300
    EKMTSGYYLG EIMRLVLLDL YDSGFIFKDQ DISKLKEAYV MDTSYPSKIE 350
    DDPFENLEDT DDLFKTNLNI ETTVVERKLI RKLAELVGTR AARLTVCGVS 400
    AICDKRGYKT AHIAADGSVF NRYPGYKEKA AQALKDIYNW DVEKMEDHPI 450
    QLVAAEDGSG VGAAIIACLT QKRLAAGKSV GIKGE 485
    Length:485
    Mass (Da):53,610
    Last modified:January 23, 2007 - v3
    Checksum:i3E93D80C92663FB0
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti206 – 2061A → R in CAA43855. (PubMed:8321195)Curated

    Mass spectrometryi

    Molecular mass is 53476±5 Da from positions 2 - 485. Determined by ESI. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X61680 Genomic DNA. Translation: CAA43855.1.
    CR382124 Genomic DNA. Translation: CAH00663.1.
    PIRiA48132.
    RefSeqiXP_453567.1. XM_453567.1.

    Genome annotation databases

    GeneIDi2893280.
    KEGGikla:KLLA0D11352g.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X61680 Genomic DNA. Translation: CAA43855.1 .
    CR382124 Genomic DNA. Translation: CAH00663.1 .
    PIRi A48132.
    RefSeqi XP_453567.1. XM_453567.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3O08 X-ray 2.00 A/B 1-485 [» ]
    3O1B X-ray 2.80 A 1-485 [» ]
    3O1W X-ray 1.66 A/B 1-485 [» ]
    3O4W X-ray 1.61 A/B 1-485 [» ]
    3O5B X-ray 1.97 A/B 1-485 [» ]
    3O6W X-ray 1.48 A/B 1-485 [» ]
    3O80 X-ray 2.18 A 1-485 [» ]
    3O8M X-ray 1.42 A 1-485 [» ]
    4JAX X-ray 2.26 A/B/C/D/E/F 1-485 [» ]
    ProteinModelPortali P33284.
    SMRi P33284. Positions 18-484.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 28985.P33284.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 2893280.
    KEGGi kla:KLLA0D11352g.

    Phylogenomic databases

    eggNOGi COG5026.
    HOGENOMi HOG000162670.
    KOi K00844.
    OMAi ARISACG.
    OrthoDBi EOG79SF68.

    Enzyme and pathway databases

    UniPathwayi UPA00242 .
    BRENDAi 2.7.1.1. 2825.
    SABIO-RK P33284.

    Miscellaneous databases

    EvolutionaryTracei P33284.

    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. "The hexokinase gene is required for transcriptional regulation of the glucose transporter gene RAG1 in Kluyveromyces lactis."
      Prior C., Mamessier P., Fukuhara H., Chen X.J., Wesolowski-Louvel M.
      Mol. Cell. Biol. 13:3882-3889(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 76492 / CBS 2359/152 / CLIB 210 and PM6-7A.
    2. "Genome evolution in yeasts."
      Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.
      , Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., Wincker P., Souciet J.-L.
      Nature 430:35-44(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37.
    3. "The unique hexokinase of Kluyveromyces lactis. Molecular and functional characterization and evaluation of a role in glucose signaling."
      Baer D., Golbik R., Huebner G., Lilie H., Mueller E.-C., Naumann M., Otto A., Reuter R., Breunig K.D., Kriegel T.M.
      J. Biol. Chem. 278:39280-39286(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-21; 136-163 AND 198-226, MASS SPECTROMETRY, SUBUNIT, PHOSPHORYLATION AT SER-15.
      Strain: ATCC 76492 / CBS 2359/152 / CLIB 210.

    Entry informationi

    Entry nameiHXK_KLULA
    AccessioniPrimary (citable) accession number: P33284
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1994
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 107 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    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

    External Data

    Dasty 3