ID Q5KCL1_CRYNJ Unreviewed; 557 AA. AC Q5KCL1; DT 15-FEB-2005, integrated into UniProtKB/TrEMBL. DT 15-FEB-2005, sequence version 1. DT 24-JAN-2024, entry version 124. DE RecName: Full=Phosphotransferase {ECO:0000256|RuleBase:RU362007}; DE EC=2.7.1.- {ECO:0000256|RuleBase:RU362007}; GN OrderedLocusNames=CNH01400 {ECO:0000313|EMBL:AAW45021.1}; OS Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC OS MYA-565) (Filobasidiella neoformans). OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes; OC Tremellales; Cryptococcaceae; Cryptococcus; OC Cryptococcus neoformans species complex. OX NCBI_TaxID=214684 {ECO:0000313|EMBL:AAW45021.1, ECO:0000313|Proteomes:UP000002149}; RN [1] {ECO:0000313|EMBL:AAW45021.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=JEC21 {ECO:0000313|EMBL:AAW45021.1}; RA Loftus B., Amedeo P., Roncaglia P., Vamathevan J., Utterback T., RA Van Aken S., Fraser C.; RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:AAW45021.1, ECO:0000313|Proteomes:UP000002149} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JEC21 {ECO:0000313|EMBL:AAW45021.1}, and JEC21 / ATCC MYA-565 RC {ECO:0000313|Proteomes:UP000002149}; RX PubMed=15653466; DOI=10.1126/science.1103773; RA Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D., RA Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E., RA Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A., RA Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C., RA Janbon G., Jones S.J., Koo H.L., Krzywinski M.I., Kwon-Chung J.K., RA Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A., RA Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E., RA Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A., RA Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W., RA Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.; RT "The genome of the basidiomycetous yeast and human pathogen Cryptococcus RT neoformans."; RL Science 307:1321-1324(2005). RN [3] {ECO:0000313|EMBL:AAW45021.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=JEC21 {ECO:0000313|EMBL:AAW45021.1}; RA Janbon G., Paulet D., Chon C.C., Mornico D.; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. 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; AE017348; AAW45021.1; -; Genomic_DNA. DR EMBL; AE017348; ALO69532.1; -; Genomic_DNA. DR RefSeq; XP_572328.1; XM_572328.1. DR RefSeq; XP_572329.1; XM_572329.1. DR AlphaFoldDB; Q5KCL1; -. DR STRING; 214684.Q5KCL1; -. DR PaxDb; 214684-Q5KCL1; -. DR EnsemblFungi; AAW45021; AAW45021; CNH01400. DR EnsemblFungi; ALO69532; ALO69532; CNH01400. DR GeneID; 3259022; -. DR VEuPathDB; FungiDB:CNH01400; -. DR eggNOG; KOG1369; Eukaryota. DR HOGENOM; CLU_014393_5_2_1; -. DR OMA; ADCVQQF; -. DR OrthoDB; 5481886at2759; -. DR UniPathway; UPA00109; UER00180. DR Proteomes; UP000002149; Chromosome 8. 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-UniRule. 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:0019158; F:mannokinase activity; IBA:GO_Central. DR GO; GO:0046835; P:carbohydrate phosphorylation; IBA:GO_Central. DR GO; GO:0006000; P:fructose metabolic process; IEA:EnsemblFungi. DR GO; GO:0051156; P:glucose 6-phosphate metabolic process; IBA:GO_Central. 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; 3.30.420.40; -; 1. DR Gene3D; 3.40.367.20; -; 1. DR InterPro; IPR043129; ATPase_NBD. DR InterPro; IPR001312; Hexokinase. DR InterPro; IPR019807; Hexokinase_BS. 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; PS00378; HEXOKINASE_1; 1. 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|ARBA:ARBA00023152, 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:UP000002149}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU362007}. FT DOMAIN 106..300 FT /note="Hexokinase N-terminal" FT /evidence="ECO:0000259|Pfam:PF00349" FT DOMAIN 306..544 FT /note="Hexokinase C-terminal" FT /evidence="ECO:0000259|Pfam:PF03727" FT REGION 1..78 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..36 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 54..70 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 557 AA; 60724 MW; E888A8C802A84E0F CRC64; MSETPDQLAT RVQNLSTAPT TTQRTGSGSA VLENGTNIGS AAGRKASIPA QVDPERIIST SGSGRTSRRG SGLVMTPGGV QTVYHTRTNE DIEFPHAGKK TMADLLRKYE SLFTLTPQRM RMIVHAIEET LDNGLQKNGQ VVPMIPTYVF GWPTGNEVGD FLALDLGGTN LRVCLVTLLG SGKFEVTQTK YRLTEEQKQG EGQALLDFCA ECLNSFIRDT LGRTEKDGIL PLGFTFSYPC SQDRIDHGVL IRWTKGFGAP NIEGYDVAAM FKDSLKRMDV PAELTALIND TTGTLIASNY VDPHTKIAVI FGTGCNAAYM ETAGSIPKID YVGLPEEQGM AINCEWGAFD SFDHQHLPRT KYDIIIDESS NKPGEQSFEK MIAGLYLGEI FRLVLCELID SGDLFLGQNT YKLEKAYAFD TAFLSLMEAD VTEELLTIIG VFAHFFGLET TLEERQFFKK LAVLVGTRSA RLSACGIAAI VSKKGYLEEG CAVGADGSLY NKYPNFADRV HEALTDIFGE SGKKIVTHHA EDGSGVGSAI IAAMTKARKD SGFFVEY //