ID   HXKB_YEAST              Reviewed;         486 AA.
AC   P04807; D6VV82; Q05838;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 4.
DT   27-MAR-2024, entry version 225.
DE   RecName: Full=Hexokinase-2;
DE            EC=2.7.1.1 {ECO:0000305|PubMed:332086};
DE   AltName: Full=Hexokinase PII;
DE   AltName: Full=Hexokinase-B;
GN   Name=HXK2; Synonyms=HEX1, HKB; OrderedLocusNames=YGL253W;
GN   ORFNames=NRB486;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3003701; DOI=10.1093/nar/14.2.945;
RA   Stachelek C., Stachelek J., Swan J., Botstein D., Konigsberg W.;
RT   "Identification, cloning and sequence determination of the genes specifying
RT   hexokinase A and B from yeast.";
RL   Nucleic Acids Res. 14:945-963(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=3905511; DOI=10.1016/0378-1119(85)90074-5;
RA   Froehlich K.-U., Entian K.-D., Mecke D.;
RT   "The primary structure of the yeast hexokinase PII gene (HXK2) which is
RT   responsible for glucose repression.";
RL   Gene 36:105-111(1985).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 96604 / S288c / FY1679;
RX   PubMed=8972578;
RX   DOI=10.1002/(sici)1097-0061(199612)12:15%3c1555::aid-yea43%3e3.0.co;2-q;
RA   Coissac E., Maillier E., Robineau S., Netter P.;
RT   "Sequence of a 39,411 bp DNA fragment covering the left end of chromosome
RT   VII of Saccharomyces cerevisiae.";
RL   Yeast 12:1555-1562(1996).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169869;
RA   Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA   Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA   Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA   Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA   Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA   Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA   Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA   Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA   Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA   Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA   Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA   Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA   Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA   Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA   Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA   Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA   Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA   Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA   Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA   Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA   Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA   Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL   Nature 387:81-84(1997).
RN   [5]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [6]
RP   NUCLEOTIDE SEQUENCE OF 1-247.
RC   STRAIN=ATCC 200060 / W303;
RX   PubMed=8322518; DOI=10.1002/yea.320090512;
RA   Breitwieser W., Price C., Schuster T.;
RT   "Identification of a gene encoding a novel zinc finger protein in
RT   Saccharomyces cerevisiae.";
RL   Yeast 9:551-556(1993).
RN   [7]
RP   PROTEIN SEQUENCE OF 119-127; 176-185 AND 304-314.
RC   STRAIN=ATCC 38531 / Y41;
RX   PubMed=7737086; DOI=10.1002/elps.1150160124;
RA   Norbeck J., Blomberg A.;
RT   "Gene linkage of two-dimensional polyacrylamide gel electrophoresis
RT   resolved proteins from isogene families in Saccharomyces cerevisiae by
RT   microsequencing of in-gel trypsin generated peptides.";
RL   Electrophoresis 16:149-156(1995).
RN   [8]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=332086; DOI=10.1016/0003-9861(77)90544-6;
RA   Lobo Z., Maitra P.K.;
RT   "Physiological role of glucose-phosphorylating enzymes in Saccharomyces
RT   cerevisiae.";
RL   Arch. Biochem. Biophys. 182:639-645(1977).
RN   [9]
RP   PHOSPHORYLATION AT SER-15.
RX   PubMed=8286332; DOI=10.1021/bi00167a019;
RA   Kriegel T.M., Rush J., Vojtek A.B., Clifton D., Fraenkel D.G.;
RT   "In vivo phosphorylation site of hexokinase 2 in Saccharomyces
RT   cerevisiae.";
RL   Biochemistry 33:148-152(1994).
RN   [10]
RP   PHOSPHORYLATION AT SER-158.
RX   PubMed=9047292; DOI=10.1021/bi9623643;
RA   Heidrich K., Otto A., Behlke J., Rush J., Wenzel K.W., Kriegel T.;
RT   "Autophosphorylation-inactivation site of hexokinase 2 in Saccharomyces
RT   cerevisiae.";
RL   Biochemistry 36:1960-1964(1997).
RN   [11]
RP   PROTEIN SEQUENCE OF 2-19, AND PHOSPHORYLATION AT SER-15.
RX   PubMed=9718324; DOI=10.1021/bi980914m;
RA   Behlke J., Heidrich K., Naumann M., Mueller E.-C., Otto A., Reuter R.,
RA   Kriegel T.;
RT   "Hexokinase 2 from Saccharomyces cerevisiae: regulation of oligomeric
RT   structure by in vivo phosphorylation at serine-14.";
RL   Biochemistry 37:11989-11995(1998).
RN   [12]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-38 AND SER-158, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth phosphoproteome
RT   analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
RN   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15 AND SER-245, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19779198; DOI=10.1126/science.1172867;
RA   Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT   "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT   into evolution.";
RL   Science 325:1682-1686(2009).
