ID   C5M2X5_CANTT            Unreviewed;       483 AA.
AC   C5M2X5;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 61.
DE   RecName: Full=Phosphotransferase {ECO:0000256|RuleBase:RU362007};
DE            EC=2.7.1.- {ECO:0000256|RuleBase:RU362007};
GN   ORFNames=CTRG_00414 {ECO:0000313|EMBL:EER35675.1};
OS   Candida tropicalis (strain ATCC MYA-3404 / T1) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=294747 {ECO:0000313|EMBL:EER35675.1, ECO:0000313|Proteomes:UP000002037};
RN   [1] {ECO:0000313|EMBL:EER35675.1, ECO:0000313|Proteomes:UP000002037}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-3404 / T1 {ECO:0000313|Proteomes:UP000002037};
RX   PubMed=19465905; DOI=10.1038/nature08064;
RA   Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA   Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA   Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA   Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA   Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA   Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA   Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA   Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA   Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA   Cuomo C.A.;
RT   "Evolution of pathogenicity and sexual reproduction in eight Candida
RT   genomes.";
RL   Nature 459:657-662(2009).
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:0000256|ARBA:ARBA00001397};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16126;
CC         Evidence={ECO:0000256|ARBA:ARBA00001397};
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC       phosphate and glycerone phosphate from D-glucose: step 1/4.
CC       {ECO:0000256|ARBA:ARBA00004888}.
CC   -!- PATHWAY: Carbohydrate metabolism; hexose metabolism.
CC       {ECO:0000256|ARBA:ARBA00005028}.
CC   -!- SIMILARITY: Belongs to the hexokinase family.
CC       {ECO:0000256|ARBA:ARBA00009225, ECO:0000256|RuleBase:RU362007}.
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DR   EMBL; GG692395; EER35675.1; -; Genomic_DNA.
DR   RefSeq; XP_002545633.1; XM_002545587.1.
DR   AlphaFoldDB; C5M2X5; -.
DR   STRING; 294747.C5M2X5; -.
DR   EnsemblFungi; CTRG_00414-t43_1; CTRG_00414-t43_1-p1; CTRG_00414.
DR   GeneID; 8296095; -.
DR   KEGG; ctp:CTRG_00414; -.
DR   VEuPathDB; FungiDB:CTRG_00414; -.
DR   eggNOG; KOG1369; Eukaryota.
DR   HOGENOM; CLU_014393_5_2_1; -.
DR   OrthoDB; 5481886at2759; -.
DR   UniPathway; UPA00109; UER00180.
DR   Proteomes; UP000002037; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008865; F:fructokinase activity; IEA:RHEA.
DR   GO; GO:0005536; F:glucose binding; IEA:InterPro.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0001678; P:intracellular glucose homeostasis; IEA:InterPro.
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.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU362007};
KW   Glycolysis {ECO:0000256|RuleBase:RU362007};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU362007};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU362007};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002037};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU362007}.
FT   DOMAIN          27..220
FT                   /note="Hexokinase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00349"
FT   DOMAIN          226..468
FT                   /note="Hexokinase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03727"
SQ   SEQUENCE   483 AA;  53206 MW;  1E4BCEDDA30C0130 CRC64;
     MVHLGPKPAQ PRKGTFTDVP SQLLEAIKPF EKEFTISGET LRAIVAHFIK ELNRGLSKQG
     GNIPMIPGWV MEYPTGKETG NYLAIDLGGT NLRVVLVKLG GNRDFDTTQS KFALPSHMRT
     ATKDELWDFI AKCLKQVVDE VFPEGVTQPI PLGFTFSYPA SQDRINEGVL QRWTKGWAID
     GIEGHDVVPM LQSAVKKVGV PINVVALIND TTGTLVASLY TDPETKMGVI FGTGVNGAYY
     DVVGEIPKLE GRCGADIPPT SLMAINCEYG SFDNEHFILP RTKYDIQIDA ESPKPGQQTF
     EKMNSGYYLG ELLRLILLEL ADEKKLIFKG QNIDKLRKPY VMDTSFPSRI ELDPFENLSD
     VADIFQDELG IQTTEPERKI IRRLSELIGE RSARLSVCGI AAICQKRGYE TAHIAADGSV
     FNRYPGFKER AAKALRDIYQ WPATQKDPIV IVAAEDGSGV GAAIIAALTE KRLKEGKSVG
     VIA
//