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Protein

N-acetylglucosamine kinase 1

Gene

HXK1

Organism
Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Component of the N-acetylglucosamine catabolic cascade that phosphorylates N-acetylglucosamine (GlcNAc), and allows the unique ability to utilise GlcNAc as carbon source. Converts GlcNAc to GlcNAc-6-P. Also able to phosphorylate glucose, glucosamine (GlcN), and mannose. Galactose, fructose, N-acetylmannosamine (ManNAc), mannosamine (ManN), galactosamine (GalN), and N-acetylgalactosamine (GalNAc) are not phosphorylated by HXK1. GlcNAc metabolism is closely associated with virulence and morphogenesis, and is involved in the cell wall synthesis. Acts both as a repressor and an activator of genes involved in maintaining cellular homeostasis. Contributes to white-opaque morphological transition and plays a role as a filamentation repressor.7 Publications

Catalytic activityi

ATP + N-acetyl-D-glucosamine = ADP + N-acetyl-D-glucosamine 6-phosphate.1 Publication

Kineticsi

  1. KM=375.5 µM for N-acetylglucosamine (GlcNAc)1 Publication
  2. KM=482.5 µM for glucose1 Publication
  3. KM=426.0 µM for mannose1 Publication

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Kinase, Transferase

    Keywords - Biological processi

    Cell wall biogenesis/degradation, Glycolysis, Virulence

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.1.59. 1096.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    N-acetylglucosamine kinase 11 Publication (EC:2.7.1.591 Publication)
    Short name:
    GlcNAc kinase 1Curated
    Alternative name(s):
    Hexokinase 1Curated
    Gene namesi
    Name:HXK11 Publication
    Synonyms:NAG51 Publication
    ORF Names:CaO19.2154Imported, CaO19.9701Imported
    OrganismiCandida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
    Taxonomic identifieri237561 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDebaryomycetaceaeCandida/Lodderomyces cladeCandida
    ProteomesiUP000000559 Componenti: Unassembled WGS sequence

    Organism-specific databases

    CGDiCAL0005368. HXK1.
    CAL0079099. HXK1.

    Subcellular locationi

    • Cytoplasm 1 Publication
    • Nucleus 1 Publication
    • Mitochondrion 1 Publication

    • Note: Localized in cytoplasm and nucleus in a filamentation-inducing medium whereas in 2% GlcNAc, where catabolism is more prominent, a major fraction is seen to be present in cytoplasm. Localizes to mitochondria in non-fermentative carbon sources like ethanol.1 Publication

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm, Mitochondrion, Nucleus

    Pathology & Biotechi

    Disruption phenotypei

    Greatly retards the growth of cells using GlcNAc as the sole carbon source, increases resistance against farnesol, and attenuates the virulence in a mouse systemic infection model. Leads to derepression of opaque specific gene expression, as well as to constitutive filamentous growth and hyperfilamentation in filamentation-inducing conditions.6 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 493493N-acetylglucosamine kinase 1PRO_0000431722Add
    BLAST

    Expressioni

    Inductioni

    Expression is induced by N-acetylglucosamine (GlcNAc), by the alpha pheromone, and in filamentation-inducing media.4 Publications

    Interactioni

    Subunit structurei

    Interacts with histone deacetylase SIR2 under filamentation-inducing conditions.1 Publication

    Protein-protein interaction databases

    STRINGi5476.CAL0005368.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini27 – 490464HexokinasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni79 – 221143Hexokinase small subdomainPROSITE-ProRule annotationAdd
    BLAST
    Regioni222 – 479258Hexokinase large subdomainPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the hexokinase family.PROSITE-ProRule annotationCurated
    Contains 1 hexokinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG5026.
    InParanoidiQ59RG5.
    KOiK00844.
    OrthoDBiEOG7NGQMP.

    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.
    PROSITEiPS51748. HEXOKINASE_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q59RW5-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MTETSISGLR GPKSMYFMEI VDVSSQESSV LSSIVESFTS AVSASNLGVY
    60 70 80 90 100
    SDEVLCDIKS SLKENSPITM LPNYNVSPTG DEHGQYLVID LGGSTLRIAV
    110 120 130 140 150
    VDISKPHPNL SRSERITIVV EKSWIIGNDF KRIDGEFFKY IGSKINEILM
    160 170 180 190 200
    GQNVIDVKSV INTGITWSFP LETTDYNRGK IKHVSKGYTV GEDIYDKDLK
    210 220 230 240 250
    MVLEDTLRQE YGLTLDVQSI LNDSLAVYSA GCFIDSKMKL AMVLGTGINM
    260 270 280 290 300
    CCSLKRSSDI HPSKMLADAT LFNCELSLFG QNLCKDFATK YDIIIDKRFA
    310 320 330 340 350
    GFSHHFKTFM EPDPITKTLF QPHELMTSGR YLPELTRLVV VDLIEAGEIF
    360 370 380 390 400
    QNVDHQQMYQ EYGGFSGELM CFVHENDDYD DIHDKLCKAY GWTTVGLSDI
    410 420 430 440 450
    VCLKEVVSCI IKRAAFIVAN AIIAFFKLLG SDELGGDVTI GYVGSVLNYF
    460 470 480 490
    HKYRRLIVEY VNNAEEAKGI KVDLKLIENS SIIGAAIGAA YHK
    Length:493
    Mass (Da):54,902
    Last modified:April 26, 2005 - v1
    Checksum:iC3D42FD735B13DF0
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti302 – 3021F → L in allele: CaO19.9701. Imported
    Natural varianti370 – 3701M → I in allele: CaO19.9701. Imported
    Natural varianti463 – 4631N → S in allele: CaO19.9701. Imported

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AACQ01000158 Genomic DNA. Translation: EAK93243.1.
    AACQ01000162 Genomic DNA. Translation: EAK93093.1.
    RefSeqiXP_712286.1. XM_707193.1.
    XP_712429.1. XM_707336.1.

