ID KPYK1_ECOLI Reviewed; 470 AA. AC P0AD61; P14178; P76921; P78165; P78231; DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot. DT 06-DEC-2005, sequence version 1. DT 02-SEP-2026, entry version 160. DE RecName: Full=Pyruvate kinase I {ECO:0000303|PubMed:2674937}; DE EC=2.7.1.40 {ECO:0000269|PubMed:10751408, ECO:0000305|PubMed:7011316}; DE AltName: Full=PK-1; GN Name=pykF {ECO:0000303|PubMed:9023191}; GN OrderedLocusNames=b1676, JW1666; OS Escherichia coli (strain K12). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Enterobacterales; Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83333; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2674937; DOI=10.1073/pnas.86.18.6883; RA Ohara O., Dorit R.L., Gilbert W.; RT "Direct genomic sequencing of bacterial DNA: the pyruvate kinase I gene of RT Escherichia coli."; RL Proc. Natl. Acad. Sci. U.S.A. 86:6883-6887(1989). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=K12; RX PubMed=9023191; DOI=10.1128/jb.179.4.1105-1111.1997; RA Hensel M., Shea J.E., Baeumler A.J., Gleeson C., Blattner F.R., RA Holden D.W.; RT "Analysis of the boundaries of Salmonella pathogenicity island 2 and the RT corresponding chromosomal region of Escherichia coli K-12."; RL J. Bacteriol. 179:1105-1111(1997). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=9097039; DOI=10.1093/dnares/3.6.363; RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T., RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K., RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y., RA Wada C., Yamamoto Y., Horiuchi T.; RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to RT the 28.0-40.1 min region on the linkage map."; RL DNA Res. 3:363-377(1996). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX PubMed=9278503; DOI=10.1126/science.277.5331.1453; RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., RA Shao Y.; RT "The complete genome sequence of Escherichia coli K-12."; RL Science 277:1453-1462(1997). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION TO RP 451-470. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=16738553; DOI=10.1038/msb4100049; RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 RT and W3110."; RL Mol. Syst. Biol. 2:E1-E5(2006). RN [6] RP PROTEIN SEQUENCE OF 1-48. RX PubMed=1859631; DOI=10.1515/bchm3.1991.372.1.91; RA Valentini G., Stoppini M., Speranza M.L., Malcovati M., Ferri G.; RT "Bacterial pyruvate kinases have a shorter N-terminal domain."; RL Biol. Chem. Hoppe-Seyler 372:91-93(1991). RN [7] RP PROTEIN SEQUENCE OF 1-11. RC STRAIN=K12 / EMG2; RX PubMed=9298646; DOI=10.1002/elps.1150180807; RA Link A.J., Robison K., Church G.M.; RT "Comparing the predicted and observed properties of proteins encoded in the RT genome of Escherichia coli K-12."; RL Electrophoresis 18:1259-1313(1997). RN [8] RP PROTEIN SEQUENCE OF 293-319; 369-385 AND 389-404. RX PubMed=2653362; DOI=10.1515/bchm3.1989.370.1.211; RA Speranza M.L., Valentini G., Iadarola P., Stoppini M., Malcovati