ID   HXK1_RAT                Reviewed;         918 AA.
AC   P05708;
DT   01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 4.
DT   02-SEP-2026, entry version 202.
DE   RecName: Full=Hexokinase-1 {ECO:0000305};
DE            EC=2.7.1.1 {ECO:0000269|PubMed:13211595, ECO:0000269|PubMed:3579310, ECO:0000269|PubMed:5871820};
DE   AltName: Full=Brain form hexokinase {ECO:0000303|PubMed:2704734};
DE   AltName: Full=Hexokinase type I {ECO:0000303|PubMed:3579310};
DE            Short=HK I {ECO:0000303|PubMed:3579310};
DE   AltName: Full=Hexokinase-A {ECO:0000303|PubMed:5871820};
GN   Name=Hk1 {ECO:0000312|RGD:2796};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-466.
RC   TISSUE=Brain;
RX   PubMed=2704734; DOI=10.1073/pnas.86.8.2563;
RA   Schwab D.A., Wilson J.E.;
RT   "Complete amino acid sequence of rat brain hexokinase, deduced from the
RT   cloned cDNA, and proposed structure of a mammalian hexokinase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 86:2563-2567(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 467-918.
RC   TISSUE=Brain;
RX   PubMed=3277968; DOI=10.1016/s0021-9258(18)69058-1;
RA   Schwab D.A., Wilson J.E.;
RT   "The complete amino acid sequence of the catalytic domain of rat brain
RT   hexokinase, deduced from the cloned cDNA.";
RL   J. Biol. Chem. 263:3220-3224(1988).
RN   [3]
RP   SEQUENCE REVISION.
RA   Wilson J.E.;
RL   Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   PROTEIN SEQUENCE OF 597-617; 625-636 AND 802-816.
RC   TISSUE=Brain;
RX   PubMed=3631958; DOI=10.1016/0003-9861(87)90536-4;
RA   Schirch D.M., Wilson J.E.;
RT   "Rat brain hexokinase: amino acid sequence at the substrate hexose binding
RT   site is homologous to that of yeast hexokinase.";
RL   Arch. Biochem. Biophys. 257:1-12(1987).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.
RC   STRAIN=Sprague-Dawley; TISSUE=Liver;
RA   White J.A., Liu W., Wilson J.E.;
RL   Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 221-246 AND 631-668.
RA   White J.A., Wilson J.E.;
RL   Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=13211595; DOI=10.1016/s0021-9258(18)65384-0;
RA   Sols A., Crane R.K.;
RT   "Substrate specificity of brain hexokinase.";
RL   J. Biol. Chem. 210:581-595(1954).
RN   [8]
RP   FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=5871820; DOI=10.1016/0006-291x(64)90038-5;
RA   Gonzalez C., Ureta T., Sanchez R., Niemeyer H.;
RT   "Multiple molecular forms of ATP:hexose 6-phosphotransferase from rat
RT   liver.";
RL   Biochem. Biophys. Res. Commun. 16:347-352(1964).
RN   [9]
RP   REVIEW.
RX   PubMed=7044667; DOI=10.1016/0305-0491(82)90461-8;
RA   Ureta T.;
RT   "The comparative isozymology of vertebrate hexokinases.";
RL   Comp. Biochem. Physiol. 71:549-555(1982).
RN   [10]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=3579310; DOI=10.1016/0003-9861(87)90116-0;
RA   Schirch D.M., Wilson J.E.;
RT   "Rat brain hexokinase: location of the substrate hexose binding site in a
RT   structural domain at the C-terminus of the enzyme.";
RL   Arch. Biochem. Biophys. 254:385-396(1987).
RN   [11]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND TISSUE SPECIFICITY.
RX   PubMed=19423663; DOI=10.1530/rep-09-0052;
RA   Khan S.A., Suryawanshi A.R., Ranpura S.A., Jadhav S.V., Khole V.V.;
RT   "Identification of novel immunodominant epididymal sperm proteins using
RT   combinatorial approach.";
RL   Reproduction 138:81-93(2009).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-337, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
RN   [13]
RP   X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH GLUCOSE AND
RP   GLUCOSE-6-PHOSPHATE.
