TKT1_ECOLI
ID TKT1_ECOLI Reviewed; 663 AA.
AC P27302; Q2M9Q8; Q6BF59;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 5.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Transketolase 1;
DE Short=TK 1;
DE EC=2.2.1.1 {ECO:0000269|PubMed:17914867, ECO:0000269|PubMed:7607225};
GN Name=tktA; Synonyms=tkt; OrderedLocusNames=b2935, JW5478;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=8241274; DOI=10.1016/0167-4781(93)90161-6;
RA Sprenger G.A.;
RT "Nucleotide sequence of the Escherichia coli K-12 transketolase (tkt)
RT gene.";
RL Biochim. Biophys. Acta 1216:307-310(1993).
RN [2]
RP SEQUENCE REVISION TO 632-633.
RA Sprenger G.A.;
RL Submitted (JUN-1993) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
RP SEQUENCE REVISION TO 584.
RX PubMed=16397293; DOI=10.1093/nar/gkj405;
RA Riley M., Abe T., Arnaud M.B., Berlyn M.K.B., Blattner F.R.,
RA Chaudhuri R.R., Glasner J.D., Horiuchi T., Keseler I.M., Kosuge T.,
RA Mori H., Perna N.T., Plunkett G. III, Rudd K.E., Serres M.H., Thomas G.H.,
RA Thomson N.R., Wishart D., Wanner B.L.;
RT "Escherichia coli K-12: a cooperatively developed annotation snapshot
RT -- 2005.";
RL Nucleic Acids Res. 34:1-9(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-27.
RX PubMed=2153656; DOI=10.1128/jb.172.2.538-547.1990;
RA Szumanski M.B.W., Boyle S.M.;
RT "Analysis and sequence of the speB gene encoding agmatine ureohydrolase, a
RT putrescine biosynthetic enzyme in Escherichia coli.";
RL J. Bacteriol. 172:538-547(1990).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-46, AND IDENTIFICATION BY MASS
RP 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 [8]
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND COFACTOR.
RX PubMed=7607225; DOI=10.1111/j.1432-1033.1995.0525h.x;
RA Sprenger G.A., Schorken U., Sprenger G., Sahm H.;
RT "Transketolase A of Escherichia coli K12. Purification and properties of
RT the enzyme from recombinant strains.";
RL Eur. J. Biochem. 230:525-532(1995).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 2-663 IN COMPLEX WITH CALCIUM AND
RP THIAMINE PYROPHOSPHATE.
RA Isupov M.N., Rupprecht M.P., Wilson K.S., Dauter Z., Littlechild J.A.;
RT "Crystal structure of Escherichia coli transketolase.";
RL Submitted (APR-1999) to the PDB data bank.
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.47 ANGSTROMS) IN COMPLEXES WITH SUBSTRATES;
RP CALCIUM AND THIAMINE PYROPHOSPHATE, CATALYTIC ACTIVITY, FUNCTION, COFACTOR,
RP SUBUNIT, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17914867; DOI=10.1021/bi700844m;
RA Asztalos P., Parthier C., Golbik R., Kleinschmidt M., Hubner G.,
RA Weiss M.S., Friedemann R., Wille G., Tittmann K.;
RT "Strain and near attack conformers in enzymic thiamin catalysis: X-ray
RT crystallographic snapshots of bacterial transketolase in covalent complex
RT with donor ketoses xylulose 5-phosphate and fructose 6-phosphate, and in
RT noncovalent complex with acceptor aldose ribose 5-phosphate.";
RL Biochemistry 46:12037-12052(2007).
