PFLB_ECOLI
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 03-AUG-2022, entry version 200.
DE RecName: Full=Formate acetyltransferase 1;
DE EC=2.3.1.54;
DE AltName: Full=Pyruvate formate-lyase 1;
GN Name=pflB; Synonyms=pfl; OrderedLocusNames=b0903, JW0886;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; 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 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 [7]
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 [8]
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 [9]
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 [10]
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 [11]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
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 -!- 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 -!- PATHWAY: Fermentation; pyruvate fermentation; formate from pyruvate:
CC step 1/1.
CC -!- SUBUNIT: Homodimer.
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}.
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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 SWISS-2DPAGE; P09373; -.
DR jPOST; P09373; -.
DR PaxDb; P09373; -.
DR PRIDE; P09373; -.
DR EnsemblBacteria; AAC73989; AAC73989; b0903.
DR EnsemblBacteria; BAA35638; BAA35638; BAA35638.
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; PYGGIKM; -.
DR PhylomeDB; P09373; -.
DR BioCyc; EcoCyc:PYRUVFORMLY-MON; -.
DR BioCyc; MetaCyc:PYRUVFORMLY-MON; -.
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 GO; GO:0006567; P:threonine catabolic process; IBA:GO_Central.
DR CDD; cd01678; PFL1; 1.
DR InterPro; IPR005949; Form_AcTrfase.
DR InterPro; IPR019777; Form_AcTrfase_GR_CS.
DR InterPro; IPR001150; Gly_radical.
DR InterPro; IPR004184; PFL_dom.
DR Pfam; PF01228; Gly_radical; 1.
DR Pfam; PF02901; PFL-like; 1.
DR TIGRFAMs; TIGR01255; pyr_form_ly_1; 1.
DR PROSITE; PS00850; GLY_RADICAL_1; 1.
DR PROSITE; PS51149; GLY_RADICAL_2; 1.
DR PROSITE; PS51554; PFL; 1.
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