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, such as D-
CC       glucose, D-glucosamine, D-fructose, D-mannose and 2-deoxy-D-glucose, to
CC       hexose 6-phosphate (D-glucose 6-phosphate, D-glucosamine 6-phosphate,
CC       D-fructose 6-phosphate, D-mannose 6-phosphate and 2-deoxy-D-glucose 6-
CC       phosphate, respectively) (PubMed:13211595, PubMed:3579310,
CC       PubMed:5871820). Mediates the initial step of glycolysis by catalyzing
CC       phosphorylation of D-glucose to D-glucose 6-phosphate (PubMed:13211595,
CC       PubMed:5871820). Involved in innate immunity and inflammation by acting
CC       as a pattern recognition receptor for bacterial peptidoglycan (By
CC       similarity). When released in the cytosol, N-acetyl-D-glucosamine
CC       component of bacterial peptidoglycan inhibits the hexokinase activity
CC       of HK1 and causes its dissociation from mitochondrial outer membrane,
CC       thereby activating the NLRP3 inflammasome (By similarity).
CC       {ECO:0000250|UniProtKB:P19367, ECO:0000269|PubMed:13211595,
CC       ECO:0000269|PubMed:3579310, ECO:0000269|PubMed:5871820}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a D-hexose + ATP = a D-hexose 6-phosphate + ADP + H(+);
CC         Xref=Rhea:RHEA:22740, ChEBI:CHEBI:4194, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:229467, ChEBI:CHEBI:456216;
CC         EC=2.7.1.1; Evidence={ECO:0000269|PubMed:13211595,
CC         ECO:0000269|PubMed:3579310, ECO:0000269|PubMed:5871820};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22741;
CC         Evidence={ECO:0000269|PubMed:13211595, ECO:0000269|PubMed:3579310,
CC         ECO:0000269|PubMed:5871820};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-fructose + ATP = D-fructose 6-phosphate + ADP + 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:0000269|PubMed:13211595, ECO:0000269|PubMed:5871820};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16126;
CC         Evidence={ECO:0000269|PubMed:13211595, ECO:0000269|PubMed:5871820};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-glucose + ATP = D-glucose 6-phosphate + ADP + 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:0000269|PubMed:13211595, ECO:0000269|PubMed:5871820};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17826;
CC         Evidence={ECO:0000269|PubMed:5871820};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-mannose + ATP = D-mannose 6-phosphate + ADP + 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:0000269|PubMed:13211595};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11029;
CC         Evidence={ECO:0000269|PubMed:13211595};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-glucosamine + ATP = D-glucosamine 6-phosphate + ADP + H(+);
CC         Xref=Rhea:RHEA:10948, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:58723, ChEBI:CHEBI:58725, ChEBI:CHEBI:456216; EC=2.7.1.1;
CC         Evidence={ECO:0000250|UniProtKB:P19367};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10949;
CC         Evidence={ECO:0000250|UniProtKB:P19367};
CC   -!- ACTIVITY REGULATION: Hexokinase is an allosteric enzyme inhibited by
CC       its product D-glucose 6-phosphate. Hexokinase activity is inhibited by
CC       N-acetyl-D-glucosamine. {ECO:0000250|UniProtKB:P19367}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=44 uM for D-glucose {ECO:0000269|PubMed:5871820};
CC         KM=3.1 mM for D-fructose {ECO:0000269|PubMed:5871820};
CC         KM=0.42 mM for ATP {ECO:0000269|PubMed:5871820};
CC   -!- PATHWAY: Carbohydrate metabolism; hexose metabolism.
CC       {ECO:0000305|PubMed:5871820}.
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC       phosphate and glycerone phosphate from D-glucose: step 1/4.
CC       {ECO:0000305|PubMed:5871820}.
CC   -!- SUBUNIT: Monomer (By similarity). Interacts with RABL2/RABL2A; binds
CC       preferentially to GTP-bound RABL2 (By similarity). Interacts with
CC       VDAC1. The HK1-VDAC1 complex interacts with ATF2 (By similarity).
CC       Interacts (via N-terminal spermatogenic cell-specific region) with PFKM
CC       (via C-terminus) (By similarity). Interacts with SMAD5 (By similarity).