CC -!- FUNCTION: Catalyzes the transfer of a two-carbon ketol group from a
CC ketose donor to an aldose acceptor, via a covalent intermediate with
CC the cofactor thiamine pyrophosphate. Thus, catalyzes the reversible
CC transfer of a two-carbon ketol group from sedoheptulose-7-phosphate to
CC glyceraldehyde-3-phosphate, producing xylulose-5-phosphate and ribose-
CC 5-phosphate. {ECO:0000269|PubMed:17914867, ECO:0000269|PubMed:7607225}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glyceraldehyde 3-phosphate + D-sedoheptulose 7-phosphate =
CC aldehydo-D-ribose 5-phosphate + D-xylulose 5-phosphate;
CC Xref=Rhea:RHEA:10508, ChEBI:CHEBI:57483, ChEBI:CHEBI:57737,
CC ChEBI:CHEBI:58273, ChEBI:CHEBI:59776; EC=2.2.1.1;
CC Evidence={ECO:0000269|PubMed:17914867, ECO:0000269|PubMed:7607225};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:7607225};
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:7607225};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:7607225};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000269|PubMed:7607225};
CC Note=Binds 1 Mg(2+) ion per subunit. Can also utilize other divalent
CC metal cations, such as Ca(2+), Mn(2+) and Co(2+).
CC {ECO:0000269|PubMed:7607225};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000269|PubMed:7607225};
CC Note=Binds 1 thiamine pyrophosphate per subunit. During the reaction,
CC the substrate forms a covalent intermediate with the cofactor.
CC {ECO:0000269|PubMed:17914867};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:17914867,
CC ECO:0000269|PubMed:7607225, ECO:0000269|Ref.9}.
CC -!- SIMILARITY: Belongs to the transketolase family. {ECO:0000305}.
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DR EMBL; X68025; CAA48166.1; -; Genomic_DNA.
DR EMBL; U28377; AAA69102.1; -; Genomic_DNA.
DR EMBL; U00096; AAT48155.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76998.1; -; Genomic_DNA.
DR EMBL; M32363; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; F65078; XJECTK.
DR RefSeq; WP_000098614.1; NZ_STEB01000001.1.
DR RefSeq; YP_026188.1; NC_000913.3.
DR PDB; 1QGD; X-ray; 1.90 A; A/B=2-663.
DR PDB; 2R5N; X-ray; 1.60 A; A/B=1-663.
DR PDB; 2R8O; X-ray; 1.47 A; A/B=1-663.
DR PDB; 2R8P; X-ray; 1.65 A; A/B=1-663.
DR PDB; 5HHT; X-ray; 1.50 A; A/B=1-663.
DR PDB; 6RJC; X-ray; 1.05 A; A/B=1-663.
DR PDB; 6TJ8; X-ray; 0.92 A; A/B=1-663.
DR PDB; 6TJ9; X-ray; 0.95 A; A/B=1-663.
DR PDBsum; 1QGD; -.
DR PDBsum; 2R5N; -.
DR PDBsum; 2R8O; -.
DR PDBsum; 2R8P; -.
DR PDBsum; 5HHT; -.
DR PDBsum; 6RJC; -.
DR PDBsum; 6TJ8; -.
DR PDBsum; 6TJ9; -.
DR AlphaFoldDB; P27302; -.
DR SMR; P27302; -.
DR BioGRID; 4260954; 9.
DR DIP; DIP-10998N; -.
DR IntAct; P27302; 1.
DR STRING; 511145.b2935; -.
DR DrugBank; DB01987; Cocarboxylase.
DR MoonProt; P27302; -.
DR iPTMnet; P27302; -.
DR jPOST; P27302; -.
DR PaxDb; P27302; -.
DR PRIDE; P27302; -.
DR EnsemblBacteria; AAT48155; AAT48155; b2935.
DR EnsemblBacteria; BAE76998; BAE76998; BAE76998.
DR GeneID; 58460601; -.
DR GeneID; 947420; -.
DR KEGG; ecj:JW5478; -.
DR KEGG; eco:b2935; -.
DR PATRIC; fig|1411691.4.peg.3798; -.
DR EchoBASE; EB1397; -.
DR eggNOG; COG0021; Bacteria.
DR HOGENOM; CLU_009227_0_0_6; -.
DR InParanoid; P27302; -.
DR OMA; HHTEGIE; -.
