ID   PFLA_LISMF              Reviewed;         248 AA.
AC   Q71ZR3;
DT   25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 101.
DE   RecName: Full=Pyruvate formate-lyase-activating enzyme;
DE            Short=PFL-activating enzyme;
DE            EC=1.97.1.4;
GN   Name=pflA; OrderedLocusNames=LMOf2365_1426;
OS   Listeria monocytogenes serotype 4b (strain F2365).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=265669;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F2365;
RX   PubMed=15115801; DOI=10.1093/nar/gkh562;
RA   Nelson K.E., Fouts D.E., Mongodin E.F., Ravel J., DeBoy R.T., Kolonay J.F.,
RA   Rasko D.A., Angiuoli S.V., Gill S.R., Paulsen I.T., Peterson J.D.,
RA   White O., Nelson W.C., Nierman W.C., Beanan M.J., Brinkac L.M.,
RA   Daugherty S.C., Dodson R.J., Durkin A.S., Madupu R., Haft D.H.,
RA   Selengut J., Van Aken S.E., Khouri H.M., Fedorova N., Forberger H.A.,
RA   Tran B., Kathariou S., Wonderling L.D., Uhlich G.A., Bayles D.O.,
RA   Luchansky J.B., Fraser C.M.;
RT   "Whole genome comparisons of serotype 4b and 1/2a strains of the food-borne
RT   pathogen Listeria monocytogenes reveal new insights into the core genome
RT   components of this species.";
RL   Nucleic Acids Res. 32:2386-2395(2004).
CC   -!- FUNCTION: Activation of pyruvate formate-lyase 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. {ECO:0000250}.
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; Evidence={ECO:0000250};
CC       Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3
CC       cysteines and an exchangeable S-adenosyl-L-methionine. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the organic radical-activating enzymes family.
CC       {ECO:0000305}.
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DR   EMBL; AE017262; AAT04201.1; -; Genomic_DNA.
DR   RefSeq; WP_003721912.1; NC_002973.6.
DR   AlphaFoldDB; Q71ZR3; -.
DR   SMR; Q71ZR3; -.
DR   GeneID; 57122101; -.
DR   KEGG; lmf:LMOf2365_1426; -.
DR   HOGENOM; CLU_058969_1_1_9; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0043365; F:[formate-C-acetyltransferase]-activating enzyme activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd01335; Radical_SAM; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 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   NCBIfam; TIGR02493; PFLA; 1.
DR   PANTHER; PTHR30352:SF23; PYRUVATE FORMATE-LYASE 1-ACTIVATING ENZYME; 1.
DR   PANTHER; PTHR30352; PYRUVATE FORMATE-LYASE-ACTIVATING ENZYME; 1.
DR   Pfam; PF13353; Fer4_12; 1.
DR   Pfam; PF04055; Radical_SAM; 1.
DR   PIRSF; PIRSF000371; PFL_act_enz; 1.
DR   SFLD; SFLDG01066; organic_radical-activating_enz; 1.
DR   SFLD; SFLDF00278; pyruvate_formate-lyase_activas; 1.
DR   SUPFAM; SSF102114; Radical SAM enzymes; 1.
DR   PROSITE; PS01087; RADICAL_ACTIVATING; 1.
DR   PROSITE; PS51918; RADICAL_SAM; 1.
PE   3: Inferred from homology;
KW   4Fe-4S; Cytoplasm; Iron; Iron-sulfur; Metal-binding; Oxidoreductase;
KW   S-adenosyl-L-methionine.
FT   CHAIN           1..248
FT                   /note="Pyruvate formate-lyase-activating enzyme"
FT                   /id="PRO_0000200531"
FT   DOMAIN          17..248
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT   BINDING         31
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="4Fe-4S-S-AdoMet"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9N4"
FT   BINDING         35
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="4Fe-4S-S-AdoMet"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9N4"
FT   BINDING         37..39
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9N4"
FT   BINDING         38
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="4Fe-4S-S-AdoMet"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9N4"
FT   BINDING         80
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9N4"
FT   BINDING         135..137
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9N4"
FT   BINDING         208
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9N4"
SQ   SEQUENCE   248 AA;  28115 MW;  0A6F5BBA95CBEBC9 CRC64;
     MTEVLGRVHS VETMGTVDGP GIRFIVFMQG CLLRCQFCHN PDTWKIGTGT ERSAQDVFDE
     AIKYKEFWDA SGGGVTVSGG EPLLQVDFLI EFFTLCKAAG VHTTIDSCGG CFTRDPEFIE
     KLDRLMEVTD LILLDIKQIN PEKHLKLTTK SNAPIIDFAH YLRDKEQPIW IRHVLIPTKT
     DDPEDLTKLH EFIQTLPNVK QVDVLPYHTM GVYKWKEMGI RYPLEGIEAP EEEVVALANK
     ILETSSYK
//