M., RA Ferri G.; RT "Primary structure of three peptides at the catalytic and allosteric sites RT of the fructose-1,6-bisphosphate-activated pyruvate kinase from Escherichia RT coli."; RL Biol. Chem. Hoppe-Seyler 370:211-216(1989). RN [9] RP CATALYTIC ACTIVITY, MAGNESIUM COFACTOR, AND ACTIVITY REGULATION. RC STRAIN=K12; RX PubMed=7011316; DOI=10.1042/bj1890421; RA Markus M., Plesser T., Boiteux A., Hess B., Malcovati M.; RT "Analysis of progress curves. Rate law of pyruvate kinase type I from RT Escherichia coli."; RL Biochem. J. 189:421-433(1980). RN [10] RP IDENTIFICATION BY 2D-GEL. RX PubMed=9298644; DOI=10.1002/elps.1150180805; RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.; RT "Escherichia coli proteome analysis using the gene-protein database."; RL Electrophoresis 18:1243-1251(1997). RN [11] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-76 AND LYS-319, AND RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=K12 / JW1106, and K12 / MG1655 / ATCC 47076; RX PubMed=18723842; DOI=10.1074/mcp.m800187-mcp200; RA Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., RA Grishin N.V., Zhao Y.; RT "Lysine acetylation is a highly abundant and evolutionarily conserved RT modification in Escherichia coli."; RL Mol. Cell. Proteomics 8:215-225(2009). RN [12] RP LACTYLATION, AND MUTAGENESIS OF LYS-382. RC STRAIN=K12 / MG1655 / ATCC 47076; RX PubMed=36333310; DOI=10.1038/s41467-022-34399-y; RA Dong H., Zhang J., Zhang H., Han Y., Lu C., Chen C., Tan X., Wang S., RA Bai X., Zhai G., Tian S., Zhang T., Cheng Z., Li E., Xu L., Zhang K.; RT "YiaC and CobB regulate lysine lactylation in Escherichia coli."; RL Nat. Commun. 13:6628-6628(2022). RN [13] {ECO:0007744|PDB:1PKY} RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF THE INACTIVE T-STATE, AND SUBUNIT. RX PubMed=8591049; DOI=10.1016/s0969-2126(01)00207-6; RA Mattevi A., Valentini G., Rizzi M., Speranza M.L., Bolognesi M., Coda A.; RT "Crystal structure of Escherichia coli pyruvate kinase type I: molecular RT basis of the allosteric transition."; RL Structure 3:729-741(1995). RN [14] {ECO:0007744|PDB:1E0T, ECO:0007744|PDB:1E0U} RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF MUTANT ENZYMES, FUNCTION, RP CATALYTIC ACTIVITY, SUBUNIT, AND MUTAGENESIS OF ARG-271; ARG-292; ASP-297; RP LYS-382; LYS-413 AND ARG-431. RX PubMed=10751408; DOI=10.1074/jbc.m001870200; RA Valentini G., Chiarelli L., Fortin R., Speranza M.L., Galizzi A., RA Mattevi A.; RT "The allosteric regulation of pyruvate kinase."; RL J. Biol. Chem. 275:18145-18152(2000). RN [15] {ECO:0007744|PDB:4YNG} RP X-RAY CRYSTALLOGRAPHY (2.28 ANGSTROMS), AND SUBUNIT. RX PubMed=27050130; DOI=10.1107/s205979831600142x; RA Donovan K.A., Atkinson S.C., Kessans S.A., Peng F., Cooper T.F., RA Griffin M.D., Jameson G.B., Dobson R.C.; RT "Grappling with anisotropic data, pseudo-merohedral twinning and pseudo- RT translational noncrystallographic symmetry: a case study involving pyruvate RT kinase."; RL Acta Crystallogr. D 72:512-519(2016). CC -!