HXK_SCHMA
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 03-AUG-2022, entry version 124.
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}.
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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.Smp_043030.1; -.
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 OMA; IAINCEW; -.
DR OrthoDB; 1153545at2759; -.
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.
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:0001678; P:cellular glucose homeostasis; IEA:InterPro.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0019318; P:hexose metabolic process; IEA:UniProtKB-UniPathway.
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; PTHR19443; 1.
DR Pfam; PF00349; Hexokinase_1; 1.
DR Pfam; PF03727; Hexokinase_2; 1.
DR SUPFAM; SSF53067; SSF53067; 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
