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Database: UniProt/SWISS-PROT
Entry: HXKB_CANAL
LinkDB: HXKB_CANAL
Original site: 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   07-JUN-2017, entry version 50.
DE   RecName: Full=Hexokinase-2;
DE            EC=2.7.1.1;
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;
OC   Saccharomycetes; Saccharomycetales; Debaryomycetaceae;
OC   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.,
RA   Magee B.B., Newport G., Thorstenson Y.R., Agabian N., Magee P.T.,
RA   Davis R.W., 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
RT   aligned on the eight chromosomes.";
RL   Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME
RP   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
RT   allele-specific measurements and provides a simple model for repeat
RT   and indel 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
RT   for diagnosis of systemic candidiasis in patients with underlying
RT   hematological malignancies.";
RL   Proteomics 4:3084-3106(2004).
CC   -!- FUNCTION: Main glucose phosphorylating enzyme. May play a
CC       regulatory role in both induction and repression of gene
CC       expression by glucose (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY: ATP + D-hexose = ADP + D-hexose 6-phosphate.
CC   -!- PATHWAY: Carbohydrate metabolism; hexose metabolism.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
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
CC       malignant hematological disorders.
CC   -!- SIMILARITY: Belongs to the hexokinase family.
CC       {ECO:0000255|PROSITE-ProRule:PRU01084, ECO:0000305}.
DR   EMBL; CP017630; AOW31187.1; -; Genomic_DNA.
DR   RefSeq; XP_717405.1; XM_712312.1.
DR   ProteinModelPortal; P83776; -.
DR   SMR; P83776; -.
DR   COMPLUYEAST-2DPAGE; P83776; -.
DR   PRIDE; P83776; -.
DR   GeneID; 3641015; -.
DR   KEGG; cal:CAALFM_CR04510WA; -.
DR   CGD; CAL0000189097; HXK2.
DR   InParanoid; P83776; -.
DR   KO; K00844; -.
DR   OrthoDB; EOG092C2JW4; -.
DR   UniPathway; UPA00242; -.
DR   PRO; PR:P83776; -.
DR   Proteomes; UP000000559; Chromosome R.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005536; F:glucose binding; IEA:InterPro.
DR   GO; GO:0004396; F:hexokinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0001678; P:cellular glucose homeostasis; IEA:InterPro.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR   GO; GO:0019318; P:hexose metabolic process; IEA:UniProtKB-UniPathway.
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   PROSITE; PS51748; HEXOKINASE_2; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Complete proteome; Cytoplasm; Direct protein sequencing;
KW   Glycolysis; Kinase; Nucleotide-binding; Reference proteome;
KW   Transferase.
FT   CHAIN         1    484       Hexokinase-2.
FT                                /FTId=PRO_0000089303.
FT   DOMAIN       21    467       Hexokinase. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01084}.
FT   REGION       75    208       Hexokinase small subdomain.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01084}.
FT   REGION      209    456       Hexokinase large subdomain.
FT                                {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
//
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