- FUNCTION: Catalyzes the formation of pyruvate in the last step of CC glycolysis, it is irreversible under physiological conditions. The CC reaction is critical for the control of metabolic flux in the second CC part of glycolysis. {ECO:0000269|PubMed:10751408}. CC -!- CATALYTIC ACTIVITY: CC Reaction=pyruvate + ATP = phosphoenolpyruvate + ADP + H(+); CC Xref=Rhea:RHEA:18157, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58702, ChEBI:CHEBI:456216; CC EC=2.7.1.40; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:18159; CC Evidence={ECO:0000269|PubMed:10751408, ECO:0000305|PubMed:7011316}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000269|PubMed:7011316}; CC -!- COFACTOR: CC Name=K(+); Xref=ChEBI:CHEBI:29103; CC Evidence={ECO:0000250|UniProtKB:Q02499}; CC -!- ACTIVITY REGULATION: Belongs to type I PK; fructose 1,6-bisphosphate- CC activated. {ECO:0000269|PubMed:7011316}. CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D- CC glyceraldehyde 3-phosphate: step 5/5. CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:10751408, CC ECO:0000269|PubMed:27050130, ECO:0000269|PubMed:8591049}. CC -!- INTERACTION: CC P0AD61; P0AD61: pykF; NbExp=2; IntAct=EBI-909449, EBI-909449; CC -!- PTM: Can be lactylated on Lys-382 (PubMed:36333310). Delactylated by CC the delactylase CobB (PubMed:36333310). Lactylation reduces activity of CC the enzyme and slows bacterial growth (PubMed:36333310). Lactylation CC may hinder the binding between fructose 1,6-bisphosphate (FBP) and PykF CC and weaken the allosteric activation of PykF, finally reducing the CC activity of PykF (PubMed:36333310). Delactylation by CobB regulates CC PykF activity and influences bacterial growth (PubMed:36333310). CC {ECO:0000269|PubMed:36333310}. CC -!- SIMILARITY: Belongs to the pyruvate kinase family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M24636; AAA24392.1; -; Genomic_DNA. DR EMBL; U68703; AAB47952.1; -; Genomic_DNA. DR EMBL; U00096; AAC74746.1; -; Genomic_DNA. DR EMBL; AP009048; BAA15445.2; -; Genomic_DNA. DR PIR; D64925; D64925. DR RefSeq; NP_416191.1; NC_000913.3. DR RefSeq; WP_001295403.1; NZ_CP009789.1. DR PDB; 1E0T; X-ray; 1.80 A; A/B/C/D=1-470. DR PDB; 1E0U; X-ray; 2.80 A; A/B/C/D=1-470. DR PDB; 1PKY; X-ray; 2.50 A; A/B/C/D=1-470. DR PDB; 4YNG; X-ray; 2.28 A; A/B/C/D/E/F/G/H=1-470. DR PDB; 8EDQ; X-ray; 2.88 A; A/B=1-470. DR PDB; 8EDR; X-ray; 2.64 A; A/B=1-470. DR PDB; 8EDS; X-ray; 2.10 A; A/B=1-470. DR PDB; 8EDT; X-ray; 2.09 A; A/B=1-470. DR PDB; 8EQ0; X-ray; 2.62 A; A/B=1-470. DR PDB; 8EQ1; X-ray; 2.32 A; A/B/C/D=1-470. DR PDB; 8EQ3; X-ray; 2.01 A; A/B=1-470. DR PDB; 8EU4; X-ray; 2.10 A; A/B/C/D/E/F/G/H=1-470. DR AlphaFoldDB; P0AD61; -. DR SMR; P0AD61; -. DR BioGRID; 4260275; 62. DR DIP; DIP-36221N; -. DR FunCoup; P0AD61; 723. DR IntAct; P0AD61; 21. DR STRING; 511145.b1676; -. DR iPTMnet; P0AD61; -. DR jPOST; P0AD61; -. DR PaxDb; 511145-b1676; -. DR EnsemblBacteria; AAC74746; AAC74746; b1676. DR GeneID; 93775831; -. DR