DR PhylomeDB; P27302; -.
DR BioCyc; EcoCyc:TRANSKETOI-MON; -.
DR BioCyc; MetaCyc:TRANSKETOI-MON; -.
DR BRENDA; 2.2.1.1; 2026.
DR SABIO-RK; P27302; -.
DR EvolutionaryTrace; P27302; -.
DR PRO; PR:P27302; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0000287; F:magnesium ion binding; IDA:EcoCyc.
DR GO; GO:0030145; F:manganese ion binding; IDA:EcoCyc.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IDA:EcoCyc.
DR GO; GO:0004802; F:transketolase activity; IDA:EcoCyc.
DR GO; GO:0006098; P:pentose-phosphate shunt; IBA:GO_Central.
DR GO; GO:0009052; P:pentose-phosphate shunt, non-oxidative branch; IMP:EcoCyc.
DR CDD; cd02012; TPP_TK; 1.
DR Gene3D; 3.40.50.920; -; 1.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR009014; Transketo_C/PFOR_II.
DR InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR InterPro; IPR005478; Transketolase_bac-like.
DR InterPro; IPR020826; Transketolase_BS.
DR InterPro; IPR033248; Transketolase_C.
DR InterPro; IPR033247; Transketolase_fam.
DR InterPro; IPR005474; Transketolase_N.
DR PANTHER; PTHR43522; PTHR43522; 1.
DR Pfam; PF02779; Transket_pyr; 1.
DR Pfam; PF02780; Transketolase_C; 1.
DR Pfam; PF00456; Transketolase_N; 1.
DR SMART; SM00861; Transket_pyr; 1.
DR SUPFAM; SSF52518; SSF52518; 2.
DR SUPFAM; SSF52922; SSF52922; 1.
DR TIGRFAMs; TIGR00232; tktlase_bact; 1.
DR PROSITE; PS00801; TRANSKETOLASE_1; 1.
DR PROSITE; PS00802; TRANSKETOLASE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Calcium; Magnesium; Metal-binding;
KW Reference proteome; Thiamine pyrophosphate; Transferase.
FT CHAIN 1..663
FT /note="Transketolase 1"
FT /id="PRO_0000191856"
FT ACT_SITE 411
FT /note="Proton donor"
FT /evidence="ECO:0000305"
FT BINDING 26
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:17914867"
FT BINDING 66
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000269|PubMed:17914867, ECO:0000269|Ref.9,
FT ECO:0007744|PDB:1QGD, ECO:0007744|PDB:2R5N"
FT BINDING 114..116
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000269|PubMed:17914867, ECO:0000269|Ref.9,
FT ECO:0007744|PDB:1QGD, ECO:0007744|PDB:2R5N"
FT BINDING 155
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000305|PubMed:17914867, ECO:0000305|Ref.9"
FT BINDING 156
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000269|Ref.9, ECO:0007744|PDB:1QGD"
FT BINDING 185
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000305|PubMed:17914867, ECO:0000305|Ref.9"
FT BINDING 185
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000269|PubMed:17914867, ECO:0000269|Ref.9,
FT ECO:0007744|PDB:1QGD, ECO:0007744|PDB:2R5N"
FT BINDING 187
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000305|PubMed:17914867, ECO:0000305|Ref.9"
FT BINDING 261
