HXKB_YEAST
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 03-AUG-2022, entry version 218.
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; 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<1555::aid-yea43>3.0.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; 305.
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 SWISS-2DPAGE; P04807; -.
DR MaxQB; P04807; -.
DR PaxDb; P04807; -.
DR PRIDE; P04807; -.
DR TopDownProteomics; P04807; -.
DR EnsemblFungi; YGL253W_mRNA; YGL253W; YGL253W.
DR GeneID; 852639; -.
DR KEGG; sce:YGL253W; -.
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; IAINCEW; -.
DR BioCyc; MetaCyc:YGL253W-MON; -.
DR BioCyc; YEAST:YGL253W-MON; -.
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 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:0001678; P:cellular glucose homeostasis; 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: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 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; 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
