HXK1_RAT
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 03-AUG-2022, entry version 184.
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:5871820,
CC PubMed:3579310). 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=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:0000269|PubMed:13211595, ECO:0000269|PubMed:3579310,
CC 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=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: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=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: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=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:0000269|PubMed:13211595};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11029;
CC Evidence={ECO:0000269|PubMed:13211595};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + D-glucosamine = ADP + D-glucosamine 6-phosphate + 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). {ECO:0000250|UniProtKB:P17710,
CC 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_036866.1; NM_012734.1.
DR PDB; 1BG3; X-ray; 2.80 A; A/B=1-918.
DR PDBsum; 1BG3; -.
DR AlphaFoldDB; P05708; -.
DR SMR; P05708; -.
DR BioGRID; 247135; 5.
DR IntAct; P05708; 3.
DR MINT; P05708; -.
DR ChEMBL; CHEMBL4783; -.
DR iPTMnet; P05708; -.
DR PhosphoSitePlus; P05708; -.
DR World-2DPAGE; 0004:P05708; -.
DR jPOST; P05708; -.
DR PaxDb; P05708; -.
DR PRIDE; P05708; -.
DR DNASU; 25058; -.
DR GeneID; 25058; -.
DR KEGG; rno:25058; -.
DR CTD; 3098; -.
DR RGD; 2796; Hk1.
DR InParanoid; P05708; -.
DR OrthoDB; 1153545at2759; -.
DR PhylomeDB; P05708; -.
DR BRENDA; 2.7.1.1; 5301.
DR Reactome; R-RNO-70171; Glycolysis.
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:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0045121; C:membrane raft; ISO:RGD.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:RGD.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0005524; F:ATP binding; IDA:RGD.
DR GO; GO:0016887; F:ATP hydrolysis activity; IC: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; IEA:RHEA.
DR GO; GO:0005536; F:glucose binding; IDA:RGD.
DR GO; GO:0004396; F:hexokinase activity; IDA:RGD.
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:0044877; F:protein-containing complex binding; IDA:RGD.
DR GO; GO:0061621; P:canonical glycolysis; ISO:RGD.
DR GO; GO:0046835; P:carbohydrate phosphorylation; IDA:RGD.
DR GO; GO:0001678; P:cellular glucose homeostasis; IBA:GO_Central.
DR GO; GO:0072655; P:establishment of protein localization to mitochondrion; ISO:RGD.
DR GO; GO:0006002; P:fructose 6-phosphate metabolic process; IDA:UniProtKB.
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:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
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: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:0006468; P:protein phosphorylation; IDA:RGD.
DR GO; GO:0010359; P:regulation of anion channel activity; 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 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; 2.
DR Pfam; PF00349; Hexokinase_1; 2.
DR Pfam; PF03727; Hexokinase_2; 2.
DR SUPFAM; SSF53067; SSF53067; 4.
DR PROSITE; PS00378; HEXOKINASE_1; 2.
DR PROSITE; PS51748; HEXOKINASE_2; 2.
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..97
FT /evidence="ECO:0007829|PDB:1BG3"
FT STRAND 106..108
FT /evidence="ECO:0007829|PDB:1BG3"
FT HELIX 123..140
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 TURN 501..503
FT /evidence="ECO:0007829|PDB:1BG3"
FT HELIX 504..506
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