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:17914867"
FT BINDING 261
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000269|PubMed:17914867, ECO:0000269|Ref.9,
FT ECO:0007744|PDB:1QGD, ECO:0007744|PDB:2R5N"
FT BINDING 358
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:17914867"
FT BINDING 385
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:17914867"
FT BINDING 437
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000269|PubMed:17914867, ECO:0000269|Ref.9"
FT BINDING 461
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:17914867"
FT BINDING 469
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:17914867"
FT BINDING 473
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:17914867"
FT BINDING 520
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:17914867"
FT SITE 26
FT /note="Important for catalytic activity"
FT SITE 261
FT /note="Important for catalytic activity"
FT MOD_RES 46
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:18723842"
FT CONFLICT 103..107
FT /note="VGYTA -> SGVTPL (in Ref. 1; CAA48166)"
FT /evidence="ECO:0000305"
FT CONFLICT 584
FT /note="P -> S (in Ref. 1; CAA48166 and 3; AAA69102)"
FT /evidence="ECO:0000305"
FT HELIX 4..22
FT /evidence="ECO:0007829|PDB:6TJ8"
FT HELIX 28..43
FT /evidence="ECO:0007829|PDB:6TJ8"
FT STRAND 59..64
FT /evidence="ECO:0007829|PDB:6TJ8"
FT HELIX 65..67
FT /evidence="ECO:0007829|PDB:6TJ8"
FT HELIX 68..78
FT /evidence="ECO:0007829|PDB:6TJ8"
FT HELIX 84..87
FT /evidence="ECO:0007829|PDB:6TJ8"
FT TURN 88..91
FT /evidence="ECO:0007829|PDB:6TJ8"
FT TURN 103..105
FT /evidence="ECO:0007829|PDB:6TJ8"
FT HELIX 118..137
FT /evidence="ECO:0007829|PDB:6TJ8"
FT STRAND 149..153
FT /evidence="ECO:0007829|PDB:6TJ8"
FT HELIX 155..159
FT /evidence="ECO:0007829|PDB:6TJ8"
FT HELIX 161..172
FT /evidence="ECO:0007829|PDB:6TJ8"
FT STRAND 178..184
FT /evidence="ECO:0007829|PDB:6TJ8"
FT STRAND 186..188
FT /evidence="ECO:0007829|PDB:6TJ8"
FT HELIX 193..195
FT /evidence="ECO:0007829|PDB:6TJ8"
FT HELIX 201..207
FT /evidence="ECO:0007829|PDB:6TJ8"
FT STRAND 211..217
FT /evidence="ECO:0007829|PDB:6TJ8"
FT HELIX 221..233
FT /evidence="ECO:0007829|PDB:6TJ8"
FT STRAND 239..244
FT /evidence="ECO:0007829|PDB:6TJ8"
FT TURN 247..250
FT /evidence="ECO:0007829|PDB:6TJ8"
FT TURN 252..256
FT /evidence="ECO:0007829|PDB:6TJ8"
FT HELIX 258..260
FT /evidence="ECO:0007829|PDB:6TJ8"
FT STRAND 261..263
FT /evidence="ECO:0007829|PDB:6TJ9"
FT HELIX 267..277
FT /evidence="ECO:0007829|PDB:6TJ8"
FT HELIX 288..294
FT /evidence="ECO:0007829|PDB:6TJ8"
FT HELIX 297..317
FT /evidence="ECO:0007829|PDB:6TJ8"
FT HELIX 319..330
FT /evidence="ECO:0007829|PDB:6TJ8"
FT HELIX 337..350
FT /evidence="ECO:0007829|PDB:6TJ8"