RN   [15]
RP   X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
RX   PubMed=355643; DOI=10.1016/0022-2836(78)90374-1;
RA   Anderson C.M., Stenkamp R.E., Steitz T.A.;
RT   "Sequencing a protein by X-ray crystallography. II. Refinement of yeast
RT   hexokinase B co-ordinates and sequence at 2.1-A resolution.";
RL   J. Mol. Biol. 123:15-33(1978).
CC   -!- FUNCTION: Catalyzes the phosphorylation of hexose, such as D-glucose
CC       and D-fructose, to hexose 6-phosphate (D-glucose 6-phosphate and D-
CC       fructose 6-phosphate, respectively) (PubMed:332086). Mediates the
CC       initial step of glycolysis by catalyzing phosphorylation of D-glucose
CC       to D-glucose 6-phosphate (PubMed:332086). {ECO:0000269|PubMed:332086}.
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:0000305|PubMed:332086};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22741;
CC         Evidence={ECO:0000305|PubMed:332086};
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:0000305|PubMed:332086};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16126;
CC         Evidence={ECO:0000305|PubMed:332086};
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:0000305|PubMed:332086};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17826;
CC         Evidence={ECO:0000305|PubMed:332086};
CC   -!- ACTIVITY REGULATION: Subject to allosteric control. Substrate
CC       inhibition by ATP.
CC   -!- PATHWAY: Carbohydrate metabolism; hexose metabolism.
CC       {ECO:0000305|PubMed:332086}.
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC       phosphate and glycerone phosphate from D-glucose: step 1/4.
CC       {ECO:0000305|PubMed:332086}.
CC   -!- SUBUNIT: Homodimer.
CC   -!- MISCELLANEOUS: In yeast there are three glucose-phosphorylating
CC       isoenzymes, designated hexokinase I, II and glucokinase.
CC   -!- MISCELLANEOUS: Present with 114000 molecules/cell in log phase SD
CC       medium. {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the hexokinase family. {ECO:0000255|PROSITE-
CC       ProRule:PRU01084, ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Worthington enzyme manual;
CC       URL="https://www.worthington-biochem.com/HK/";
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DR   EMBL; X03483; CAA27203.1; -; Genomic_DNA.
DR   EMBL; M11181; AAA34697.1; -; Genomic_DNA.
DR   EMBL; M14411; AAA34699.1; -; mRNA.
DR   EMBL; X94357; CAA64134.1; -; Genomic_DNA.
DR   EMBL; Z72775; CAA96973.1; -; Genomic_DNA.
DR   EMBL; X67787; CAA48003.1; -; Genomic_DNA.
DR   EMBL; BK006941; DAA07866.1; -; Genomic_DNA.
DR   PIR; S61608; KIBYHB.
DR   RefSeq; NP_011261.1; NM_001181119.1.
DR   PDB; 1IG8; X-ray; 2.20 A; A=1-486.
DR   PDB; 2YHX; X-ray; 2.10 A; A=152-471.
DR   PDB; 5UWT; X-ray; 2.34 A; D=14-36.
DR   PDBsum; 1IG8; -.
DR   PDBsum; 2YHX; -.
DR   PDBsum; 5UWT; -.
DR   AlphaFoldDB; P04807; -.
DR   SMR; P04807; -.
DR   BioGRID; 33026; 323.
DR   DIP; DIP-2380N; -.
DR   IntAct; P04807; 17.
DR   MINT; P04807; -.
DR   STRING; 4932.YGL253W; -.
DR   MoonProt; P04807; -.
DR   CarbonylDB; P04807; -.
DR   iPTMnet; P04807; -.
DR   MaxQB; P04807; -.
DR   PaxDb; 4932-YGL253W; -.
DR   PeptideAtlas; P04807; -.
DR   TopDownProteomics; P04807; -.
DR   EnsemblFungi; YGL253W_mRNA; YGL253W; YGL253W.
DR   GeneID; 852639; -.
DR   KEGG; sce:YGL253W; -.
DR   AGR; SGD:S000003222; -.
DR   SGD; S000003222; HXK2.
DR   VEuPathDB; FungiDB:YGL253W; -.
DR   eggNOG; KOG1369; Eukaryota.
DR   GeneTree; ENSGT00950000182787; -.
DR   HOGENOM; CLU_014393_5_2_1; -.
DR   InParanoid; P04807; -.
DR   OMA; ADCVQQF; -.
DR   OrthoDB; 5481886at2759; -.
DR   BioCyc; MetaCyc:YGL253W-MONOMER; -.
DR   BioCyc; YEAST:YGL253W-MONOMER; -.
DR   BRENDA; 2.7.1.1; 984.
