PFLA_ECOLI
ID PFLA_ECOLI Reviewed; 246 AA.
AC P0A9N4; P09374;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Pyruvate formate-lyase 1-activating enzyme;
DE EC=1.97.1.4;
DE AltName: Full=Formate-C-acetyltransferase-activating enzyme 1;
DE AltName: Full=PFL-activating enzyme 1;
GN Name=pflA; Synonyms=act; OrderedLocusNames=b0902, JW0885;
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 X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) IN COMPLEXES WITH IRON-SULFUR
RP (4FE-4S); SAM AND A PEPTIDE SUBSTRATE VAL-SER-GLY-TYR-ALA-VAL, COFACTOR,
RP AND SUBUNIT.
RX PubMed=18852451; DOI=10.1073/pnas.0806640105;
RA Vey J.L., Yang J., Li M., Broderick W.E., Broderick J.B., Drennan C.L.;
RT "Structural basis for glycyl radical formation by pyruvate formate-lyase
RT activating enzyme.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:16137-16141(2008).
CC -!- FUNCTION: Activation of pyruvate formate-lyase 1 under anaerobic
CC conditions by generation of an organic free radical, using S-
CC adenosylmethionine and reduced flavodoxin as cosubstrates to produce
CC 5'-deoxy-adenosine.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glycyl-[formate C-acetyltransferase] + reduced [flavodoxin] +
CC S-adenosyl-L-methionine = 5'-deoxyadenosine + glycin-2-yl radical-
CC [formate C-acetyltransferase] + H(+) + L-methionine + semiquinone
CC [flavodoxin]; Xref=Rhea:RHEA:19225, Rhea:RHEA-COMP:10622, Rhea:RHEA-
CC COMP:12190, Rhea:RHEA-COMP:12191, Rhea:RHEA-COMP:14480,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17319, ChEBI:CHEBI:29947,
CC ChEBI:CHEBI:32722, ChEBI:CHEBI:57618, ChEBI:CHEBI:57844,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:140311; EC=1.97.1.4;
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000269|PubMed:18852451};
CC Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3
CC cysteines and an exchangeable S-adenosyl-L-methionine.
CC {ECO:0000269|PubMed:18852451};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:18852451}.
CC -!- INTERACTION:
CC P0A9N4; P64455: ydcY; NbExp=4; IntAct=EBI-1114060, EBI-9129853;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the organic radical-activating enzymes family.
CC {ECO:0000305}.
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DR EMBL; X08035; CAA30829.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73988.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35637.1; -; Genomic_DNA.
DR PIR; S01789; S01789.
DR RefSeq; NP_415422.1; NC_000913.3.
DR RefSeq; WP_000111043.1; NZ_STEB01000006.1.
DR PDB; 3C8F; X-ray; 2.25 A; A=2-246.
DR PDB; 3CB8; X-ray; 2.77 A; A=2-246.
DR PDBsum; 3C8F; -.
DR PDBsum; 3CB8; -.
DR AlphaFoldDB; P0A9N4; -.
DR SMR; P0A9N4; -.
DR BioGRID; 4259353; 13.
DR BioGRID; 849891; 2.
DR DIP; DIP-35915N; -.
DR IntAct; P0A9N4; 19.
DR STRING; 511145.b0902; -.
DR jPOST; P0A9N4; -.
DR PaxDb; P0A9N4; -.
DR PRIDE; P0A9N4; -.
DR EnsemblBacteria; AAC73988; AAC73988; b0902.
DR EnsemblBacteria; BAA35637; BAA35637; BAA35637.
DR GeneID; 67414210; -.
DR GeneID; 945517; -.
DR KEGG; ecj:JW0885; -.
DR KEGG; eco:b0902; -.
DR PATRIC; fig|1411691.4.peg.1374; -.
DR EchoBASE; EB0027; -.
DR eggNOG; COG1180; Bacteria.
DR HOGENOM; CLU_058969_1_0_6; -.
DR InParanoid; P0A9N4; -.
DR OMA; IGVPNKR; -.
DR PhylomeDB; P0A9N4; -.
DR BioCyc; EcoCyc:PFLACTENZ-MON; -.
DR BRENDA; 1.97.1.4; 2026.
DR EvolutionaryTrace; P0A9N4; -.
DR PRO; PR:P0A9N4; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IDA:EcoCyc.
DR GO; GO:0043365; F:[formate-C-acetyltransferase]-activating enzyme activity; IDA:EcoCyc.
DR GO; GO:0016491; F:oxidoreductase activity; IDA:EcoliWiki.