FT HELIX 357..368
FT /evidence="ECO:0007829|PDB:6TJ8"
FT TURN 369..371
FT /evidence="ECO:0007829|PDB:6TJ8"
FT STRAND 375..381
FT /evidence="ECO:0007829|PDB:6TJ8"
FT HELIX 383..386
FT /evidence="ECO:0007829|PDB:6TJ8"
FT TURN 396..398
FT /evidence="ECO:0007829|PDB:6TJ8"
FT STRAND 403..406
FT /evidence="ECO:0007829|PDB:6TJ8"
FT HELIX 411..424
FT /evidence="ECO:0007829|PDB:6TJ8"
FT STRAND 428..434
FT /evidence="ECO:0007829|PDB:6TJ8"
FT HELIX 435..439
FT /evidence="ECO:0007829|PDB:6TJ8"
FT HELIX 442..450
FT /evidence="ECO:0007829|PDB:6TJ8"
FT STRAND 456..460
FT /evidence="ECO:0007829|PDB:6TJ8"
FT HELIX 464..466
FT /evidence="ECO:0007829|PDB:6TJ8"
FT TURN 471..473
FT /evidence="ECO:0007829|PDB:6TJ8"
FT HELIX 478..483
FT /evidence="ECO:0007829|PDB:6TJ8"
FT STRAND 489..491
FT /evidence="ECO:0007829|PDB:6TJ8"
FT HELIX 496..508
FT /evidence="ECO:0007829|PDB:6TJ8"
FT STRAND 510..512
FT /evidence="ECO:0007829|PDB:6TJ8"
FT STRAND 514..518
FT /evidence="ECO:0007829|PDB:6TJ8"
FT STRAND 520..523
FT /evidence="ECO:0007829|PDB:6TJ8"
FT HELIX 530..535
FT /evidence="ECO:0007829|PDB:6TJ8"
FT HELIX 536..538
FT /evidence="ECO:0007829|PDB:6TJ8"
FT STRAND 541..544
FT /evidence="ECO:0007829|PDB:6TJ8"
FT STRAND 547..549
FT /evidence="ECO:0007829|PDB:6TJ8"
FT STRAND 551..556
FT /evidence="ECO:0007829|PDB:6TJ8"
FT HELIX 558..560
FT /evidence="ECO:0007829|PDB:6TJ8"
FT HELIX 561..574
FT /evidence="ECO:0007829|PDB:6TJ8"
FT STRAND 578..582
FT /evidence="ECO:0007829|PDB:6TJ8"
FT HELIX 586..590
FT /evidence="ECO:0007829|PDB:6TJ8"
FT HELIX 594..600
FT /evidence="ECO:0007829|PDB:6TJ8"
FT STRAND 608..615
FT /evidence="ECO:0007829|PDB:6TJ8"
FT HELIX 616..619
FT /evidence="ECO:0007829|PDB:6TJ8"
FT HELIX 620..623
FT /evidence="ECO:0007829|PDB:6TJ8"
FT STRAND 626..632
FT /evidence="ECO:0007829|PDB:6TJ8"
FT HELIX 641..647
FT /evidence="ECO:0007829|PDB:6TJ8"
FT HELIX 652..663
FT /evidence="ECO:0007829|PDB:6TJ8"
SQ SEQUENCE 663 AA; 72212 MW; FE6D624ADD11939A CRC64;
MSSRKELANA IRALSMDAVQ KAKSGHPGAP MGMADIAEVL WRDFLKHNPQ NPSWADRDRF
VLSNGHGSML IYSLLHLTGY DLPMEELKNF RQLHSKTPGH PEVGYTAGVE TTTGPLGQGI
ANAVGMAIAE KTLAAQFNRP GHDIVDHYTY AFMGDGCMME GISHEVCSLA GTLKLGKLIA
FYDDNGISID GHVEGWFTDD TAMRFEAYGW HVIRDIDGHD AASIKRAVEE ARAVTDKPSL
LMCKTIIGFG SPNKAGTHDS HGAPLGDAEI ALTREQLGWK YAPFEIPSEI YAQWDAKEAG
QAKESAWNEK FAAYAKAYPQ EAAEFTRRMK GEMPSDFDAK AKEFIAKLQA NPAKIASRKA
SQNAIEAFGP LLPEFLGGSA DLAPSNLTLW SGSKAINEDA AGNYIHYGVR EFGMTAIANG
ISLHGGFLPY TSTFLMFVEY ARNAVRMAAL MKQRQVMVYT HDSIGLGEDG PTHQPVEQVA
SLRVTPNMST WRPCDQVESA VAWKYGVERQ DGPTALILSR QNLAQQERTE EQLANIARGG
YVLKDCAGQP ELIFIATGSE VELAVAAYEK LTAEGVKARV VSMPSTDAFD KQDAAYRESV
LPKAVTARVA VEAGIADYWY KYVGLNGAIV GMTTFGESAP AELLFEEFGF TVDNVVAKAK
ELL