CC       {ECO:0000250|UniProtKB:P17710, ECO:0000250|UniProtKB:P19367}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC       {ECO:0000250|UniProtKB:P19367}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:P19367}. Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:P19367}. Note=The mitochondrial-binding peptide
CC       (MBP) region promotes association with the mitochondrial outer
CC       membrane. Dissociates from the mitochondrial outer membrane following
CC       inhibition by N-acetyl-D-glucosamine, leading to relocation to the
CC       cytosol. {ECO:0000250|UniProtKB:P19367}.
CC   -!- TISSUE SPECIFICITY: Expressed in flagella of epididymal sperm.
CC       {ECO:0000269|PubMed:19423663}.
CC   -!- DOMAIN: The N- and C-terminal halves of this hexokinase contain a
CC       hexokinase domain. The catalytic activity is associated with the C-
CC       terminus while regulatory function is associated with the N-terminus.
CC       Each domain can bind a single D-glucose and D-glucose 6-phosphate
CC       molecule. {ECO:0000250|UniProtKB:P19367}.
CC   -!- SIMILARITY: Belongs to the hexokinase family. {ECO:0000255|PROSITE-
CC       ProRule:PRU01084, ECO:0000305}.
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DR   EMBL; J04526; AAC20075.1; -; mRNA.
DR   EMBL; U27319; AAC52945.1; -; Genomic_DNA.
DR   EMBL; U89160; AAB71376.1; -; Genomic_DNA.
DR   EMBL; U89158; AAB71374.1; -; Genomic_DNA.
DR   PIR; A32521; A32521.
DR   PIR; B32521; B32521.
DR   PIR; C32521; C32521.
DR   PIR; C59226; C59226.
DR   RefSeq; NP_036866.2; NM_012734.2.
DR   PDB; 1BG3; X-ray; 2.80 A; A/B=1-918.
DR   AlphaFoldDB; P05708; -.
DR   SMR; P05708; -.
DR   BioGRID; 247135; 6.
DR   FunCoup; P05708; 778.
DR   IntAct; P05708; 4.
DR   MINT; P05708; -.
DR   STRING; 10116.ENSRNOP00000066611; -.
DR   ChEMBL; CHEMBL4783; -.
DR   GlyGen; P05708; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P05708; -.
DR   PhosphoSitePlus; P05708; -.
DR   jPOST; P05708; -.
DR   PaxDb; 10116-ENSRNOP00000066611; -.
DR   DNASU; 25058; -.
DR   GeneID; 25058; -.
DR   KEGG; rno:25058; -.
DR   AGR; RGD:2796; -.
DR   CTD; 3098; -.
DR   RGD; 2796; Hk1.
DR   InParanoid; P05708; -.
DR   PhylomeDB; P05708; -.
DR   BRENDA; 2.7.1.1; 5301.
DR   SABIO-RK; P05708; -.
DR   UniPathway; UPA00109; UER00180.
DR   UniPathway; UPA00242; -.
DR   EvolutionaryTrace; P05708; -.
DR   PRO; PR:P05708; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005901; C:caveola; IDA:RGD.
DR   GO; GO:0005929; C:cilium; ISO:RGD.
DR   GO; GO:0005829; C:cytosol; ISO:RGD.
DR   GO; GO:0045121; C:membrane raft; ISO:RGD.
DR   GO; GO:0005741; C:mitochondrial outer membrane; ISS:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; IDA:CACAO.
DR   GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR   GO; GO:0097228; C:sperm principal piece; ISO:RGD.
DR   GO; GO:0005524; F:ATP binding; IDA:RGD.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IC:RGD.
DR   GO; GO:0005536; F:D-glucose binding; IDA:RGD.
DR   GO; GO:0008865; F:fructokinase activity; IDA:UniProtKB.
DR   GO; GO:0004340; F:glucokinase activity; IDA:UniProtKB.
DR   GO; GO:0047931; F:glucosamine kinase activity; ISS:UniProtKB.
DR   GO; GO:0004396; F:hexokinase activity; IDA:CACAO.
DR   GO; GO:0042802; F:identical protein binding; IPI:RGD.
DR   GO; GO:0019158; F:mannokinase activity; IDA:UniProtKB.
DR   GO; GO:0042834; F:peptidoglycan binding; ISO:RGD.
DR   GO; GO:0004672; F:protein kinase activity; IDA:RGD.
DR   GO; GO:0061621; P:canonical glycolysis; ISO:RGD.