GeneID; 946179; -. DR KEGG; ecj:JW1666; -. DR KEGG; eco:b1676; -. DR KEGG; ecoc:C3026_09605; -. DR PATRIC; fig|1411691.4.peg.582; -. DR EchoBASE; EB0797; -. DR eggNOG; COG0469; Bacteria. DR HOGENOM; CLU_015439_0_0_6; -. DR InParanoid; P0AD61; -. DR OMA; HQGRYDR; -. DR OrthoDB; 9812123at2; -. DR PhylomeDB; P0AD61; -. DR BioCyc; EcoCyc:PKI-MONOMER; -. DR BioCyc; MetaCyc:PKI-MONOMER; -. DR SABIO-RK; P0AD61; -. DR UniPathway; UPA00109; UER00188. DR EvolutionaryTrace; P0AD61; -. DR PRO; PR:P0AD61; -. DR Proteomes; UP000000625; Chromosome. DR AbasyAtlas; P0AD61; -. DR GO; GO:0005829; C:cytosol; IDA:EcoCyc. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:1902912; C:pyruvate kinase complex; IDA:EcoCyc. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro. DR GO; GO:0030955; F:potassium ion binding; IEA:InterPro. DR GO; GO:0004743; F:pyruvate kinase activity; IDA:EcoCyc. DR GO; GO:0006096; P:glycolytic process; EXP:EcoCyc. DR GO; GO:0009408; P:response to heat; IMP:EcoCyc. DR CDD; cd00288; Pyruvate_Kinase; 1. DR FunFam; 2.40.33.10:FF:000001; Pyruvate kinase; 1. DR FunFam; 3.20.20.60:FF:000001; Pyruvate kinase; 1. DR FunFam; 3.40.1380.20:FF:000003; Pyruvate kinase; 1. DR Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1. DR Gene3D; 2.40.33.10; PK beta-barrel domain-like; 1. DR Gene3D; 3.40.1380.20; Pyruvate kinase, C-terminal domain; 1. DR InterPro; IPR001697; Pyr_Knase. DR InterPro; IPR015813; Pyrv/PenolPyrv_kinase-like_dom. DR InterPro; IPR040442; Pyrv_kinase-like_dom_sf. DR InterPro; IPR011037; Pyrv_Knase-like_insert_dom_sf. DR InterPro; IPR018209; Pyrv_Knase_AS. DR InterPro; IPR015793; Pyrv_Knase_brl. DR InterPro; IPR015795; Pyrv_Knase_C. DR InterPro; IPR036918; Pyrv_Knase_C_sf. DR InterPro; IPR015806; Pyrv_Knase_insert_dom_sf. DR NCBIfam; NF004491; PRK05826.1; 1. DR NCBIfam; NF004978; PRK06354.1; 1. DR NCBIfam; NF006664; PRK09206.1; 1. DR NCBIfam; TIGR01064; pyruv_kin; 1. DR PANTHER; PTHR11817; PYRUVATE KINASE; 1. DR Pfam; PF00224; PK; 1. DR Pfam; PF02887; PK_C; 1. DR PRINTS; PR01050; PYRUVTKNASE. DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1. DR SUPFAM; SSF50800; PK beta-barrel domain-like; 1. DR SUPFAM; SSF52935; PK C-terminal domain-like; 1. DR PROSITE; PS00110; PYRUVATE_KINASE; 1. DR PDBsum; 1E0T; -. DR PDBsum; 1E0U; -. DR PDBsum; 1PKY; -. DR PDBsum; 4YNG; -. DR PDBsum; 8EDQ; -. DR PDBsum; 8EDR; -. DR PDBsum; 8EDS; -. DR PDBsum; 8EDT; -. DR PDBsum; 8EQ0; -. DR PDBsum; 8EQ1; -. DR PDBsum; 8EQ3; -. DR PDBsum; 8EU4; -. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Allosteric enzyme; ATP-binding; KW Direct protein sequencing; Glycolysis; Kinase; Magnesium; Metal-binding; KW Nucleotide-binding; Potassium; Pyruvate; Reference proteome; Transferase. FT CHAIN 1..470 FT /note="Pyruvate kinase I" FT /id="PRO_0000112069" FT BINDING 32 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P30613" FT BINDING 34..37 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P14618" FT BINDING 34 