KPYK1_ECOLI
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 03-AUG-2022, entry version 142.
DE RecName: Full=Pyruvate kinase I;
DE EC=2.7.1.40 {ECO:0000269|PubMed:7011316};
DE AltName: Full=PK-1;
GN Name=pykF; OrderedLocusNames=b1676, JW1666;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC 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] {ECO:0007744|PDB:1PKY}
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF THE INACTIVE T-STATE, FUNCTION,
RP 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 [13] {ECO:0007744|PDB:1E0T, ECO:0007744|PDB:1E0U}
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF MUTANT ENZYMES, FUNCTION, SUBUNIT,
RP AND MUTAGENESIS OF ARG-271; ARG-292; ASP-297; 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 [14] {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:0000305|PubMed:8591049}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + pyruvate = ADP + H(+) + phosphoenolpyruvate;
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 -!- SIMILARITY: Belongs to the pyruvate kinase family. {ECO:0000305}.
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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_STEB01000003.1.
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 PDBsum; 1E0T; -.
DR PDBsum; 1E0U; -.
DR PDBsum; 1PKY; -.
DR PDBsum; 4YNG; -.
DR AlphaFoldDB; P0AD61; -.
DR SMR; P0AD61; -.
DR BioGRID; 4260275; 36.
DR DIP; DIP-36221N; -.
DR IntAct; P0AD61; 21.
DR STRING; 511145.b1676; -.
DR iPTMnet; P0AD61; -.
DR SWISS-2DPAGE; P0AD61; -.
DR jPOST; P0AD61; -.
DR PaxDb; P0AD61; -.
DR PRIDE; P0AD61; -.
DR EnsemblBacteria; AAC74746; AAC74746; b1676.
DR EnsemblBacteria; BAA15445; BAA15445; BAA15445.
DR GeneID; 66674431; -.
DR GeneID; 946179; -.
DR KEGG; ecj:JW1666; -.
DR KEGG; eco:b1676; -.
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; MVRVHHL; -.
DR PhylomeDB; P0AD61; -.
DR BioCyc; EcoCyc:PKI-MON; -.
DR BioCyc; MetaCyc:PKI-MON; -.
DR SABIO-RK; P0AD61; -.
DR UniPathway; UPA00109; UER00188.
DR EvolutionaryTrace; P0AD61; -.
DR PRO; PR:P0AD61; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
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; IBA:GO_Central.
DR GO; GO:0009408; P:response to heat; IMP:EcoCyc.
DR CDD; cd00288; Pyruvate_Kinase; 1.
DR Gene3D; 2.40.33.10; -; 1.
DR Gene3D; 3.20.20.60; -; 1.
DR Gene3D; 3.40.1380.20; -; 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 PANTHER; PTHR11817; PTHR11817; 1.
DR Pfam; PF00224; PK; 1.
DR Pfam; PF02887; PK_C; 1.
DR PRINTS; PR01050; PYRUVTKNASE.
DR SUPFAM; SSF50800; SSF50800; 1.
DR SUPFAM; SSF51621; SSF51621; 1.
DR SUPFAM; SSF52935; SSF52935; 1.
DR TIGRFAMs; TIGR01064; pyruv_kin; 1.
DR PROSITE; PS00110; PYRUVATE_KINASE; 1.
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 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."
FT /evidence="ECO:0000269|PubMed:10751408"
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 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:1PKY"
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:1PKY"
FT HELIX 322..336
FT /evidence="ECO:0007829|PDB:1E0T"
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