DR   GO; GO:0046835; P:carbohydrate phosphorylation; IDA:RGD.
DR   GO; GO:0006002; P:fructose 6-phosphate metabolic process; IDA:UniProtKB.
DR   GO; GO:0009298; P:GDP-mannose biosynthetic process; ISO:RGD.
DR   GO; GO:0051156; P:glucose 6-phosphate metabolic process; IDA:UniProtKB.
DR   GO; GO:0006006; P:glucose metabolic process; IBA:GO_Central.
DR   GO; GO:0006096; P:glycolytic process; IDA:RGD.
DR   GO; GO:0001678; P:intracellular glucose homeostasis; IEA:InterPro.
DR   GO; GO:0072656; P:maintenance of protein location in mitochondrion; ISO:RGD.
DR   GO; GO:0006013; P:mannose metabolic process; IDA:UniProtKB.
DR   GO; GO:1903960; P:negative regulation of anion transmembrane transport; IDA:RGD.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; IMP:RGD.
DR   GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:RGD.
DR   GO; GO:0018107; P:peptidyl-threonine phosphorylation; IDA:RGD.
DR   GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA:RGD.
DR   GO; GO:0002720; P:positive regulation of cytokine production involved in immune response; ISO:RGD.
DR   GO; GO:0032731; P:positive regulation of interleukin-1 beta production; ISO:RGD.
DR   GO; GO:0046777; P:protein autophosphorylation; IDA:RGD.
DR   GO; GO:0070585; P:protein localization to mitochondrion; ISO:RGD.
DR   GO; GO:0006468; P:protein phosphorylation; IDA:RGD.
DR   GO; GO:0009741; P:response to brassinosteroid; IEP:RGD.
DR   GO; GO:0001666; P:response to hypoxia; IEP:RGD.
DR   GO; GO:0002931; P:response to ischemia; IDA:RGD.
DR   GO; GO:1901986; P:response to ketamine; IEP:RGD.
DR   CDD; cd24127; ASKHA_NBD_HK1_meta_rpt2; 1.
DR   FunFam; 3.30.420.40:FF:000015; Hexokinase 1; 2.
DR   FunFam; 3.40.367.20:FF:000001; Hexokinase 1; 1.
DR   FunFam; 3.40.367.20:FF:000020; Hexokinase-1; 1.
DR   Gene3D; 3.30.420.40; -; 2.
DR   Gene3D; 3.40.367.20; -; 2.
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:SF80; HEXOKINASE-1; 1.
DR   Pfam; PF00349; Hexokinase_1; 2.
DR   Pfam; PF03727; Hexokinase_2; 2.
DR   PRINTS; PR00475; HEXOKINASE.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 4.
DR   PROSITE; PS00378; HEXOKINASE_1; 2.
DR   PROSITE; PS51748; HEXOKINASE_2; 2.
DR   PDBsum; 1BG3; -.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Allosteric enzyme; ATP-binding; Cytoplasm;
KW   Direct protein sequencing; Glycolysis; Immunity; Inflammatory response;
KW   Innate immunity; Kinase; Membrane; Mitochondrion;
KW   Mitochondrion outer membrane; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome; Repeat; Transferase.