    Genome annotation databases

    GeneIDi3645964.
    3646114.
    KEGGical:CaO19.2154.
    cal:CaO19.9701.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AACQ01000158 Genomic DNA. Translation: EAK93243.1.
    AACQ01000162 Genomic DNA. Translation: EAK93093.1.
    RefSeqiXP_712286.1. XM_707193.1.
    XP_712429.1. XM_707336.1.

    3D structure databases

    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi5476.CAL0005368.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    GeneIDi3645964.
    3646114.
    KEGGical:CaO19.2154.
    cal:CaO19.9701.

    Organism-specific databases

    CGDiCAL0005368. HXK1.
    CAL0079099. HXK1.

    Phylogenomic databases

    eggNOGiCOG5026.
    InParanoidiQ59RG5.
    KOiK00844.
    OrthoDBiEOG7NGQMP.

    Enzyme and pathway databases

    BRENDAi2.7.1.59. 1096.

    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.
    PROSITEiPS51748. HEXOKINASE_2. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: SC5314 / ATCC MYA-2876.
    2. "The inducible N-acetylglucosamine catabolic pathway gene cluster in Candida albicans: discrete N-acetylglucosamine-inducible factors interact at the promoter of NAG1."
      Kumar M.J., Jamaluddin M.S., Natarajan K., Kaur D., Datta A.
      Proc. Natl. Acad. Sci. U.S.A. 97:14218-14223(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION, INDUCTION.
    3. "Identification and characterization of the genes for N-acetylglucosamine kinase and N-acetylglucosamine-phosphate deacetylase in the pathogenic fungus Candida albicans."
      Yamada-Okabe T., Sakamori Y., Mio T., Yamada-Okabe H.
      Eur. J. Biochem. 268:2498-2505(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION, DISRUPTION PHENOTYPE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
    4. "Attenuation of virulence and changes in morphology in Candida albicans by disruption of the N-acetylglucosamine catabolic pathway."
      Singh P., Ghosh S., Datta A.
      Infect. Immun. 69:7898-7903(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE, FUNCTION.
    5. "Use of the porcine intestinal epithelium (PIE)-assay to analyze early stages of colonization by the human fungal pathogen Candida albicans."
      Wendland J., Hellwig D., Walther A., Sickinger S., Shadkchan Y., Martin R., Bauer J., Osherov N., Tretiakov A., Saluz H.P.
      J. Basic Microbiol. 46:513-523(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE, FUNCTION.
    6. "The role of nutrient regulation and the Gpa2 protein in the mating pheromone response of C. albicans."
      Bennett R.J., Johnson A.D.
      Mol. Microbiol. 62:100-119(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    7. "N-acetylglucosamine utilization by Saccharomyces cerevisiae based on expression of Candida albicans NAG genes."
      Wendland J., Schaub Y., Walther A.
      Appl. Environ. Microbiol. 75:5840-5845(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    8. "Identification of GIG1, a GlcNAc-induced gene in Candida albicans needed for normal sensitivity to the chitin synthase inhibitor nikkomycin Z."
      Gunasekera A., Alvarez F.J., Douglas L.M., Wang H.X., Rosebrock A.P., Konopka J.B.
      Eukaryot. Cell 9:1476-1483(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    9. "N-acetylglucosamine (GlcNAc) induction of hyphal morphogenesis and transcriptional responses in Candida albicans are not dependent on its metabolism."
      Naseem S., Gunasekera A., Araya E., Konopka J.B.
      J. Biol. Chem. 286:28671-28680(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE, FUNCTION.
    10. "N-acetylglucosamine kinase, HXK1 is involved in morphogenetic transition and metabolic gene expression in Candida albicans."
      Rao K.H., Ghosh S., Natarajan K., Datta A.
      PLoS ONE 8:E53638-E53638(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE, INDUCTION, INTERACTION WITH SIR2, FUNCTION, SUBCELLULAR LOCATION.
    11. "N-acetylglucosamine kinase, HXK1 contributes to white-opaque morphological transition in Candida albicans."
      Rao K.H., Ruhela D., Ghosh S., Abdin M.Z., Datta A.
      Biochem. Biophys. Res. Commun. 445:138-144(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE.

    Entry informationi

    Entry nameiHXK1_CANAL
    AccessioniPrimary (citable) accession number: Q59RW5
    Secondary accession number(s): Q59RG5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 4, 2015
    Last sequence update: April 26, 2005
    Last modified: May 27, 2015
    This is version 64 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Candida albicans
      Candida albicans: entries and gene names
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.