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N-acetylglucosamine kinase 1 (GlcNAc kinase 1) (EC 2.7.1.59) (Hexokinase 1)

 HXK1_CANAL              Reviewed;         493 AA.
Q59RW5; A0A1D8PQG2; Q59RG5;
04-FEB-2015, integrated into UniProtKB/Swiss-Prot.
15-MAR-2017, sequence version 2.
07-NOV-2018, entry version 80.
RecName: Full=N-acetylglucosamine kinase 1 {ECO:0000303|PubMed:11114181};
Short=GlcNAc kinase 1 {ECO:0000305};
EC=2.7.1.59 {ECO:0000269|PubMed:11298769};
AltName: Full=Hexokinase 1 {ECO:0000305};
Name=HXK1 {ECO:0000303|PubMed:11114181};
Synonyms=NAG5 {ECO:0000303|PubMed:11298769};
OrderedLocusNames=CAALFM_C604580WA; ORFNames=CaO19.2154, CaO19.9701;
Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Debaryomycetaceae;
Candida/Lodderomyces clade; Candida.
NCBI_TaxID=237561;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=SC5314 / ATCC MYA-2876;
PubMed=15123810; DOI=10.1073/pnas.0401648101;
Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S.,
Magee B.B., Newport G., Thorstenson Y.R., Agabian N., Magee P.T.,
Davis R.W., Scherer S.;
"The diploid genome sequence of Candida albicans.";
Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
[2]
GENOME REANNOTATION.
STRAIN=SC5314 / ATCC MYA-2876;
PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
Chibana H., Nantel A., Magee P.T.;
"Assembly of the Candida albicans genome into sixteen supercontigs
aligned on the eight chromosomes.";
Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME
REANNOTATION.
STRAIN=SC5314 / ATCC MYA-2876;
PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
"Assembly of a phased diploid Candida albicans genome facilitates
allele-specific measurements and provides a simple model for repeat
and indel structure.";
Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
[4]
IDENTIFICATION, AND INDUCTION.
PubMed=11114181; DOI=10.1073/pnas.250452997;
Kumar M.J., Jamaluddin M.S., Natarajan K., Kaur D., Datta A.;
"The inducible N-acetylglucosamine catabolic pathway gene cluster in
Candida albicans: discrete N-acetylglucosamine-inducible factors
interact at the promoter of NAG1.";
Proc. Natl. Acad. Sci. U.S.A. 97:14218-14223(2000).
[5]
IDENTIFICATION, DISRUPTION PHENOTYPE, FUNCTION, CATALYTIC ACTIVITY,
AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=11298769; DOI=10.1046/j.1432-1327.2001.02135.x;
Yamada-Okabe T., Sakamori Y., Mio T., Yamada-Okabe H.;
"Identification and characterization of the genes for N-
acetylglucosamine kinase and N-acetylglucosamine-phosphate deacetylase
in the pathogenic fungus Candida albicans.";
Eur. J. Biochem. 268:2498-2505(2001).
[6]
DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=11705974; DOI=10.1128/IAI.69.12.7898-7903.2001;
Singh P., Ghosh S., Datta A.;
"Attenuation of virulence and changes in morphology in Candida
albicans by disruption of the N-acetylglucosamine catabolic pathway.";
Infect. Immun. 69:7898-7903(2001).
[7]
DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=17139615; DOI=10.1002/jobm.200610167;
Wendland J., Hellwig D., Walther A., Sickinger S., Shadkchan Y.,
Martin R., Bauer J., Osherov N., Tretiakov A., Saluz H.P.;
"Use of the porcine intestinal epithelium (PIE)-assay to analyze early
stages of colonization by the human fungal pathogen Candida
albicans.";
J. Basic Microbiol. 46:513-523(2006).
[8]
INDUCTION.
PubMed=16987174; DOI=10.1111/j.1365-2958.2006.05367.x;
Bennett R.J., Johnson A.D.;
"The role of nutrient regulation and the Gpa2 protein in the mating
pheromone response of C. albicans.";
Mol. Microbiol. 62:100-119(2006).
[9]
FUNCTION.