FT   CHAIN           1..918
FT                   /note="Hexokinase-1"
FT                   /id="PRO_0000197586"
FT   DOMAIN          16..458
FT                   /note="Hexokinase 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01084"
FT   DOMAIN          464..906
FT                   /note="Hexokinase 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01084"
FT   REGION          1..10
FT                   /note="Mitochondrial-binding peptide (MBP)"
FT                   /evidence="ECO:0000250|UniProtKB:P19367"
FT   REGION          73..207
FT                   /note="Hexokinase small subdomain 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01084"
FT   REGION          208..447
FT                   /note="Hexokinase large subdomain 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01084"
FT   REGION          521..655
FT                   /note="Hexokinase small subdomain 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01084"
FT   REGION          656..895
FT                   /note="Hexokinase large subdomain 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01084"
FT   BINDING         30
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P19367"
FT   BINDING         84..89
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P19367"
FT   BINDING         84..88
FT                   /ligand="D-glucose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:61548"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|PubMed:9665168,
FT                   ECO:0007744|PDB:1BG3"
FT   BINDING         155
FT                   /ligand="D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:4167"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|PubMed:9665168,
FT                   ECO:0007744|PDB:1BG3"
FT   BINDING         172..173
FT                   /ligand="D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:4167"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|PubMed:9665168,
FT                   ECO:0007744|PDB:1BG3"
FT   BINDING         208..209
FT                   /ligand="D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:4167"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|PubMed:9665168,
FT                   ECO:0007744|PDB:1BG3"
FT   BINDING         209
FT                   /ligand="D-glucose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:61548"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|PubMed:9665168,
FT                   ECO:0007744|PDB:1BG3"
FT   BINDING         232
FT                   /ligand="D-glucose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:61548"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|PubMed:9665168,
FT                   ECO:0007744|PDB:1BG3"
FT   BINDING         235
FT                   /ligand="D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:4167"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|PubMed:9665168,
FT                   ECO:0007744|PDB:1BG3"
FT   BINDING         260
FT                   /ligand="D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:4167"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|PubMed:9665168,
FT                   ECO:0007744|PDB:1BG3"
FT   BINDING         291..294
FT                   /ligand="D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:4167"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|PubMed:9665168,
FT                   ECO:0007744|PDB:1BG3"
FT   BINDING         413..415
FT                   /ligand="D-glucose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:61548"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|PubMed:9665168,
FT                   ECO:0007744|PDB:1BG3"
FT   BINDING         425..426
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P19367"
FT   BINDING         449
FT                   /ligand="D-glucose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:61548"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|PubMed:9665168,
FT                   ECO:0007744|PDB:1BG3"
FT   BINDING         532..537
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P19367"
FT   BINDING         532..536
FT                   /ligand="D-glucose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:61548"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:9665168,
FT                   ECO:0007744|PDB:1BG3"
FT   BINDING         603
FT                   /ligand="D-glucose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:61548"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:9665168,
FT                   ECO:0007744|PDB:1BG3"
FT   BINDING         620..621
FT                   /ligand="D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:4167"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:9665168,
FT                   ECO:0007744|PDB:1BG3"
FT   BINDING         656..657
