ID PFLB_ECOLI Reviewed; 760 AA. AC P09373; P76826; Q47478; DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 27-MAR-2024, entry version 208. DE RecName: Full=Formate acetyltransferase 1; DE EC=2.3.1.54 {ECO:0000269|PubMed:4615902}; DE AltName: Full=Pyruvate formate-lyase 1; GN Name=pflB; Synonyms=pfl; OrderedLocusNames=b0903, JW0886; OS Escherichia coli (strain K12). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83333; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE. RC STRAIN=K12; RX PubMed=3053170; DOI=10.1111/j.1432-1033.1988.tb14356.x; RA Roedel W., Plaga W., Frank R., Knappe J.; RT "Primary structures of Escherichia coli pyruvate formate-lyase and RT pyruvate-formate-lyase-activating enzyme deduced from the DNA nucleotide RT sequences."; RL Eur. J. Biochem. 177:153-158(1988). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=8905232; DOI=10.1093/dnares/3.3.137; RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H., RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G., RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M., RA Horiuchi T.; RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to RT the 12.7-28.0 min region on the linkage map."; RL DNA Res. 3:137-155(1996). 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 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 [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-13. RX PubMed=2651404; DOI=10.1128/jb.171.5.2485-2498.1989; RA Sawers G., Boeck A.; RT "Novel transcriptional control of the pyruvate formate-lyase gene: upstream RT regulatory sequences and multiple promoters regulate anaerobic RT expression."; RL J. Bacteriol. 171:2485-2498(1989). RN [6] RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=4615902; DOI=10.1111/j.1432-1033.1974.tb03894.x; RA Knappe J., Blaschkowski H.P., Groebner P., Schmitt T.; RT "Pyruvate formate-lyase of Escherichia coli: the acetyl-enzyme RT intermediate."; RL Eur. J. Biochem. 50:253-263(1974). RN [7] RP ORGANIC RADICAL AT GLY-420. RX PubMed=1310545; DOI=10.1073/pnas.89.3.996; RA Wagner A.F.V., Frey M., Neugebauer F.A., Schaefer W., Knappe J.; RT "The free radical in pyruvate formate-lyase is located on glycine-734."; RL Proc. Natl. Acad. Sci. U.S.A. 89:996-1000(1992). RN [8] RP PROTEIN SEQUENCE OF 2-6. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=9629924; DOI=10.1002/elps.1150190539; RA Molloy M.P., Herbert B.R., Walsh B.J., Tyler M.I., Traini M., RA Sanchez J.-C., Hochstrasser D.F., Williams K.L., Gooley A.A.; RT "Extraction of membrane proteins by differential solubilization for RT separation using two-dimensional gel electrophoresis."; RL Electrophoresis 19:837-844(1998). RN [9] 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 [10] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-63; LYS-117; LYS-195; LYS-454; RP LYS-541 AND LYS-591, AND 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 [11] RP SUCCINYLATION AT LYS-63; LYS-107; LYS-117; LYS-124; LYS-195; LYS-454; RP LYS-467 AND LYS-654. RC STRAIN=K12; RX PubMed=21151122; DOI=10.1038/nchembio.495; RA Zhang Z., Tan M., Xie Z., Dai L., Chen Y., Zhao Y.; RT "Identification of lysine succinylation as a new post-translational RT modification."; RL Nat. Chem. Biol. 7:58-63(2011). RN [12] RP FUNCTION IN FOCA REGULATION, AND INTERACTION WITH FOCA. RX PubMed=24887098; DOI=10.1016/j.jmb.2014.05.023; RA Doberenz C., Zorn M., Falke D., Nannemann D., Hunger D., Beyer L., RA Ihling C.H., Meiler J., Sinz A., Sawers R.G.; RT "Pyruvate formate-lyase interacts directly with the formate channel FocA to RT regulate formate translocation."; RL J. Mol. Biol. 426:2827-2839(2014). RN [13] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS), AND SUBUNIT. RX PubMed=10504733; DOI=10.1038/13341; RA Becker A., Fritz-Wolf K., Kabsch W., Knappe J., Schultz S., Wagner A.F.V.; RT "Structure and mechanism of the glycyl radical enzyme pyruvate formate- RT lyase."; RL Nat. Struct. Biol. 6:969-975(1999). CC -!- FUNCTION: Catalyzes the conversion of pyruvate to formate and acetyl- CC CoA (PubMed:4615902). In addition, may be involved in the control of CC the activity of the formate channel FocA, via direct interaction with CC FocA (PubMed:24887098). {ECO:0000269|PubMed:24887098, CC ECO:0000269|PubMed:4615902}. CC -!- CATALYTIC ACTIVITY: CC Reaction=acetyl-CoA + formate = CoA + pyruvate; Xref=Rhea:RHEA:11844, CC ChEBI:CHEBI:15361, ChEBI:CHEBI:15740, ChEBI:CHEBI:57287, CC ChEBI:CHEBI:57288; EC=2.3.1.54; CC Evidence={ECO:0000269|PubMed:4615902}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=2.05 mM for pyruvate (at pH 8.1 and 30 degrees Celsius) CC {ECO:0000269|PubMed:4615902}; CC KM=0.0068 mM for CoA (at pH 8.1 and 30 degrees Celsius) CC {ECO:0000269|PubMed:4615902}; CC KM=24.5 mM for formate (at pH 8.1 and 30 degrees Celsius) CC {ECO:0000269|PubMed:4615902}; CC KM=0.051 mM for acetyl-CoA (at pH 8.1 and 30 degrees Celsius) CC {ECO:0000269|PubMed:4615902}; CC Note=kcat is 1100 sec(-1) with pyruvate and CoA as substrates. kcat CC is 380 sec(-1) with formate and acetyl-CoA as substrates. CC {ECO:0000269|PubMed:4615902}; CC -!- PATHWAY: Fermentation; pyruvate fermentation; formate from pyruvate: CC step 1/1. CC -!- SUBUNIT: Homodimer (PubMed:10504733). Interacts specifically with FocA CC (PubMed:24887098). {ECO:0000269|PubMed:10504733, CC ECO:0000269|PubMed:24887098}. CC -!- INTERACTION: CC P09373; P15082: srlR; NbExp=3; IntAct=EBI-546682, EBI-558448; CC P09373; P0A858: tpiA; NbExp=7; IntAct=EBI-546682, EBI-368978; CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- INDUCTION: By pfl-activating enzyme under anaerobic conditions by CC generation of an organic free radical. Exposure of activated pfl to CC oxygen resulted in cleavage at the glycine residue harboring its CC organic radical with loss of the 25 C-terminal AA. CC -!- MISCELLANEOUS: Several mechanisms have been proposed based on complexes CC formed with substrate analogs. After activation by the glycine radical, CC the cysteine radical, Cys-420, can abstract hydrogen atoms from the CC other active site cysteine, Cys-419, and from coenzyme A, and it can CC also transfer hydrogen atoms to product radicals. The other active site CC cysteine can attack the central carbonyl of pyruvate and covalently CC bind the product acetyl group. CC -!