PubMed=19648376; DOI=10.1128/AEM.00053-09;
Wendland J., Schaub Y., Walther A.;
"N-acetylglucosamine utilization by Saccharomyces cerevisiae based on
expression of Candida albicans NAG genes.";
Appl. Environ. Microbiol. 75:5840-5845(2009).
[10]
INDUCTION.
PubMed=20675577; DOI=10.1128/EC.00178-10;
Gunasekera A., Alvarez F.J., Douglas L.M., Wang H.X., Rosebrock A.P.,
Konopka J.B.;
"Identification of GIG1, a GlcNAc-induced gene in Candida albicans
needed for normal sensitivity to the chitin synthase inhibitor
nikkomycin Z.";
Eukaryot. Cell 9:1476-1483(2010).
[11]
DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=21700702; DOI=10.1074/jbc.M111.249854;
Naseem S., Gunasekera A., Araya E., Konopka J.B.;
"N-acetylglucosamine (GlcNAc) induction of hyphal morphogenesis and
transcriptional responses in Candida albicans are not dependent on its
metabolism.";
J. Biol. Chem. 286:28671-28680(2011).
[12]
DISRUPTION PHENOTYPE, INDUCTION, INTERACTION WITH SIR2, FUNCTION, AND
SUBCELLULAR LOCATION.
PubMed=23341961; DOI=10.1371/journal.pone.0053638;
Rao K.H., Ghosh S., Natarajan K., Datta A.;
"N-acetylglucosamine kinase, HXK1 is involved in morphogenetic
transition and metabolic gene expression in Candida albicans.";
PLoS ONE 8:E53638-E53638(2013).
[13]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=24491547; DOI=10.1016/j.bbrc.2014.01.123;
Rao K.H., Ruhela D., Ghosh S., Abdin M.Z., Datta A.;
"N-acetylglucosamine kinase, HXK1 contributes to white-opaque
morphological transition in Candida albicans.";
Biochem. Biophys. Res. Commun. 445:138-144(2014).
-!- FUNCTION: 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. {ECO:0000269|PubMed:11298769,
ECO:0000269|PubMed:11705974, ECO:0000269|PubMed:17139615,
ECO:0000269|PubMed:19648376, ECO:0000269|PubMed:21700702,
ECO:0000269|PubMed:23341961, ECO:0000269|PubMed:24491547}.
-!- CATALYTIC ACTIVITY: ATP + N-acetyl-D-glucosamine = ADP + N-acetyl-
D-glucosamine 6-phosphate. {ECO:0000269|PubMed:11298769}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=375.5 uM for N-acetylglucosamine (GlcNAc)
{ECO:0000269|PubMed:11298769};
KM=482.5 uM for glucose {ECO:0000269|PubMed:11298769};
KM=426.0 uM for mannose {ECO:0000269|PubMed:11298769};
-!- SUBUNIT: Interacts with histone deacetylase SIR2 under
filamentation-inducing conditions. {ECO:0000269|PubMed:23341961}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23341961}.
Nucleus {ECO:0000269|PubMed:23341961}. Mitochondrion
{ECO:0000269|PubMed:23341961}. 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.
{ECO:0000269|PubMed:23341961}.
-!- INDUCTION: Expression is induced by N-acetylglucosamine (GlcNAc),
by the alpha pheromone, and in filamentation-inducing media.
{ECO:0000269|PubMed:11114181, ECO:0000269|PubMed:16987174,
ECO:0000269|PubMed:20675577, ECO:0000269|PubMed:23341961}.
-!- DISRUPTION PHENOTYPE: 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.
{ECO:0000269|PubMed:11298769, ECO:0000269|PubMed:11705974,
ECO:0000269|PubMed:17139615, ECO:0000269|PubMed:21700702,
ECO:0000269|PubMed:23341961, ECO:0000269|PubMed:24491547}.
-!- SIMILARITY: Belongs to the hexokinase family.
{ECO:0000255|PROSITE-ProRule:PRU01084, ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; CP017628; AOW30374.1; -; Genomic_DNA.
RefSeq; XP_712429.2; XM_707336.2.
EnsemblFungi; AOW30374; AOW30374; CAALFM_C604580WA.
GeneID; 3645964; -.
KEGG; cal:CAALFM_C604580WA; -.
