ID B9WLQ0_CANDC Unreviewed; 484 AA. AC B9WLQ0; DT 24-MAR-2009, integrated into UniProtKB/TrEMBL. DT 24-MAR-2009, sequence version 1. DT 27-MAR-2024, entry version 73. DE RecName: Full=Phosphotransferase {ECO:0000256|RuleBase:RU362007}; DE EC=2.7.1.- {ECO:0000256|RuleBase:RU362007}; GN OrderedLocusNames=Cd36_29870 {ECO:0000313|CGD:CAL0000166854}; GN ORFNames=CD36_29870 {ECO:0000313|EMBL:CAX40012.1}; OS Candida dubliniensis (strain CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 / OS NRRL Y-17841) (Yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida. OX NCBI_TaxID=573826 {ECO:0000313|EMBL:CAX40012.1, ECO:0000313|Proteomes:UP000002605}; RN [1] {ECO:0000313|EMBL:CAX40012.1, ECO:0000313|Proteomes:UP000002605} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 / NRRL Y-17841 RC {ECO:0000313|Proteomes:UP000002605}; RX PubMed=19745113; DOI=10.1101/gr.097501.109; RA Jackson A.P., Gamble J.A., Yeomans T., Moran G.P., Saunders D., Harris D., RA Aslett M., Barrell J.F., Butler G., Citiulo F., Coleman D.C., RA de Groot P.W.J., Goodwin T.J., Quail M.A., McQuillan J., Munro C.A., RA Pain A., Poulter R.T., Rajandream M.A., Renauld H., Spiering M.J., RA Tivey A., Gow N.A.R., Barrell B., Sullivan D.J., Berriman M.; RT "Comparative genomics of the fungal pathogens Candida dubliniensis and RT Candida albicans."; RL Genome Res. 19:2231-2244(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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; FM992695; CAX40012.1; -; Genomic_DNA. DR RefSeq; XP_002422011.1; XM_002421966.1. DR AlphaFoldDB; B9WLQ0; -. DR GeneID; 8050127; -. DR KEGG; cdu:CD36_29870; -. DR CGD; CAL0000166854; Cd36_29870. DR VEuPathDB; FungiDB:CD36_29870; -. DR eggNOG; KOG1369; Eukaryota. DR HOGENOM; CLU_014393_5_2_1; -. DR OrthoDB; 5481886at2759; -. DR UniPathway; UPA00109; UER00180. DR Proteomes; UP000002605; Chromosome R. 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 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 484 AA; 53566 MW; F39482D7A0EDD0D8 CRC64; MVHLGPKPAQ KRKGTFTDVS PQLLDALKPI QEQFTISADT LRAIVKHFIS ELDRGLSKAG GNIPMIPGWV MDFPTGKETG SYIAIDLGGT NLRVVLVKLG GNRDFDTTQS KFALPPHMRT ATSDELWDFI AKCLKDFVDE IYPDGCTEPL PLGFTFSYPA SQSRINEGIL QRWTKGWAID GIEGKDVVPM LQKAIKKVGV PINVVALIND TTGTLVASMY TDPEAKMGLI FGTGVNGAYF DVVKDIPKLE GKCPADIPPE SPMAINCEYG SFDNEKYILP RTKYDVQIDE ESPRPGQQTF EKMISGYYLG EVLRLILLEF AEEKKLIFKG QNIDKLKIPY VMDASYPSRI EEDPFENLSD VADLFREKLG IETTEPERKI IRRLAELIGE RSARFSVCGI AAICQKRGYE TAHCAADGSV YNKYPGFKER TAQALRDIYE WPADIKDPII IVPAEDGSGV GAAIIAALTE KRLREGKSVG LLEA //