HXKB_CANAL
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 03-AUG-2022, entry version 72.
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 COMPLUYEAST-2DPAGE; P83776; -.
DR PRIDE; P83776; -.
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; 1153545at2759; -.
DR UniPathway; UPA00109; UER00180.
DR UniPathway; UPA00242; -.
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:0001678; P:cellular glucose homeostasis; 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:0006013; P:mannose metabolic process; IBA:GO_Central.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR001312; Hexokinase.
DR InterPro; IPR022673; Hexokinase_C.
DR InterPro; IPR022672; Hexokinase_N.
DR PANTHER; PTHR19443; PTHR19443; 1.
DR Pfam; PF00349; Hexokinase_1; 1.
DR Pfam; PF03727; Hexokinase_2; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
DR PROSITE; PS51748; HEXOKINASE_2; 1.
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