CGD; CAL0000186127; HXK1.
KO; K00844; -.
OrthoDB; EOG092C2ODC; -.
BRENDA; 2.7.1.59; 1096.
PRO; PR:Q59RW5; -.
Proteomes; UP000000559; Chromosome 6.
GO; GO:0005829; C:cytosol; IDA:CGD.
GO; GO:0005739; C:mitochondrion; IDA:CGD.
GO; GO:0005634; C:nucleus; IDA:CGD.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0008865; F:fructokinase activity; IBA:GO_Central.
GO; GO:0004340; F:glucokinase activity; IBA:GO_Central.
GO; GO:0005536; F:glucose binding; IEA:InterPro.
GO; GO:0019158; F:mannokinase activity; IBA:GO_Central.
GO; GO:0045127; F:N-acetylglucosamine kinase activity; IDA:CGD.
GO; GO:0044406; P:adhesion of symbiont to host; IDA:CGD.
GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
GO; GO:0001678; P:cellular glucose homeostasis; IBA:GO_Central.
GO; GO:0044114; P:development of symbiont in host; IMP:CGD.
GO; GO:0030447; P:filamentous growth; IMP:CGD.
GO; GO:0044182; P:filamentous growth of a population of unicellular organisms; IMP:CGD.
GO; GO:0006043; P:glucosamine catabolic process; IMP:CGD.
GO; GO:0006096; P:glycolytic process; IBA:GO_Central.
GO; GO:0044117; P:growth of symbiont in host; IMP:CGD.
GO; GO:0006046; P:N-acetylglucosamine catabolic process; IMP:CGD.
GO; GO:0009405; P:pathogenesis; IMP:CGD.
GO; GO:1900239; P:regulation of phenotypic switching; IMP:CGD.
InterPro; IPR001312; Hexokinase.
InterPro; IPR022673; Hexokinase_C.
InterPro; IPR022672; Hexokinase_N.
PANTHER; PTHR19443; PTHR19443; 1.
Pfam; PF00349; Hexokinase_1; 1.
Pfam; PF03727; Hexokinase_2; 1.
PROSITE; PS51748; HEXOKINASE_2; 1.
1: Evidence at protein level;
ATP-binding; Cell wall biogenesis/degradation; Complete proteome;
Cytoplasm; Glycolysis; Kinase; Mitochondrion; Nucleotide-binding;
Nucleus; Reference proteome; Transferase; Virulence.
CHAIN 1 493 N-acetylglucosamine kinase 1.
/FTId=PRO_0000431722.
DOMAIN 27 490 Hexokinase. {ECO:0000255|PROSITE-
ProRule:PRU01084}.
REGION 79 221 Hexokinase small subdomain.
{ECO:0000255|PROSITE-ProRule:PRU01084}.
REGION 222 479 Hexokinase large subdomain.
{ECO:0000255|PROSITE-ProRule:PRU01084}.
SEQUENCE 493 AA; 54823 MW; F1C4A571B9552FC5 CRC64;
MTETSISGLR GPKSMYFMEI VDVSSQESSV LSSIVESFTS AVSASNLGVY SDEVLCDIKS
SLKENSPITM LPNYNVSPTG DEHGQYLVID LGGSTLRIAV VDISKPHPNL SRSERITIVV
EKSWIIGNDF KRIDGEFFKY IGSKINEILM GQNVIDVKSV INTGITWSFP LETTDYNRGK
IKHVSKGYTV GEDIYDKDLK MVLEDTLRQE YGLTLDVQSI LNDSLAVYSA GCFIDSKMKL
AMVLGTGINM CCSLKRSSDI HPSKMLADAT LFNCELSLFG QNLCKDFATK YDIIIDKRFA
GLSHHFKTFM EPDPITKTLF QPHELMTSGR YLPELTRLVV VDLIEAGEIF QNVDHQQMYQ
EYGGFSGELI CFVHENDDYD DIHDKLCKAY GWTTVGLSDI VCLKEVVSCI IKRAAFIVAN
AIIAFFKLLG SDELGGDVTI GYVGSVLNYF HKYRRLIVEY VNSAEEAKGI KVDLKLIENS
SIIGAAIGAA YHK


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