- SIMILARITY: Belongs to the glycyl radical enzyme (GRE) family. PFL CC subfamily. {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; X08035; CAA30828.1; -; Genomic_DNA. DR EMBL; U00096; AAC73989.1; -; Genomic_DNA. DR EMBL; AP009048; BAA35638.1; -; Genomic_DNA. DR EMBL; M26413; AAA20391.1; -; Genomic_DNA. DR PIR; S01788; S01788. DR RefSeq; NP_415423.1; NC_000913.3. DR RefSeq; WP_001292822.1; NZ_SSZK01000002.1. DR PDB; 1CM5; X-ray; 2.30 A; A/B=2-760. DR PDB; 1H16; X-ray; 1.53 A; A=2-760. DR PDB; 1H17; X-ray; 1.75 A; A=2-760. DR PDB; 1H18; X-ray; 2.30 A; A/B=2-760. DR PDB; 1MZO; X-ray; 2.70 A; A/B=2-760. DR PDB; 1QHM; X-ray; 2.80 A; A/B=2-625. DR PDB; 2PFL; X-ray; 2.90 A; A/B=2-760. DR PDB; 3PFL; X-ray; 2.60 A; A/B=2-760. DR PDBsum; 1CM5; -. DR PDBsum; 1H16; -. DR PDBsum; 1H17; -. DR PDBsum; 1H18; -. DR PDBsum; 1MZO; -. DR PDBsum; 1QHM; -. DR PDBsum; 2PFL; -. DR PDBsum; 3PFL; -. DR AlphaFoldDB; P09373; -. DR SMR; P09373; -. DR BioGRID; 4260835; 7. DR BioGRID; 849888; 3. DR DIP; DIP-10467N; -. DR IntAct; P09373; 45. DR STRING; 511145.b0903; -. DR DrugBank; DB01992; Coenzyme A. DR DrugBank; DB03278; D-Treitol. DR DrugBank; DB03940; Oxamic Acid. DR iPTMnet; P09373; -. DR jPOST; P09373; -. DR PaxDb; 511145-b0903; -. DR EnsemblBacteria; AAC73989; AAC73989; b0903. DR GeneID; 83577159; -. DR GeneID; 945514; -. DR KEGG; ecj:JW0886; -. DR KEGG; eco:b0903; -. DR PATRIC; fig|1411691.4.peg.1373; -. DR EchoBASE; EB0695; -. DR eggNOG; COG1882; Bacteria. DR HOGENOM; CLU_023898_0_0_6; -. DR InParanoid; P09373; -. DR OMA; DTAIACC; -. DR OrthoDB; 9803969at2; -. DR PhylomeDB; P09373; -. DR BioCyc; EcoCyc:PYRUVFORMLY-MONOMER; -. DR BioCyc; MetaCyc:PYRUVFORMLY-MONOMER; -. DR BRENDA; 2.3.1.54; 2026. DR UniPathway; UPA00920; UER00891. DR EvolutionaryTrace; P09373; -. DR PRO; PR:P09373; -. DR Proteomes; UP000000318; Chromosome. DR Proteomes; UP000000625; Chromosome. DR GO; GO:0005829; C:cytosol; IDA:EcoCyc. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0008861; F:formate C-acetyltransferase activity; IDA:EcoCyc. DR GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW. DR CDD; cd01678; PFL1; 1. DR Gene3D; 3.20.70.20; -; 1. DR InterPro; IPR005949; Form_AcTrfase. DR InterPro; IPR019777; Form_AcTrfase_GR_CS. DR InterPro; IPR001150; Gly_radical. DR InterPro; IPR004184; PFL_dom. DR NCBIfam; TIGR01255; pyr_form_ly_1; 1. DR PANTHER; PTHR30191; FORMATE ACETYLTRANSFERASE; 1. DR PANTHER; PTHR30191:SF0; FORMATE ACETYLTRANSFERASE 1; 1. DR Pfam; PF01228; Gly_radical; 1. DR Pfam; PF02901; PFL-like; 1. DR PIRSF; PIRSF000379; For_Ac_trans_1; 1. DR SUPFAM; SSF51998; PFL-like glycyl radical enzymes; 1. DR PROSITE; PS00850; GLY_RADICAL_1; 1. DR PROSITE; PS51149; GLY_RADICAL_2; 1. DR PROSITE; PS51554; PFL; 1. DR SWISS-2DPAGE; P09373; -. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Acyltransferase; Carbohydrate metabolism; KW Cytoplasm; Direct protein sequencing; Glucose metabolism; Organic radical; KW Reference proteome; Transferase. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:9629924" FT CHAIN 2..760 FT /note="Formate acetyltransferase 1" FT /id="PRO_0000166687" FT DOMAIN 3..625 FT /note="PFL" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00887" FT DOMAIN 632..760 FT /note="Glycine radical" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00493" FT ACT_SITE 419 FT /note="S-acetylcysteine intermediate" FT /evidence="ECO:0000269|PubMed:1310545" FT ACT_SITE 420 FT /note="Cysteine radical intermediate" FT /evidence="ECO:0000269|PubMed:1310545" FT MOD_RES 63 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000269|PubMed:18723842" FT MOD_RES 63 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000269|PubMed:21151122" FT MOD_RES 107 FT /note="N6-succinyllysine" FT /evidence="ECO:0000269|PubMed:21151122" FT MOD_RES 117 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000269|PubMed:18723842" FT MOD_RES 117 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000269|PubMed:21151122" FT MOD_RES 124 FT /note="N6-succinyllysine" FT /evidence="ECO:0000269|PubMed:21151122" FT MOD_RES 195 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000269|PubMed:18723842" FT MOD_RES 195 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000269|PubMed:21151122" FT MOD_RES 454 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000269|PubMed:18723842" FT MOD_RES 454 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000269|PubMed:21151122" FT MOD_RES 467 FT /note="N6-succinyllysine" FT /evidence="ECO:0000269|PubMed:21151122" FT MOD_RES 541 FT /note="N6-acetyllysine" FT /evidence="ECO:0000269|PubMed:18723842" FT MOD_RES 591 FT /note="N6-acetyllysine" FT /evidence="ECO:0000269|PubMed:18723842" FT MOD_RES 654 FT /note="N6-succinyllysine" FT /evidence="ECO:0000269|PubMed:21151122" FT MOD_RES 735 FT /note="Glycine radical" FT /evidence="ECO:0000269|PubMed:1310545" FT HELIX 6..11 FT /evidence="ECO:0007829|PDB:1H16" FT TURN 12..14 FT /evidence="ECO:0007829|PDB:1H16" FT HELIX 19..21 FT /evidence="ECO:0007829|PDB:1H16" FT HELIX 26..33 FT /evidence="ECO:0007829|PDB:1H16" FT HELIX 41..43 FT /evidence="ECO:0007829|PDB:1H16" FT HELIX 49..68 FT /evidence="ECO:0007829|PDB:1H16" FT STRAND 72..79 FT /evidence="ECO:0007829|PDB:1H16" FT STRAND 82..85 FT /evidence="ECO:0007829|PDB:1H16" FT TURN 92..94 FT /evidence="ECO:0007829|PDB:1H16" FT STRAND 101..104 FT /evidence="ECO:0007829|PDB:1H16" FT STRAND 107..110 FT /evidence="ECO:0007829|PDB:1H16" FT HELIX 112..114 FT /evidence="ECO:0007829|PDB:1H16" FT HELIX 117..125 FT /evidence="ECO:0007829|PDB:1H16" FT HELIX 132..140 FT /evidence="ECO:0007829|PDB:1H16" FT HELIX 145..152 FT /evidence="ECO:0007829|PDB:1H16" FT HELIX 155..162 FT /evidence="ECO:0007829|PDB:1H16" FT STRAND 164..167 FT /evidence="ECO:0007829|PDB:1QHM" FT STRAND 172..174 FT /evidence="ECO:0007829|PDB:1H16" FT HELIX 183..188 FT /evidence="ECO:0007829|PDB:1H16" FT HELIX 190..202 FT /evidence="ECO:0007829|PDB:1H16" FT HELIX 205..210 FT /evidence="ECO:0007829|PDB:1H16" FT TURN 211..213 FT /evidence="ECO:0007829|PDB:1H16" FT HELIX 214..240 FT /evidence="ECO:0007829|PDB:1H16" FT HELIX 252..269 FT /evidence="ECO:0007829|PDB:1H16" FT HELIX 281..293 FT /evidence="ECO:0007829|PDB:1H16" FT HELIX 299..313 FT /evidence="ECO:0007829|PDB:1H16" FT