DR   Reactome; R-SCE-170822; Regulation of Glucokinase by Glucokinase Regulatory Protein.
DR   Reactome; R-SCE-6798695; Neutrophil degranulation.
DR   Reactome; R-SCE-70171; Glycolysis.
DR   SABIO-RK; P04807; -.
DR   UniPathway; UPA00109; UER00180.
DR   UniPathway; UPA00242; -.
DR   BioGRID-ORCS; 852639; 1 hit in 10 CRISPR screens.
DR   EvolutionaryTrace; P04807; -.
DR   PRO; PR:P04807; -.
DR   Proteomes; UP000002311; Chromosome VII.
DR   RNAct; P04807; Protein.
DR   GO; GO:0005829; C:cytosol; IDA:SGD.
DR   GO; GO:0031966; C:mitochondrial membrane; IMP:SGD.
DR   GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR   GO; GO:0005634; C:nucleus; IDA:SGD.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008865; F:fructokinase activity; IBA:GO_Central.
DR   GO; GO:0004340; F:glucokinase activity; IBA:GO_Central.
DR   GO; GO:0005536; F:glucose binding; IEA:InterPro.
DR   GO; GO:0004396; F:hexokinase activity; IDA:SGD.
DR   GO; GO:0019158; F:mannokinase activity; IBA:GO_Central.
DR   GO; GO:0046835; P:carbohydrate phosphorylation; IBA:GO_Central.
DR   GO; GO:1990539; P:fructose import across plasma membrane; IGI:SGD.
DR   GO; GO:0006000; P:fructose metabolic process; IMP:SGD.
DR   GO; GO:0051156; P:glucose 6-phosphate metabolic process; IBA:GO_Central.
DR   GO; GO:0046323; P:glucose import; IGI:SGD.
DR   GO; GO:0006006; P:glucose metabolic process; IMP:SGD.
DR   GO; GO:0006096; P:glycolytic process; IDA:SGD.
DR   GO; GO:0001678; P:intracellular glucose homeostasis; IBA:GO_Central.
DR   GO; GO:0006013; P:mannose metabolic process; IDA:SGD.
DR   GO; GO:2001234; P:negative regulation of apoptotic signaling pathway; IMP:SGD.
DR   GO; GO:0008361; P:regulation of cell size; HMP:SGD.
DR   GO; GO:0046015; P:regulation of transcription by glucose; IDA:SGD.
DR   CDD; cd00012; NBD_sugar-kinase_HSP70_actin; 1.
DR   Gene3D; 1.10.287.1250; -; 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.
DR   SWISS-2DPAGE; P04807; -.
PE   1: Evidence at protein level;
KW   3D-structure; Allosteric enzyme; ATP-binding; Direct protein sequencing;
KW   Glycolysis; Kinase; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW   Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:9718324"
FT   CHAIN           2..486
FT                   /note="Hexokinase-2"
FT                   /id="PRO_0000197602"
FT   DOMAIN          21..469
FT                   /note="Hexokinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01084"
FT   REGION          75..209
FT                   /note="Hexokinase small subdomain"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01084"
FT   REGION          210..458
FT                   /note="Hexokinase large subdomain"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01084"
FT   BINDING         86..91
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         111
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   BINDING         158
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         175..176
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         210..211
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         237
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         269
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         302
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         307..308
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         344..348
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         419..423
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         15
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:8286332,
FT                   ECO:0000269|PubMed:9718324, ECO:0007744|PubMed:19779198"
FT   MOD_RES         38
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   MOD_RES         158
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:9047292,
FT                   ECO:0007744|PubMed:18407956"
FT   MOD_RES         245
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         272
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P04806"
FT   CONFLICT        29
FT                   /note="N -> I (in Ref. 1; CAA27203)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        33
FT                   /note="I -> N (in Ref. 2; AAA34697/AAA34699)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        61
FT                   /note="G -> V (in Ref. 1; CAA27203)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        197
FT                   /note="T -> S (in Ref. 1; CAA27203)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        202
