ID   E9AUZ2_LEIMU            Unreviewed;       471 AA.
AC   E9AUZ2;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   27-MAR-2024, entry version 62.
DE   RecName: Full=Phosphotransferase {ECO:0000256|RuleBase:RU362007};
DE            EC=2.7.1.- {ECO:0000256|RuleBase:RU362007};
GN   ORFNames=LMXM_21_0250 {ECO:0000313|EMBL:CBZ26773.1};
OS   Leishmania mexicana (strain MHOM/GT/2001/U1103).
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX   NCBI_TaxID=929439 {ECO:0000313|EMBL:CBZ26773.1, ECO:0000313|Proteomes:UP000007259};
RN   [1] {ECO:0000313|EMBL:CBZ26773.1, ECO:0000313|Proteomes:UP000007259}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MHOM/GT/2001/U1103 {ECO:0000313|EMBL:CBZ26773.1,
RC   ECO:0000313|Proteomes:UP000007259};
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).
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; FR799574; CBZ26773.1; -; Genomic_DNA.
DR   RefSeq; XP_003875265.1; XM_003875216.1.
DR   AlphaFoldDB; E9AUZ2; -.
DR   SMR; E9AUZ2; -.
DR   GeneID; 13454093; -.
DR   KEGG; lmi:LMXM_21_0250; -.
DR   VEuPathDB; TriTrypDB:LmxM.21.0250; -.
DR   OMA; ADCVQQF; -.
DR   OrthoDB; 5481886at2759; -.
DR   PhylomeDB; E9AUZ2; -.
DR   UniPathway; UPA00109; UER00180.
DR   Proteomes; UP000007259; Chromosome 21.
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; 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   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;  51671 MW;  FD9E4B7B2AEC54CB CRC64;
     MATRVNNLLS HIAIRDSDSE EMRYIKQRLA LASLATQFTM SPEKMKQLTM YMIHEMVEGL
     EGRPSTVRML PSFVYTSDPA KATGVYYALD LGGTNFRVLR VSLRGGKVDD RTDSKFVIPK
     SALVGDATDL FDFIAQSVKK MMSENAPEDL EKRVPLGFTF SFPVDQKAVN KGLLIKWTKG
     FSTKNVEGSD VVELLQASLR RVRVNVNVVA LCNDTVGTLV ARYFVDTDVQ VGVIIGTGSN
     ACYFERASAV TKDPAVSARG NAVTPINMEC GNFDSKYKYA LPITVYDDEM DAITPNRENQ
     RQEKLVSGMY LGEISRRLIV HLAHLGCLPR GLVDGLCKPW AFESKHMGMV AADQMPGLQF
     TRELIKRVAG VDVTDTSDLH TIREACCLVR NRAAQQGSVF TAAPMLKTRT QGLATVAVDG
     SVYEKTPSFQ RLYQECITSI LGSTSNAKVV LQKDGSGVGA AMICALAVNK K
//