ID   Q27647_ENTHI            Unreviewed;       445 AA.
AC   Q27647; A0A175JIJ4; C4LXB2;
DT   01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT   01-NOV-1996, sequence version 1.
DT   24-JAN-2024, entry version 117.
DE   RecName: Full=Phosphotransferase {ECO:0000256|RuleBase:RU362007};
DE            EC=2.7.1.- {ECO:0000256|RuleBase:RU362007};
GN   Name=HXK1 {ECO:0000313|EMBL:CAA57681.1};
OS   Entamoeba histolytica.
OC   Eukaryota; Amoebozoa; Evosea; Archamoebae; Mastigamoebida; Entamoebidae;
OC   Entamoeba.
OX   NCBI_TaxID=5759 {ECO:0000313|EMBL:CAA57681.1};
RN   [1] {ECO:0000313|EMBL:CAA57681.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=SFL-3 {ECO:0000313|EMBL:CAA57681.1};
RX   PubMed=8577326; DOI=10.1016/0166-6851(95)00115-H;
RA   Ortner S., Plaimauer B., Binder M., Scheiner O., Wiedermann G., Duchene M.;
RT   "Molecular analysis of two hexokinase isoenzymes, pathogencity markers for
RT   the human parasite Entamoeba histolytica.";
RL   Mol. Biochem. Parasitol. 73:189-198(1995).
RN   [2] {ECO:0000313|EMBL:BAN37591.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=HM-1:IMSS {ECO:0000313|EMBL:BAN37591.1};
RA   Hiranuka K., Kumagai M., Wakaguri H., Suzuki Y., Sugano S., Watanabe J.,
RA   Makioka A.;
RT   "Short 5' UTR of Entamoeba genes.";
RL   Submitted (JUN-2012) 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; AK418850; BAN37591.1; -; mRNA.
DR   EMBL; X82197; CAA57681.1; -; mRNA.
DR   AlphaFoldDB; Q27647; -.
DR   SMR; Q27647; -.
DR   STRING; 5759.Q27647; -.
DR   EnsemblProtists; GAT93385; GAT93385; CL6EHI_098290.
DR   EnsemblProtists; rna_EHI_098290-1; rna_EHI_098290-1; EHI_098290.
DR   VEuPathDB; AmoebaDB:EHI5A_039090; -.
DR   VEuPathDB; AmoebaDB:EHI5A_083040; -.
DR   VEuPathDB; AmoebaDB:EHI7A_052510; -.
DR   VEuPathDB; AmoebaDB:EHI_098290; -.
DR   VEuPathDB; AmoebaDB:KM1_095060; -.
DR   HOGENOM; CLU_014393_5_3_1; -.
DR   InParanoid; Q27647; -.
DR   OMA; YPNFEGY; -.
DR   OrthoDB; 23424at2759; -.
DR   SABIO-RK; Q27647; -.
DR   UniPathway; UPA00109; UER00180.
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: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; 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   2: Evidence at transcript level;
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          2..191
FT                   /note="Hexokinase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00349"
FT   DOMAIN          198..439
FT                   /note="Hexokinase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03727"
SQ   SEQUENCE   445 AA;  49830 MW;  C5B888693A00826D CRC64;
     MQEIIDQFAI DKEKMEIIVS KLLEEMENGL QDKPSTLQML PTYAPIPTGK EVGTFMGIDV
     GGTNLRVLLL EIPEPGVRGE LKSVECIMPK TSTTVDQFFG FIAQKIKEFV ENNNLKEKEI
     KAGLTFSFAV EQIAIDKGIQ QSWSKGWDVK ESIGKDIVEI FHNQLAKINV NNIRIVAFIN
     DTVGTFANLA YDDASCGMGL IFGTGTNGCY IEKTSNFAAS KLKSVYKEDY MIVNTEWGGL
     QFPELGLNRF DDMINDVSVN KDQQRYEKMI SGIYMGWLAR LAIRELIEKK VIFERYADAE
     VFSNSPDDTQ FNDKKKYSSR HTEIVEDTSP ELSRVDTILK SLGVNDSTLE ERKILKAITE
     AVVKRAAYLS AAATVALYRK MVPYMKERTT AGIDGTVYEK SVPFKRFYLE AIRLLQPKEN
     FTCQLSKDGS GLGAVIVAAA VACKH
//