ID HXK_SCHMA Reviewed; 451 AA. AC Q26609; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 14-AUG-2001, sequence version 2. DT 24-JAN-2024, entry version 130. DE RecName: Full=Hexokinase; DE EC=2.7.1.1 {ECO:0000250|UniProtKB:A0A0K0JFP3}; OS Schistosoma mansoni (Blood fluke). OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda; OC Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma. OX NCBI_TaxID=6183; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=Puerto Rican; RX PubMed=7821409; DOI=10.1006/expr.1995.1005; RA Shoemaker C.B., Reynolds S., Wei G., Harn D.; RT "Schistosoma mansoni hexokinase: cDNA cloning and immunogenicity studies."; RL Exp. Parasitol. 80:36-45(1995). RN [2] RP SEQUENCE REVISION TO 33. RA Shoemaker C.B., Reynolds S., Wei G., Harn D.; RL Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases. RN [3] RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH GLUCOSE. RX PubMed=9665168; DOI=10.1038/811; RA Mulichak A.M., Wilson J.E., Padmanabhan K., Garavito R.M.; RT "The structure of mammalian hexokinase-1."; RL Nat. Struct. Biol. 5:555-560(1998). CC -!- FUNCTION: Catalyzes the phosphorylation of various hexoses to hexose 6- CC phosphate. {ECO:0000250|UniProtKB:A0A0K0JFP3}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + D-hexose = ADP + D-hexose 6-phosphate + H(+); CC Xref=Rhea:RHEA:22740, ChEBI:CHEBI:4194, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61567, ChEBI:CHEBI:456216; EC=2.7.1.1; CC Evidence={ECO:0000250|UniProtKB:A0A0K0JFP3, ECO:0000255|PROSITE- CC ProRule:PRU01084}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22741; CC Evidence={ECO:0000250|UniProtKB:A0A0K0JFP3}; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + D-mannose = ADP + D-mannose 6-phosphate + H(+); CC Xref=Rhea:RHEA:11028, ChEBI:CHEBI:4208, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58735, ChEBI:CHEBI:456216; EC=2.7.1.1; CC Evidence={ECO:0000250|UniProtKB:A0A0K0JFP3}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11029; CC Evidence={ECO:0000250|UniProtKB:A0A0K0JFP3}; 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:0000250|UniProtKB:A0A0K0JFP3}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16126; CC Evidence={ECO:0000250|UniProtKB:A0A0K0JFP3}; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + D-glucose = ADP + D-glucose 6-phosphate + H(+); CC Xref=Rhea:RHEA:17825, ChEBI:CHEBI:4167, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61548, ChEBI:CHEBI:456216; EC=2.7.1.1; CC Evidence={ECO:0000250|UniProtKB:A0A0K0JFP3}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17826; CC Evidence={ECO:0000250|UniProtKB:A0A0K0JFP3}; CC -!- PATHWAY: Carbohydrate metabolism; hexose metabolism. CC {ECO:0000250|UniProtKB:A0A0K0JFP3}. CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3- CC phosphate and glycerone phosphate from D-glucose: step 1/4. CC {ECO:0000250|UniProtKB:A0A0K0JFP3}. CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:9665168}. CC -!- SIMILARITY: Belongs to the hexokinase family. {ECO:0000255|PROSITE- CC ProRule:PRU01084, ECO:0000305}. 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; L04480; AAA29894.2; -; Genomic_DNA. DR RefSeq; XP_018651965.1; XM_018796867.1. DR PDB; 1BDG; X-ray; 2.60 A; A=1-451. DR PDBsum; 1BDG; -. DR AlphaFoldDB; Q26609; -. DR SMR; Q26609; -. DR STRING; 6183.Q26609; -. DR DrugBank; DB02379; Beta-D-Glucose. DR EnsemblMetazoa; Smp_043030.1; Smp_043030.1; Smp_043030. DR GeneID; 8347871; -. DR KEGG; smm:Smp_043030; -. DR WBParaSite; Smp_043030.1; Smp_043030.1; Smp_043030. DR CTD; 8347871; -. DR eggNOG; KOG1369; Eukaryota. DR HOGENOM; CLU_014393_5_3_1; -. DR InParanoid; Q26609; -. DR OMA; ADCVQQF; -. DR OrthoDB; 5481886at2759; -. DR PhylomeDB; Q26609; -. DR SABIO-RK; Q26609; -. DR UniPathway; UPA00109; UER00180. DR UniPathway; UPA00242; -. DR EvolutionaryTrace; Q26609; -. DR Proteomes; UP000008854; Unassembled WGS sequence. DR ExpressionAtlas; Q26609; baseline and differential. