ID   HXKB_CANAL              Reviewed;         484 AA.
AC   P83776; A0A1D8PSR8; Q5A6L2; Q5A6V6;
DT   04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-OCT-2011, sequence version 2.
DT   24-JAN-2024, entry version 77.
DE   RecName: Full=Hexokinase-2;
DE            EC=2.7.1.1 {ECO:0000250|UniProtKB:P33284};
DE   AltName: Full=Cytoplasmic antigenic protein 3;
DE   AltName: Full=Hexokinase PII;
DE   AltName: Full=Hexokinase-B;
GN   Name=HXK2; OrderedLocusNames=CAALFM_CR04510WA;
GN   ORFNames=CaO19.542, CaO19.8176;
OS   Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=237561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA   Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA   Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA   Scherer S.;
RT   "The diploid genome sequence of Candida albicans.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA   van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA   Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA   Chibana H., Nantel A., Magee P.T.;
RT   "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT   on the eight chromosomes.";
RL   Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA   Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT   "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT   specific measurements and provides a simple model for repeat and indel
RT   structure.";
RL   Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
RN   [4]
RP   PROTEIN SEQUENCE OF 176-185 AND 317-325, SUBCELLULAR LOCATION, AND
RP   ANTIGENICITY.
RC   STRAIN=SC5314 / ATCC MYA-2876; TISSUE=Protoplast;
RX   PubMed=15378761; DOI=10.1002/pmic.200400903;
RA   Pitarch A., Abian J., Carrascal M., Sanchez M., Nombela C., Gil C.;
RT   "Proteomics-based identification of novel Candida albicans antigens for
RT   diagnosis of systemic candidiasis in patients with underlying hematological
RT   malignancies.";
RL   Proteomics 4:3084-3106(2004).
CC   -!- FUNCTION: Catalyzes the phosphorylation of hexose, such as D-glucose
CC       and D-fructose, to hexose 6-phosphate (D-glucose 6-phosphate and D-
CC       fructose 6-phosphate, respectively). Mediates the initial step of
CC       glycolysis by catalyzing phosphorylation of D-glucose to D-glucose 6-
CC       phosphate. {ECO:0000250|UniProtKB:P33284}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + D-hexose = ADP + D-hexose 6-phosphate + H(+);
CC         Xref=Rhea:RHEA:22740, ChEBI:CHEBI:4194, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61567, ChEBI:CHEBI:456216; EC=2.7.1.1;
CC         Evidence={ECO:0000250|UniProtKB:P33284};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22741;
CC         Evidence={ECO:0000250|UniProtKB:P33284};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + D-fructose = ADP + D-fructose 6-phosphate + H(+);
CC         Xref=Rhea:RHEA:16125, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:37721, ChEBI:CHEBI:61527, ChEBI:CHEBI:456216; EC=2.7.1.1;
CC         Evidence={ECO:0000250|UniProtKB:P33284};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16126;
CC         Evidence={ECO:0000250|UniProtKB:P33284};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + D-glucose = ADP + D-glucose 6-phosphate + H(+);
CC         Xref=Rhea:RHEA:17825, ChEBI:CHEBI:4167, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61548, ChEBI:CHEBI:456216; EC=2.7.1.1;
CC         Evidence={ECO:0000250|UniProtKB:P33284};
CC   -!- PATHWAY: Carbohydrate metabolism; hexose metabolism.
CC       {ECO:0000250|UniProtKB:P33284}.
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC       phosphate and glycerone phosphate from D-glucose: step 1/4.
CC       {ECO:0000250|UniProtKB:P33284}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P33284}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15378761}.
CC   -!- MISCELLANEOUS: Has antigenic properties. Elicits a specific immune
CC       response in systemic candidiasis human patients undergoing malignant
CC       hematological disorders.
CC   -!- SIMILARITY: Belongs to the hexokinase family. {ECO:0000255|PROSITE-
CC       ProRule:PRU01084, ECO:0000305}.
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DR   EMBL; CP017630; AOW31187.1; -; Genomic_DNA.
DR   RefSeq; XP_717405.1; XM_712312.1.
DR   AlphaFoldDB; P83776; -.
DR   SMR; P83776; -.
DR   BioGRID; 1224030; 1.
DR   STRING; 237561.P83776; -.
DR   EnsemblFungi; CR_04510W_A-T; CR_04510W_A-T-p1; CR_04510W_A.
DR   GeneID; 3641015; -.