FT                   /ligand="D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:4167"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:9665168,
FT                   ECO:0007744|PDB:1BG3"
FT   BINDING         657
FT                   /ligand="D-glucose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:61548"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:9665168,
FT                   ECO:0007744|PDB:1BG3"
FT   BINDING         680
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P19367"
FT   BINDING         680
FT                   /ligand="D-glucose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:61548"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:9665168,
FT                   ECO:0007744|PDB:1BG3"
FT   BINDING         683
FT                   /ligand="D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:4167"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:9665168,
FT                   ECO:0007744|PDB:1BG3"
FT   BINDING         708
FT                   /ligand="D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:4167"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:9665168,
FT                   ECO:0007744|PDB:1BG3"
FT   BINDING         742
FT                   /ligand="D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:4167"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:9665168,
FT                   ECO:0007744|PDB:1BG3"
FT   BINDING         747..748
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P19367"
FT   BINDING         784..788
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P19367"
FT   BINDING         861..863
FT                   /ligand="D-glucose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:61548"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:9665168,
FT                   ECO:0007744|PDB:1BG3"
FT   BINDING         863..867
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P19367"
FT   BINDING         897
FT                   /ligand="D-glucose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:61548"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:9665168,
FT                   ECO:0007744|PDB:1BG3"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:P19367"
FT   MOD_RES         337
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   HELIX           2..25
FT                   /evidence="ECO:0007829|PDB:1BG3"
FT   HELIX           27..29
FT                   /evidence="ECO:0007829|PDB:1BG3"
FT   HELIX           33..51
FT                   /evidence="ECO:0007829|PDB:1BG3"
FT   TURN            53..55
FT                   /evidence="ECO:0007829|PDB:1BG3"
FT   HELIX           56..58
FT                   /evidence="ECO:0007829|PDB:1BG3"
FT   STRAND          78..96
FT                   /evidence="ECO:0007829|PDB:1BG3"
FT   STRAND          106..108
FT                   /evidence="ECO:0007829|PDB:1BG3"
FT   TURN            116..120
FT                   /evidence="ECO:0007829|PDB:1BG3"
FT   HELIX           123..141
FT                   /evidence="ECO:0007829|PDB:1BG3"
FT   STRAND          144..146
FT                   /evidence="ECO:0007829|PDB:1BG3"
FT   STRAND          149..154
FT                   /evidence="ECO:0007829|PDB:1BG3"
FT   HELIX           185..196
FT                   /evidence="ECO:0007829|PDB:1BG3"
FT   STRAND          202..207
FT                   /evidence="ECO:0007829|PDB:1BG3"
FT   HELIX           209..220
FT                   /evidence="ECO:0007829|PDB:1BG3"
FT   STRAND          224..241
FT                   /evidence="ECO:0007829|PDB:1BG3"
FT   HELIX           242..244
FT                   /evidence="ECO:0007829|PDB:1BG3"
FT   STRAND          252..258
FT                   /evidence="ECO:0007829|PDB:1BG3"
FT   HELIX           261..263
FT                   /evidence="ECO:0007829|PDB:1BG3"
FT   TURN            264..273
FT                   /evidence="ECO:0007829|PDB:1BG3"
FT   HELIX           276..283
FT                   /evidence="ECO:0007829|PDB:1BG3"
FT   STRAND          285..287
FT                   /evidence="ECO:0007829|PDB:1BG3"
FT   HELIX           294..297
FT                   /evidence="ECO:0007829|PDB:1BG3"
FT   TURN            299..301
FT                   /evidence="ECO:0007829|PDB:1BG3"
FT   HELIX           302..315
FT                   /evidence="ECO:0007829|PDB:1BG3"
FT   HELIX           320..322
FT                   /evidence="ECO:0007829|PDB:1BG3"
FT   HELIX           326..329
FT                   /evidence="ECO:0007829|PDB:1BG3"
FT   HELIX           336..342
FT                   /evidence="ECO:0007829|PDB:1BG3"
FT   TURN            345..347
FT                   /evidence="ECO:0007829|PDB:1BG3"
FT   HELIX           348..358
FT                   /evidence="ECO:0007829|PDB:1BG3"
FT   HELIX           365..401