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008865; F:fructokinase activity; IEA:RHEA. DR GO; GO:0004340; F:glucokinase activity; IEA:RHEA. DR GO; GO:0005536; F:glucose binding; IEA:InterPro. DR GO; GO:0019158; F:mannokinase activity; IEA:RHEA. DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway. DR GO; GO:0019318; P:hexose metabolic 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 1: Evidence at protein level; KW 3D-structure; ATP-binding; Glycolysis; Kinase; Nucleotide-binding; KW Reference proteome; Transferase. FT CHAIN 1..451 FT /note="Hexokinase" FT /id="PRO_0000197599" FT DOMAIN 6..445 FT /note="Hexokinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01084" FT REGION 63..195 FT /note="Hexokinase small subdomain" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01084" FT REGION 196..434 FT /note="Hexokinase large subdomain" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01084" FT BINDING 74..79 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255" FT BINDING 144 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:9665168" FT BINDING 161..162 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:9665168" FT BINDING 196..197 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:9665168" FT BINDING 222..223 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:9665168" FT BINDING 249 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:9665168" FT BINDING 283 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:9665168" FT BINDING 288..289 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P19367" FT BINDING 325..329 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P19367" FT BINDING 401..405 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P19367" FT HELIX 5..16 FT /evidence="ECO:0007829|PDB:1BDG" FT HELIX 17..19 FT /evidence="ECO:0007829|PDB:1BDG" FT HELIX 23..41 FT /evidence="ECO:0007829|PDB:1BDG" FT HELIX 43..46 FT /evidence="ECO:0007829|PDB:1BDG" FT STRAND 68..87 FT /evidence="ECO:0007829|PDB:1BDG" FT STRAND 95..101 FT /evidence="ECO:0007829|PDB:1BDG" FT TURN 105..109 FT /evidence="ECO:0007829|PDB:1BDG" FT HELIX 112..129 FT /evidence="ECO:0007829|PDB:1BDG" FT STRAND 137..143 FT /evidence="ECO:0007829|PDB:1BDG" FT STRAND 147..150 FT /evidence="ECO:0007829|PDB:1BDG" FT TURN 151..153 FT /evidence="ECO:0007829|PDB:1BDG" FT STRAND 154..157 FT /evidence="ECO:0007829|PDB:1BDG" FT HELIX 174..183 FT /evidence="ECO:0007829|PDB:1BDG" FT TURN 184..186 FT /evidence="ECO:0007829|PDB:1BDG" FT STRAND 189..195 FT /evidence="ECO:0007829|PDB:1BDG" FT HELIX 197..206 FT /evidence="ECO:0007829|PDB:1BDG" FT STRAND 212..229 FT /evidence="ECO:0007829|PDB:1BDG" FT TURN 230..232 FT /evidence="ECO:0007829|PDB:1BDG" FT HELIX 234..236 FT /evidence="ECO:0007829|PDB:1BDG" FT STRAND 240..247 FT /evidence="ECO:0007829|PDB:1BDG" FT HELIX 250..252 FT /evidence="ECO:0007829|PDB:1BDG" FT TURN 253..256 FT /evidence="ECO:0007829|PDB:1BDG" FT TURN 258..262 FT /evidence="ECO:0007829|PDB:1BDG" FT HELIX 265..272 FT /evidence="ECO:0007829|PDB:1BDG" FT STRAND 274..276 FT /evidence="ECO:0007829|PDB:1BDG" FT HELIX 283..286 FT /evidence="ECO:0007829|PDB:1BDG" FT HELIX 288..304 FT /evidence="ECO:0007829|PDB:1BDG" FT HELIX 309..311 FT /evidence="ECO:0007829|PDB:1BDG" FT HELIX 316..318 FT /evidence="ECO:0007829|PDB:1BDG" FT HELIX 327..331 FT /evidence="ECO:0007829|PDB:1BDG" FT HELIX 340..348 FT /evidence="ECO:0007829|PDB:1BDG" FT HELIX 357..389 FT /evidence="ECO:0007829|PDB:1BDG" FT STRAND 392..400 FT /evidence="ECO:0007829|PDB:1BDG" FT HELIX 401..405 FT /evidence="ECO:0007829|PDB:1BDG" FT HELIX 409..420 FT /evidence="ECO:0007829|PDB:1BDG" FT STRAND 426..431 FT /evidence="ECO:0007829|PDB:1BDG" FT HELIX 435..444 FT /evidence="ECO:0007829|PDB:1BDG" SQ SEQUENCE 451 AA; 50446 MW; 4CB6038AED0FF391 CRC64; MVFSDQQLFE KVVEILKPFD LSVVDYEEIC DRMGESMRLG LQKSTNEKSS IKMFPSYVTK TPNGTETGNF LALDLGGTNY RVLSVTLEGK GKSPRIQERT YCIPAEKMSG SGTELFKYIA ETLADFLENN GMKDKKFDLG FTFSFPCVQK GLTHATLVRW TKGFSADGVE GHNVAELLQT ELDKRELNVK CVAVVNDTVG TLASCALEDP KCAVGLIVGT GTNVAYIEDS SKVELMDGVK EPEVVINTEW GAFGEKGELD CWRTQFDKSM DIDSLHPGKQ LYEKMVSGMY LGELVRHIIV YLVEQKILFR GDLPERLKVR NSLLTRYLTD VERDPAHLLY NTHYMLTDDL HVPVVEPIDN RIVRYACEMV VKRAAYLAGA GIACILRRIN RSEVTVGVDG SLYKFHPKFC ERMTDMVDKL KPKNTRFCLR LSEDGSGKGA AAIAASCTRQ N //