DR   KEGG; cal:CAALFM_CR04510WA; -.
DR   CGD; CAL0000189097; HXK2.
DR   VEuPathDB; FungiDB:CR_04510W_A; -.
DR   eggNOG; KOG1369; Eukaryota.
DR   HOGENOM; CLU_014393_5_2_1; -.
DR   InParanoid; P83776; -.
DR   OrthoDB; 5481886at2759; -.
DR   UniPathway; UPA00109; UER00180.
DR   UniPathway; UPA00242; -.
DR   PHI-base; PHI:10643; -.
DR   PHI-base; PHI:8970; -.
DR   PRO; PR:P83776; -.
DR   Proteomes; UP000000559; Chromosome R.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008865; F:fructokinase activity; IBA:GO_Central.
DR   GO; GO:0004340; F:glucokinase activity; IBA:GO_Central.
DR   GO; GO:0005536; F:glucose binding; IEA:InterPro.
DR   GO; GO:0004396; F:hexokinase activity; IDA:CGD.
DR   GO; GO:0019158; F:mannokinase activity; IBA:GO_Central.
DR   GO; GO:0046835; P:carbohydrate phosphorylation; IBA:GO_Central.
DR   GO; GO:0051156; P:glucose 6-phosphate metabolic process; IMP:CGD.
DR   GO; GO:0006006; P:glucose metabolic process; IBA:GO_Central.
DR   GO; GO:0006096; P:glycolytic process; IBA:GO_Central.
DR   GO; GO:0001678; P:intracellular glucose homeostasis; IBA:GO_Central.
DR   GO; GO:0006013; P:mannose metabolic process; IBA:GO_Central.
DR   CDD; cd00012; NBD_sugar-kinase_HSP70_actin; 1.
DR   Gene3D; 1.10.287.1250; -; 1.
DR   Gene3D; 3.30.420.40; -; 1.
DR   Gene3D; 3.40.367.20; -; 1.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR001312; Hexokinase.
DR   InterPro; IPR022673; Hexokinase_C.
DR   InterPro; IPR022672; Hexokinase_N.
DR   PANTHER; PTHR19443; HEXOKINASE; 1.
DR   PANTHER; PTHR19443:SF16; HEXOKINASE TYPE 1-RELATED; 1.
DR   Pfam; PF00349; Hexokinase_1; 1.
DR   Pfam; PF03727; Hexokinase_2; 1.
DR   PRINTS; PR00475; HEXOKINASE.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR   PROSITE; PS51748; HEXOKINASE_2; 1.
DR   COMPLUYEAST-2DPAGE; P83776; -.
PE   1: Evidence at protein level;
KW   ATP-binding; Cytoplasm; Direct protein sequencing; Glycolysis; Kinase;
KW   Nucleotide-binding; Reference proteome; Transferase.
FT   CHAIN           1..484
FT                   /note="Hexokinase-2"
FT                   /id="PRO_0000089303"
FT   DOMAIN          21..467
FT                   /note="Hexokinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01084"
FT   REGION          75..208
FT                   /note="Hexokinase small subdomain"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01084"
FT   REGION          209..456
FT                   /note="Hexokinase large subdomain"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01084"
SQ   SEQUENCE   484 AA;  53416 MW;  7248469B1536C23A CRC64;
     MVHLGPKPAQ KRKGTFTDVS PQLLEALKPI QEQFTISADK LRAIVKHFIS ELDRGLSKAG
     GNIPMIPGWV MDFPTGKETG SYLAIDLGGT NLRVVLVKLG GNRDFDTTQS KFALPAHMRT
     ATSDELWDFI AKCLKEFVDE IYPDGCSEPL PLGFTFSYPA SQNRINEGIL QRWTKGWSID
     GIEGKDVVPM LQKAIKKVGV PIDVVALIND TTGTLVASMY TDPEAKMGLI FGTGVNGAYF
     DVVKDIPKLE GKCPSDIPPE SPMAINCEYG SFDNEKYILP RTKYDVQIDE ESPRPGQQTF
     EKMISGYYLG EVLRLILLEF AEEKKLIFKG QNLDKLKVPY VMDASYPSKI EEDPFENLSD
     VADLFREKLG IETTEPERKI IRCLAELIGE RSARFSVCGI AAICQKRGYK TAHCAADGSV
     YNKYPGFKER TAQALRDIYE WPADVKDPII IVPAEDGSGV GAAVIAALTE KRLKEGKSVG
     LLGA
//