FT                   /note="P -> H (in Ref. 2; AAA34699)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        421..422
FT                   /note="YN -> ST (in Ref. 2; AAA34697/AAA34699)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        444..445
FT                   /note="TS -> PH (in Ref. 2; AAA34697/AAA34699)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        453
FT                   /note="I -> V (in Ref. 2; AAA34697/AAA34699)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        462
FT                   /note="A -> P (in Ref. 2; AAA34697/AAA34699)"
FT                   /evidence="ECO:0000305"
FT   HELIX           27..34
FT                   /evidence="ECO:0007829|PDB:2YHX"
FT   HELIX           38..54
FT                   /evidence="ECO:0007829|PDB:2YHX"
FT   STRAND          58..60
FT                   /evidence="ECO:0007829|PDB:2YHX"
FT   STRAND          80..87
FT                   /evidence="ECO:0007829|PDB:2YHX"
FT   STRAND          89..100
FT                   /evidence="ECO:0007829|PDB:2YHX"
FT   STRAND          104..113
FT                   /evidence="ECO:0007829|PDB:2YHX"
FT   TURN            116..119
FT                   /evidence="ECO:0007829|PDB:2YHX"
FT   HELIX           125..142
FT                   /evidence="ECO:0007829|PDB:2YHX"
FT   STRAND          151..156
FT                   /evidence="ECO:0007829|PDB:2YHX"
FT   STRAND          159..162
FT                   /evidence="ECO:0007829|PDB:1IG8"
FT   HELIX           189..200
FT                   /evidence="ECO:0007829|PDB:2YHX"
FT   STRAND          203..209
FT                   /evidence="ECO:0007829|PDB:2YHX"
FT   HELIX           211..222
FT                   /evidence="ECO:0007829|PDB:2YHX"
FT   STRAND          226..241
FT                   /evidence="ECO:0007829|PDB:2YHX"
FT   HELIX           246..248
FT                   /evidence="ECO:0007829|PDB:2YHX"
FT   STRAND          256..258
FT                   /evidence="ECO:0007829|PDB:2YHX"
FT   STRAND          264..267
FT                   /evidence="ECO:0007829|PDB:2YHX"
FT   TURN            271..276
FT                   /evidence="ECO:0007829|PDB:2YHX"
FT   STRAND          278..280
FT                   /evidence="ECO:0007829|PDB:2YHX"
FT   HELIX           284..292
FT                   /evidence="ECO:0007829|PDB:2YHX"
FT   STRAND          293..295
FT                   /evidence="ECO:0007829|PDB:1IG8"
FT   HELIX           300..305
FT                   /evidence="ECO:0007829|PDB:2YHX"
FT   HELIX           307..309
FT                   /evidence="ECO:0007829|PDB:2YHX"
FT   HELIX           310..323
FT                   /evidence="ECO:0007829|PDB:2YHX"
FT   STRAND          326..330
FT                   /evidence="ECO:0007829|PDB:2YHX"
FT   TURN            334..336
FT                   /evidence="ECO:0007829|PDB:1IG8"
FT   HELIX           345..352
FT                   /evidence="ECO:0007829|PDB:2YHX"
FT   STRAND          355..357
FT                   /evidence="ECO:0007829|PDB:2YHX"
FT   HELIX           359..369
FT                   /evidence="ECO:0007829|PDB:2YHX"
FT   HELIX           375..396
FT                   /evidence="ECO:0007829|PDB:2YHX"
FT   HELIX           398..407
FT                   /evidence="ECO:0007829|PDB:2YHX"
FT   STRAND          410..418
FT                   /evidence="ECO:0007829|PDB:2YHX"
FT   TURN            419..422
FT                   /evidence="ECO:0007829|PDB:2YHX"
FT   HELIX           427..439
FT                   /evidence="ECO:0007829|PDB:2YHX"
FT   HELIX           446..448
FT                   /evidence="ECO:0007829|PDB:2YHX"
FT   STRAND          449..455
FT                   /evidence="ECO:0007829|PDB:2YHX"
FT   TURN            459..461
FT                   /evidence="ECO:0007829|PDB:2YHX"
FT   HELIX           462..471
FT                   /evidence="ECO:0007829|PDB:2YHX"
SQ   SEQUENCE   486 AA;  53942 MW;  D55FF3F8992B2FEF CRC64;
     MVHLGPKKPQ ARKGSMADVP KELMQQIENF EKIFTVPTET LQAVTKHFIS ELEKGLSKKG
     GNIPMIPGWV MDFPTGKESG DFLAIDLGGT NLRVVLVKLG GDRTFDTTQS KYRLPDAMRT
     TQNPDELWEF IADSLKAFID EQFPQGISEP IPLGFTFSFP ASQNKINEGI LQRWTKGFDI
     PNIENHDVVP MLQKQITKRN IPIEVVALIN DTTGTLVASY YTDPETKMGV IFGTGVNGAY
     YDVCSDIEKL QGKLSDDIPP SAPMAINCEY GSFDNEHVVL PRTKYDITID EESPRPGQQT
     FEKMSSGYYL GEILRLALMD MYKQGFIFKN QDLSKFDKPF VMDTSYPARI EEDPFENLED
     TDDLFQNEFG INTTVQERKL IRRLSELIGA RAARLSVCGI AAICQKRGYK TGHIAADGSV
     YNRYPGFKEK AANALKDIYG WTQTSLDDYP IKIVPAEDGS GAGAAVIAAL AQKRIAEGKS
     VGIIGA
//