DR GO; GO:0030955; F:potassium ion binding; IDA:EcoCyc.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEP:EcoliWiki.
DR GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0018201; P:peptidyl-glycine modification; IDA:EcoCyc.
DR GO; GO:0051604; P:protein maturation; IDA:EcoCyc.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR034457; Organic_radical-activating.
DR InterPro; IPR012839; Organic_radical_activase.
DR InterPro; IPR012838; PFL1_activating.
DR InterPro; IPR034465; Pyruvate_for-lyase_activase.
DR InterPro; IPR001989; Radical_activat_CS.
DR InterPro; IPR007197; rSAM.
DR PANTHER; PTHR30352; PTHR30352; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR PIRSF; PIRSF000371; PFL_act_enz; 1.
DR SFLD; SFLDF00278; pyruvate_formate-lyase_activas; 1.
DR TIGRFAMs; TIGR02493; PFLA; 1.
DR PROSITE; PS01087; RADICAL_ACTIVATING; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; 4Fe-4S; Carbohydrate metabolism; Cytoplasm;
KW Direct protein sequencing; Glucose metabolism; Iron; Iron-sulfur;
KW Metal-binding; Oxidoreductase; Reference proteome; S-adenosyl-L-methionine.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..246
FT /note="Pyruvate formate-lyase 1-activating enzyme"
FT /id="PRO_0000200522"
FT DOMAIN 16..239
FT /note="Radical SAM core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT BINDING 30
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000269|PubMed:18852451"
FT BINDING 34
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000269|PubMed:18852451"
FT BINDING 36..38
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:18852451"
FT BINDING 37
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000269|PubMed:18852451"
FT BINDING 79
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:18852451"
FT BINDING 130..132
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:18852451"
FT BINDING 203
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:18852451"
FT STRAND 5..14
FT /evidence="ECO:0007829|PDB:3C8F"
FT STRAND 18..28
FT /evidence="ECO:0007829|PDB:3C8F"
FT HELIX 40..42
FT /evidence="ECO:0007829|PDB:3C8F"
FT STRAND 48..51
FT /evidence="ECO:0007829|PDB:3C8F"
FT HELIX 53..60
FT /evidence="ECO:0007829|PDB:3C8F"
FT HELIX 61..63
FT /evidence="ECO:0007829|PDB:3C8F"
FT HELIX 64..67
FT /evidence="ECO:0007829|PDB:3C8F"
FT STRAND 73..79
FT /evidence="ECO:0007829|PDB:3C8F"
FT HELIX 81..84
FT /evidence="ECO:0007829|PDB:3C8F"
FT HELIX 85..96
FT /evidence="ECO:0007829|PDB:3C8F"
FT TURN 97..99
FT /evidence="ECO:0007829|PDB:3C8F"
FT STRAND 102..106
FT /evidence="ECO:0007829|PDB:3C8F"
FT HELIX 115..122
FT /evidence="ECO:0007829|PDB:3C8F"
FT STRAND 125..130
FT /evidence="ECO:0007829|PDB:3C8F"
FT HELIX 136..143
FT /evidence="ECO:0007829|PDB:3C8F"
FT HELIX 148..160
FT /evidence="ECO:0007829|PDB:3C8F"
FT STRAND 164..170
FT /evidence="ECO:0007829|PDB:3C8F"
FT TURN 172..174
FT /evidence="ECO:0007829|PDB:3C8F"
FT HELIX 178..191
FT /evidence="ECO:0007829|PDB:3C8F"
FT STRAND 194..201
FT /evidence="ECO:0007829|PDB:3C8F"
FT HELIX 207..212
FT /evidence="ECO:0007829|PDB:3C8F"
FT TURN 218..221
FT /evidence="ECO:0007829|PDB:3C8F"
FT HELIX 227..238
FT /evidence="ECO:0007829|PDB:3C8F"
FT TURN 239..241
FT /evidence="ECO:0007829|PDB:3C8F"
SQ SEQUENCE 246 AA; 28204 MW; 486E06A9CE97BF37 CRC64;
MSVIGRIHSF ESCGTVDGPG IRFITFFQGC LMRCLYCHNR DTWDTHGGKE VTVEDLMKEV
VTYRHFMNAS GGGVTASGGE AILQAEFVRD WFRACKKEGI HTCLDTNGFV RRYDPVIDEL
LEVTDLVMLD LKQMNDEIHQ NLVGVSNHRT LEFAKYLANK NVKVWIRYVV VPGWSDDDDS
AHRLGEFTRD MGNVEKIELL PYHELGKHKW VAMGEEYKLD GVKPPKKETM ERVKGILEQY
GHKVMF