FT                   /evidence="ECO:0007829|PDB:1BG3"
FT   STRAND          404..406
FT                   /evidence="ECO:0007829|PDB:1BG3"
FT   STRAND          409..413
FT                   /evidence="ECO:0007829|PDB:1BG3"
FT   HELIX           415..419
FT                   /evidence="ECO:0007829|PDB:1BG3"
FT   HELIX           423..434
FT                   /evidence="ECO:0007829|PDB:1BG3"
FT   STRAND          441..444
FT                   /evidence="ECO:0007829|PDB:1BG3"
FT   HELIX           450..474
FT                   /evidence="ECO:0007829|PDB:1BG3"
FT   HELIX           475..477
FT                   /evidence="ECO:0007829|PDB:1BG3"
FT   HELIX           481..499
FT                   /evidence="ECO:0007829|PDB:1BG3"
FT   HELIX           501..504
FT                   /evidence="ECO:0007829|PDB:1BG3"
FT   STRAND          511..513
FT                   /evidence="ECO:0007829|PDB:1BG3"
FT   STRAND          526..537
FT                   /evidence="ECO:0007829|PDB:1BG3"
FT   STRAND          539..545
FT                   /evidence="ECO:0007829|PDB:1BG3"
FT   STRAND          548..550
FT                   /evidence="ECO:0007829|PDB:1BG3"
FT   STRAND          553..559
FT                   /evidence="ECO:0007829|PDB:1BG3"
FT   HELIX           564..567
FT                   /evidence="ECO:0007829|PDB:1BG3"
FT   HELIX           571..589
FT                   /evidence="ECO:0007829|PDB:1BG3"
FT   STRAND          596..602
FT                   /evidence="ECO:0007829|PDB:1BG3"
FT   HELIX           633..644
FT                   /evidence="ECO:0007829|PDB:1BG3"
FT   STRAND          649..655
FT                   /evidence="ECO:0007829|PDB:1BG3"
FT   HELIX           657..666
FT                   /evidence="ECO:0007829|PDB:1BG3"
FT   STRAND          672..689
FT                   /evidence="ECO:0007829|PDB:1BG3"
FT   HELIX           690..692
FT                   /evidence="ECO:0007829|PDB:1BG3"
FT   STRAND          700..707
FT                   /evidence="ECO:0007829|PDB:1BG3"
FT   HELIX           709..711
FT                   /evidence="ECO:0007829|PDB:1BG3"
FT   STRAND          714..716
FT                   /evidence="ECO:0007829|PDB:1BG3"
FT   TURN            717..721
FT                   /evidence="ECO:0007829|PDB:1BG3"
FT   HELIX           724..731
FT                   /evidence="ECO:0007829|PDB:1BG3"
FT   STRAND          733..735
FT                   /evidence="ECO:0007829|PDB:1BG3"
FT   HELIX           740..743
FT                   /evidence="ECO:0007829|PDB:1BG3"
FT   TURN            747..749
FT                   /evidence="ECO:0007829|PDB:1BG3"
FT   HELIX           750..763
FT                   /evidence="ECO:0007829|PDB:1BG3"
FT   HELIX           768..770
FT                   /evidence="ECO:0007829|PDB:1BG3"
FT   HELIX           774..777
FT                   /evidence="ECO:0007829|PDB:1BG3"
FT   HELIX           784..790
FT                   /evidence="ECO:0007829|PDB:1BG3"
FT   STRAND          793..795
FT                   /evidence="ECO:0007829|PDB:1BG3"
FT   HELIX           797..806
FT                   /evidence="ECO:0007829|PDB:1BG3"
FT   HELIX           813..848
FT                   /evidence="ECO:0007829|PDB:1BG3"
FT   STRAND          857..861
FT                   /evidence="ECO:0007829|PDB:1BG3"
FT   HELIX           863..867
FT                   /evidence="ECO:0007829|PDB:1BG3"
FT   HELIX           871..882
FT                   /evidence="ECO:0007829|PDB:1BG3"
FT   STRAND          889..892
FT                   /evidence="ECO:0007829|PDB:1BG3"
FT   HELIX           896..909
FT                   /evidence="ECO:0007829|PDB:1BG3"
SQ   SEQUENCE   918 AA;  102408 MW;  D2200820F0FC41EE CRC64;
     MIAAQLLAYY FTELKDDQVK KIDKYLYAMR LSDEILIDIL TRFKKEMKNG LSRDYNPTAS
     VKMLPTFVRS IPDGSEKGDF IALDLGGSSF RILRVQVNHE KNQNVSMESE IYDTPENIVH
     GSGTQLFDHV ADCLGDFMEK KKIKDKKLPV GFTFSFPCRQ SKIDEAVLIT WTKRFKASGV
     EGADVVKLLN KAIKKRGDYD ANIVAVVNDT VGTMMTCGYD DQQCEVGLII GTGTNACYME
     ELRHIDLVEG DEGRMCINTE WGAFGDDGSL EDIRTEFDRE LDRGSLNPGK QLFEKMVSGM
     YMGELVRLIL VKMAKEGLLF EGRITPELLT RGKFNTSDVS AIEKDKEGIQ NAKEILTRLG
     VEPSDVDCVS VQHICTIVSF RSANLVAATL GAILNRLRDN KGTPRLRTTV GVDGSLYKMH
     PQYSRRFHKT LRRLVPDSDV RFLLSESGTG KGAAMVTAVA YRLAEQHRQI EETLAHFRLS
     KQTLMEVKKR LRTEMEMGLR KETNSKATVK MLPSFVRSIP DGTEHGDFLA LDLGGTNFRV
     LLVKIRSGKK RTVEMHNKIY SIPLEIMQGT GDELFDHIVS CISDFLDYMG IKGPRMPLGF
     TFSFPCHQTN LDCGILISWT KGFKATDCEG HDVASLLRDA VKRREEFDLD VVAVVNDTVG
     TMMTCAYEEP TCEIGLIVGT GTNACYMEEM KNVEMVEGNQ GQMCINMEWG AFGDNGCLDD
     IRTDFDKVVD EYSLNSGKQR FEKMISGMYL GEIVRNILID FTKKGFLFRG QISEPLKTRG
     IFETKFLSQI ESDRLALLQV RAILQQLGLN STCDDSILVK TVCGVVSKRA AQLCGAGMAA
     VVEKIRENRG LDHLNVTVGV DGTLYKLHPH FSRIMHQTVK ELSPKCTVSF LLSEDGSGKG
     AALITAVGVR LRGDPSIA
//