ID Q4VT70_LEIMA Unreviewed; 471 AA. AC Q4VT70; Q4QCJ1; DT 05-JUL-2005, integrated into UniProtKB/TrEMBL. DT 05-JUL-2005, sequence version 1. DT 24-JAN-2024, entry version 120. DE RecName: Full=Phosphotransferase {ECO:0000256|RuleBase:RU362007}; DE EC=2.7.1.- {ECO:0000256|RuleBase:RU362007}; GN Name=HK {ECO:0000313|EMBL:AAV32454.1}; GN ORFNames=LMJF_21_0240 {ECO:0000313|EMBL:CAJ03833.1}; OS Leishmania major. OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina; OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania. OX NCBI_TaxID=5664 {ECO:0000313|EMBL:AAV32454.1}; RN [1] {ECO:0000313|EMBL:AAV32454.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=16539044; DOI=10.1645/GE-502R1.1; RA Umasankar P.K., Jayakumar P.C., Shouche Y.S., Patole M.S.; RT "Molecular characterization of the hexokinase gene from Leishmania major."; RL J. Parasitol. 91:1504-1509(2005). RN [2] {ECO:0000313|EMBL:CAJ03833.1, ECO:0000313|Proteomes:UP000000542} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Friedlin {ECO:0000313|EMBL:CAJ03833.1}, and MHOM/IL/81/Friedlin RC {ECO:0000313|Proteomes:UP000000542}; RX PubMed=16020728; DOI=10.1126/science.1112680; RA Ivens A.C., Peacock C.S., Worthey E.A., Murphy L., Aggarwal G., RA Berriman M., Sisk E., Rajandream M.A., Adlem E., Aert R., Anupama A., RA Apostolou Z., Attipoe P., Bason N., Bauser C., Beck A., Beverley S.M., RA Bianchettin G., Borzym K., Bothe G., Bruschi C.V., Collins M., Cadag E., RA Ciarloni L., Clayton C., Coulson R.M., Cronin A., Cruz A.K., Davies R.M., RA De Gaudenzi J., Dobson D.E., Duesterhoeft A., Fazelina G., Fosker N., RA Frasch A.C., Fraser A., Fuchs M., Gabel C., Goble A., Goffeau A., RA Harris D., Hertz-Fowler C., Hilbert H., Horn D., Huang Y., Klages S., RA Knights A., Kube M., Larke N., Litvin L., Lord A., Louie T., Marra M., RA Masuy D., Matthews K., Michaeli S., Mottram J.C., Muller-Auer S., RA Munden H., Nelson S., Norbertczak H., Oliver K., O'neil S., Pentony M., RA Pohl T.M., Price C., Purnelle B., Quail M.A., Rabbinowitsch E., RA Reinhardt R., Rieger M., Rinta J., Robben J., Robertson L., Ruiz J.C., RA Rutter S., Saunders D., Schafer M., Schein J., Schwartz D.C., Seeger K., RA Seyler A., Sharp S., Shin H., Sivam D., Squares R., Squares S., Tosato V., RA Vogt C., Volckaert G., Wambutt R., Warren T., Wedler H., Woodward J., RA Zhou S., Zimmermann W., Smith D.F., Blackwell J.M., Stuart K.D., RA Barrell B., Myler P.J.; RT "The genome of the kinetoplastid parasite, Leishmania major."; RL Science 309:436-442(2005). RN [3] {ECO:0000313|EMBL:CAJ03833.1, ECO:0000313|Proteomes:UP000000542} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Friedlin {ECO:0000313|EMBL:CAJ03833.1}, and MHOM/IL/81/Friedlin RC {ECO:0000313|Proteomes:UP000000542}; RX PubMed=22038252; DOI=10.1101/gr.122945.111; RA Rogers M.B., Hilley J.D., Dickens N.J., Wilkes J., Bates P.A., RA Depledge D.P., Harris D., Her Y., Herzyk P., Imamura H., Otto T.D., RA Sanders M., Seeger K., Dujardin J.C., Berriman M., Smith D.F., RA Hertz-Fowler C., Mottram J.C.; RT "Chromosome and gene copy number variation allow major structural change RT between species and strains of Leishmania."; RL Genome Res. 21:2129-2142(2011). RN [4] {ECO:0000313|EMBL:CAJ03833.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Friedlin {ECO:0000313|EMBL:CAJ03833.1}; RA Aslett M.; RL Submitted (JAN-2011) 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; AY632239; AAV32454.1; -; Genomic_DNA. DR EMBL; FR796417; CAJ03833.1; -; Genomic_DNA. DR RefSeq; XP_001682957.1; XM_001682905.1. DR AlphaFoldDB; Q4VT70; -. DR STRING; 5664.Q4VT70; -. DR EnsemblProtists; CAJ03833; CAJ03833; LMJF_21_0240. DR GeneID; 5651558; -. DR KEGG; lma:LMJF_21_0240; -. DR VEuPathDB; TriTrypDB:LmjF.21.0240; -. DR VEuPathDB; TriTrypDB:LMJFC_210008400; -. DR VEuPathDB; TriTrypDB:LMJLV39_210007700; -. DR VEuPathDB; TriTrypDB:LMJSD75_210007800; -. DR VEuPathDB; TriTrypDB:LMJSD75_210007900; -. DR eggNOG; KOG1369; Eukaryota. DR HOGENOM; CLU_014393_5_2_1; -. DR InParanoid; Q4VT70; -. DR OMA; ADCVQQF; -. DR UniPathway; UPA00109; UER00180. DR Proteomes; UP000000542; Chromosome 21. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0020015; C:glycosome; ISO:GeneDB. 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:0046835; P:carbohydrate phosphorylation; IBA:GO_Central. 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 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:UP000000542}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU362007}. FT DOMAIN 31..222 FT /note="Hexokinase N-terminal" FT /evidence="ECO:0000259|Pfam:PF00349" FT DOMAIN 231..465 FT /note="Hexokinase C-terminal" FT /evidence="ECO:0000259|Pfam:PF03727" SQ SEQUENCE 471 AA; 51720 MW; 5938CBED6934FC51 CRC64; MAARVNNLLS HIAIRDSDSE EMRYIKQRLA LASLATQFTM SSEKMKQLTM YMIHEMVEGL EGRPSTVRML PSFVYTSDPA KATGVYYALD LGGTNFRVLR VSLRGGKVDD RTDSKFVIPK SALVGDATDL FDFIAQSVKK MMSENAPDDL EKRVPLGFTF SFPVDQKAVN KGLLIKWTKG FSTKNVEGND VVELLQASLR RVRVNVNVVA LCNDTVGTLV ARYFVDTDVQ VGVIIGTGSN ACYFERASAV TKDPAVSARG NAVTPINMEC GNFDSKYKYA LPITVYDDEM DAITPNRENQ RQEKLVSGMY LGEISRRLIV HLAQLGCLPR GLVDGLCRPW AFESKHMGMI AADQMPGLQF TRELIKRIAG VDMADISDLH TIRETCCLVR NRAAQQGAVF TAAPMLKTRT QGLATVAVDG SVYEKTPSFQ RLYQECITSI LGSTSNVKVV LQRDGSGVGA AMICALAANT K //