HELIX 322..327 FT /evidence="ECO:0007829|PDB:1H16" FT STRAND 336..340 FT /evidence="ECO:0007829|PDB:1H16" FT STRAND 346..348 FT /evidence="ECO:0007829|PDB:1CM5" FT HELIX 352..363 FT /evidence="ECO:0007829|PDB:1H16" FT STRAND 370..376 FT /evidence="ECO:0007829|PDB:1H16" FT HELIX 382..395 FT /evidence="ECO:0007829|PDB:1H16" FT STRAND 399..402 FT /evidence="ECO:0007829|PDB:1H16" FT HELIX 403..410 FT /evidence="ECO:0007829|PDB:1H16" FT STRAND 415..418 FT /evidence="ECO:0007829|PDB:1H16" FT TURN 419..421 FT /evidence="ECO:0007829|PDB:1H16" FT STRAND 422..425 FT /evidence="ECO:0007829|PDB:1H16" FT TURN 426..428 FT /evidence="ECO:0007829|PDB:1H16" FT STRAND 429..438 FT /evidence="ECO:0007829|PDB:1H16" FT HELIX 439..447 FT /evidence="ECO:0007829|PDB:1H16" FT TURN 448..450 FT /evidence="ECO:0007829|PDB:1H16" FT TURN 453..455 FT /evidence="ECO:0007829|PDB:1H16" FT STRAND 468..470 FT /evidence="ECO:0007829|PDB:1H16" FT HELIX 473..505 FT /evidence="ECO:0007829|PDB:1H16" FT HELIX 509..512 FT /evidence="ECO:0007829|PDB:1H16" FT STRAND 520..528 FT /evidence="ECO:0007829|PDB:1H16" FT HELIX 530..542 FT /evidence="ECO:0007829|PDB:1H16" FT STRAND 543..549 FT /evidence="ECO:0007829|PDB:1H16" FT STRAND 555..562 FT /evidence="ECO:0007829|PDB:1H16" FT STRAND 567..570 FT /evidence="ECO:0007829|PDB:1QHM" FT HELIX 572..590 FT /evidence="ECO:0007829|PDB:1H16" FT HELIX 595..597 FT /evidence="ECO:0007829|PDB:1H16" FT STRAND 599..604 FT /evidence="ECO:0007829|PDB:1H16" FT HELIX 609..615 FT /evidence="ECO:0007829|PDB:1H16" FT TURN 638..640 FT /evidence="ECO:0007829|PDB:1H17" FT HELIX 645..653 FT /evidence="ECO:0007829|PDB:1H16" FT HELIX 657..659 FT /evidence="ECO:0007829|PDB:1H16" FT STRAND 667..670 FT /evidence="ECO:0007829|PDB:1H16" FT HELIX 672..675 FT /evidence="ECO:0007829|PDB:1H16" FT HELIX 679..694 FT /evidence="ECO:0007829|PDB:1H16" FT STRAND 705..710 FT /evidence="ECO:0007829|PDB:1H16" FT HELIX 713..721 FT /evidence="ECO:0007829|PDB:1H16" FT HELIX 723..725 FT /evidence="ECO:0007829|PDB:1H16" FT STRAND 730..732 FT /evidence="ECO:0007829|PDB:1H16" FT STRAND 734..739 FT /evidence="ECO:0007829|PDB:1H16" FT HELIX 740..742 FT /evidence="ECO:0007829|PDB:1H16" FT HELIX 745..752 FT /evidence="ECO:0007829|PDB:1H16" SQ SEQUENCE 760 AA; 85357 MW; 19323C63081625D6 CRC64; MSELNEKLAT AWEGFTKGDW QNEVNVRDFI QKNYTPYEGD ESFLAGATEA TTTLWDKVME GVKLENRTHA PVDFDTAVAS TITSHDAGYI NKQLEKIVGL QTEAPLKRAL IPFGGIKMIE GSCKAYNREL DPMIKKIFTE YRKTHNQGVF DVYTPDILRC RKSGVLTGLP DAYGRGRIIG DYRRVALYGI DYLMKDKLAQ FTSLQADLEN GVNLEQTIRL REEIAEQHRA LGQMKEMAAK YGYDISGPAT NAQEAIQWTY FGYLAAVKSQ NGAAMSFGRT STFLDVYIER DLKAGKITEQ EAQEMVDHLV MKLRMVRFLR TPEYDELFSG DPIWATESIG GMGLDGRTLV TKNSFRFLNT LYTMGPSPEP NMTILWSEKL PLNFKKFAAK VSIDTSSLQY ENDDLMRPDF NNDDYAIACC VSPMIVGKQM QFFGARANLA KTMLYAINGG VDEKLKMQVG PKSEPIKGDV LNYDEVMERM DHFMDWLAKQ YITALNIIHY MHDKYSYEAS LMALHDRDVI RTMACGIAGL SVAADSLSAI KYAKVKPIRD EDGLAIDFEI EGEYPQFGNN DPRVDDLAVD LVERFMKKIQ KLHTYRDAIP TQSVLTITSN VVYGKKTGNT PDGRRAGAPF GPGANPMHGR DQKGAVASLT SVAKLPFAYA KDGISYTFSI VPNALGKDDE VRKTNLAGLM DGYFHHEASI EGGQHLNVNV MNREMLLDAM ENPEKYPQLT IRVSGYAVRF NSLTKEQQQD VITRTFTQSM //