HXK_TOXGO
ID HXK_TOXGO Reviewed; 468 AA.
AC Q969A8;
DT 03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Hexokinase;
DE EC=2.7.1.1 {ECO:0000250|UniProtKB:A0A0K0JFP3};
GN Name=HXK;
OS Toxoplasma gondii.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Sarcocystidae; Toxoplasma.
OX NCBI_TaxID=5811;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Saito T.;
RT "Hexokinase.";
RL Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
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 -!- SIMILARITY: Belongs to the hexokinase family. {ECO:0000255|PROSITE-
CC ProRule:PRU01084, ECO:0000305}.
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DR EMBL; AB049736; BAB55664.1; -; mRNA.
DR AlphaFoldDB; Q969A8; -.
DR SMR; Q969A8; -.
DR ChEMBL; CHEMBL4739860; -.
DR VEuPathDB; ToxoDB:TGARI_265450; -.
DR VEuPathDB; ToxoDB:TGCAST_265450; -.
DR VEuPathDB; ToxoDB:TGCOUG_265450; -.
DR VEuPathDB; ToxoDB:TGDOM2_265450; -.
DR VEuPathDB; ToxoDB:TGFOU_265450; -.
DR VEuPathDB; ToxoDB:TGGT1_265450; -.
DR VEuPathDB; ToxoDB:TGMAS_265450; -.
DR VEuPathDB; ToxoDB:TGME49_265450; -.
DR VEuPathDB; ToxoDB:TGP89_265450; -.
DR VEuPathDB; ToxoDB:TGPRC2_265450; -.
DR VEuPathDB; ToxoDB:TGRH88_012030; -.
DR VEuPathDB; ToxoDB:TGRUB_265450; -.
DR VEuPathDB; ToxoDB:TGVAND_265450; -.
DR VEuPathDB; ToxoDB:TGVEG_265450; -.
DR SABIO-RK; Q969A8; -.
DR UniPathway; UPA00109; UER00180.
DR UniPathway; UPA00242; -.
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 2: Evidence at transcript level;
KW ATP-binding; Glycolysis; Kinase; Nucleotide-binding; Transferase.
FT CHAIN 1..468
FT /note="Hexokinase"
FT /id="PRO_0000197600"
FT DOMAIN 10..466
FT /note="Hexokinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01084"
FT REGION 74..225
FT /note="Hexokinase small subdomain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01084"
FT REGION 163..189
FT /note="Glucose-binding"
FT /evidence="ECO:0000255"
FT REGION 226..455
FT /note="Hexokinase large subdomain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01084"
FT BINDING 85..90
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 468 AA; 51468 MW; 4758C4D97F253D68 CRC64;
MQPRQPGDEA KQLAELEVVR QMMTPTREVL LELHESFLKE LQRGLEMHKR HGITWVPEEC
SMKMLDSCVS NLPTGAEVGE AYAIDFGGST CRAVRCSLLG KGKMEIIQDK ICLRSAEHRC
AKGFMDKKAG GKELFDQFAM CIRGLMDRSG DLKKAEETNT PVPVGFTFSF PCAQAALNSS
FLIEWTKGFE TGRENPDRVE GKDVAVLLAD ALQRHNVPAV CKAIVNDTVG TLVSCAYQRV
PGTPECRVGL IIGTGFNACY VEPEASNYGY TGTVVNMEAG NFHKDLPRNE IDVEVDEKTH
NRGKQQFEKL VSGYYIGEIV RVAAVRVFGA RAPEKASVRH SIHGETASTI RDDHSQDKAA
SIQAIKECWG VTMDLDDIKC IWEICRLVFD RSAAFAATLA VALCYRTGRL DTGSTVGIDG
ALYVKNQWYR EAVEYYTKLV AGDAAKNIHY CIADDGSGKG AALIADVN