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /evidence="ECO:0000250|UniProtKB:P30613" FT BINDING 36 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /evidence="ECO:0000250|UniProtKB:P30613" FT BINDING 66 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /evidence="ECO:0000250|UniProtKB:P30613" FT BINDING 67 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /evidence="ECO:0000250|UniProtKB:P30613" FT BINDING 73 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P14618" FT BINDING 156 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P14618" FT BINDING 220 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P30613" FT BINDING 222 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:P30613" FT BINDING 245 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P30613" FT BINDING 246 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:P30613" FT BINDING 246 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P30613" FT BINDING 278 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P30613" FT SITE 220 FT /note="Transition state stabilizer" FT /evidence="ECO:0000250|UniProtKB:P00549" FT MOD_RES 76 FT /note="N6-acetyllysine" FT /evidence="ECO:0000269|PubMed:18723842" FT MOD_RES 319 FT /note="N6-acetyllysine" FT /evidence="ECO:0000269|PubMed:18723842" FT MOD_RES 382 FT /note="N6-lactoyllysine" FT /evidence="ECO:0000269|PubMed:36333310" FT MUTAGEN 271 FT /note="R->L: Loss of an interdomain salt bridge, FT stablilizes the inactive T-state." FT /evidence="ECO:0000269|PubMed:10751408" FT MUTAGEN 292 FT /note="R->D: Inactive, crystallizes in the inactive form." FT /evidence="ECO:0000269|PubMed:10751408" FT MUTAGEN 297 FT /note="D->R: Inactive." FT /evidence="ECO:0000269|PubMed:10751408" FT MUTAGEN 382 FT /note="K->Q: Significant loss of activation by fructose FT 1,6-bisphosphate, retains sigmoidal kinetics. Shows lower FT PK-1 activity and slower growth." FT /evidence="ECO:0000269|PubMed:10751408, FT ECO:0000269|PubMed:36333310" FT MUTAGEN 382 FT /note="K->R: Shows high PK-1 activity and faster growth." FT /evidence="ECO:0000269|PubMed:36333310" FT MUTAGEN 413 FT /note="K->Q: Partial activation of enzyme, loss of FT cooperativity in fructose 1,6-bisphosphate binding." FT /evidence="ECO:0000269|PubMed:10751408" FT MUTAGEN 431 FT /note="R->E: Partial activation." FT /evidence="ECO:0000269|PubMed:10751408" FT CONFLICT 44 FT /note="G -> S (in Ref. 6; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 379 FT /note="Q -> N (in Ref. 8; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 401 FT /note="T -> D (in Ref. 8; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 451..470 FT /note="MVSGALVPSGTTNTASVHVL -> YGFWCTGTERHY (in Ref. 1; FT AAA24392)" FT /evidence="ECO:0000305" FT STRAND 4..9 FT /evidence="ECO:0007829|PDB:1E0T" FT HELIX 12..14 FT /evidence="ECO:0007829|PDB:1E0T" FT HELIX 17..26 FT /evidence="ECO:0007829|PDB:1E0T" FT STRAND 28..34 FT /evidence="ECO:0007829|PDB:1E0T" FT HELIX 40..57 FT /evidence="ECO:0007829|PDB:1E0T" FT STRAND 62..66 FT /evidence="ECO:0007829|PDB:1E0T" FT STRAND 72..74 FT /evidence="ECO:0007829|PDB:1E0T" FT HELIX 78..80 FT /evidence="ECO:0007829|PDB:1E0T" FT STRAND 83..85 FT /evidence="ECO:0007829|PDB:1E0T" FT STRAND 90..95 FT /evidence="ECO:0007829|PDB:1E0T" FT STRAND 105..109 FT /evidence="ECO:0007829|PDB:1E0T" FT HELIX 113..116 FT /evidence="ECO:0007829|PDB:1E0T" FT STRAND 122..125 FT /evidence="ECO:0007829|PDB:1E0T" FT TURN 126..129 FT /evidence="ECO:0007829|PDB:1E0T" FT STRAND 130..138 FT /evidence="ECO:0007829|PDB:1E0T" FT STRAND 141..146 FT /evidence="ECO:0007829|PDB:1E0T" FT STRAND 150..152 FT /evidence="ECO:0007829|PDB:1E0T" FT STRAND 157..159 FT /evidence="ECO:0007829|PDB:1E0T" FT HELIX 163..165 FT /evidence="ECO:0007829|PDB:8EQ0" FT HELIX 172..184 FT /evidence="ECO:0007829|PDB:1E0T" FT STRAND 187..193 FT /evidence="ECO:0007829|PDB:1E0T" FT HELIX 197..208 FT /evidence="ECO:0007829|PDB:1E0T" FT TURN 209..211 FT /evidence="ECO:0007829|PDB:1E0T" FT STRAND 216..221 FT /evidence="ECO:0007829|PDB:1E0T" FT HELIX 224..228 FT /evidence="ECO:0007829|PDB:1E0T" FT HELIX 230..236 FT /evidence="ECO:0007829|PDB:1E0T" FT STRAND 237..243 FT /evidence="ECO:0007829|PDB:1E0T" FT HELIX 244..250 FT /evidence="ECO:0007829|PDB:1E0T" FT HELIX 253..270 FT /evidence="ECO:0007829|PDB:1E0T" FT STRAND 273..277 FT /evidence="ECO:0007829|PDB:1E0T" FT STRAND 278..281 FT /evidence="ECO:0007829|PDB:1PKY" FT HELIX 282..285 FT /evidence="ECO:0007829|PDB:8EQ3" FT HELIX 292..304 FT /evidence="ECO:0007829|PDB:1E0T" FT STRAND 307..311 FT /evidence="ECO:0007829|PDB:1E0T" FT HELIX 313..316 FT /evidence="ECO:0007829|PDB:8EQ3" FT HELIX 322..336 FT /evidence="ECO:0007829|PDB:1E0T" FT HELIX 351..353 FT /evidence="ECO:0007829|PDB:8EQ3" FT HELIX 355..368 FT /evidence="ECO:0007829|PDB:1E0T" FT STRAND 372..377 FT /evidence="ECO:0007829|PDB:1E0T" FT STRAND 379..381 FT /evidence="ECO:0007829|PDB:1E0T" FT HELIX 382..388 FT /evidence="ECO:0007829|PDB:1E0T" FT STRAND 393..401 FT /evidence="ECO:0007829|PDB:1E0T" FT HELIX 403..408 FT /evidence="ECO:0007829|PDB:1E0T" FT HELIX 409..411 FT /evidence="ECO:0007829|PDB:1E0T" FT STRAND 415..419 FT /evidence="ECO:0007829|PDB:1E0T" FT HELIX 426..439 FT /evidence="ECO:0007829|PDB:1E0T" FT STRAND 441..443 FT /evidence="ECO:0007829|PDB:1E0T" FT STRAND 448..453 FT /evidence="ECO:0007829|PDB:1E0T" FT STRAND 455..457 FT /evidence="ECO:0007829|PDB:1E0T" FT STRAND 464..469 FT /evidence="ECO:0007829|PDB:1E0T" SQ SEQUENCE 470 AA; 50729 MW; E29BF01B90327D8B CRC64; MKKTKIVCTI GPKTESEEML AKMLDAGMNV MRLNFSHGDY AEHGQRIQNL RNVMSKTGKT AAILLDTKGP EIRTMKLEGG NDVSLKAGQT FTFTTDKSVI GNSEMVAVTY EGFTTDLSVG NTVLVDDGLI GMEVTAIEGN KVICKVLNNG DLGENKGVNL PGVSIALPAL AEKDKQDLIF GCEQGVDFVA ASFIRKRSDV IEIREHLKAH GGENIHIISK IENQEGLNNF DEILEASDGI MVARGDLGVE IPVEEVIFAQ KMMIEKCIRA RKVVITATQM LDSMIKNPRP TRAEAGDVAN AILDGTDAVM LSGESAKGKY PLEAVSIMAT ICERTDRVMN SRLEFNNDNR KLRITEAVCR GAVETAEKLD APLIVVATQG GKSARAVRKY FPDATILALT TNEKTAHQLV LSKGVVPQLV KEITSTDDFY RLGKELALQS GLAHKGDVVV MVSGALVPSG TTNTASVHVL //