ID   PFLA_CLOPA              Reviewed;         238 AA.
AC   Q46267;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Pyruvate formate-lyase-activating enzyme;
DE            Short=PFL-activating enzyme;
DE            EC=1.97.1.4;
DE   AltName: Full=Formate-C-acetyltransferase-activating enzyme;
GN   Name=act;
OS   Clostridium pasteurianum.
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1501;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8636053; DOI=10.1128/jb.178.8.2440-2444.1996;
RA   Weidner G., Sawers G.;
RT   "Molecular characterization of the genes encoding pyruvate formate-lyase
RT   and its activating enzyme of Clostridium pasteurianum.";
RL   J. Bacteriol. 178:2440-2444(1996).
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.
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.
CC   -!- SIMILARITY: Belongs to the organic radical-activating enzymes family.
CC       {ECO:0000305}.
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DR   EMBL; X93463; CAA63749.1; -; Genomic_DNA.
DR   PIR; JC6011; JC6011.
DR   AlphaFoldDB; Q46267; -.
DR   SMR; Q46267; -.
DR   BioCyc; MetaCyc:MON-12104; -.
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   Gene3D; 3.20.20.70; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR034457; Organic_radical-activating.
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   SFLD; SFLDF00278; pyruvate_formate-lyase_activas; 1.
DR   SFLD; SFLDS00029; Radical_SAM; 1.
DR   TIGRFAMs; TIGR02493; PFLA; 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..238
FT                   /note="Pyruvate formate-lyase-activating enzyme"
FT                   /id="PRO_0000200529"
FT   DOMAIN          15..236
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT   BINDING         29
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         33
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..37
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9N4"
FT   BINDING         36
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         78
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9N4"
FT   BINDING         126..128
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9N4"
FT   BINDING         199
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9N4"
SQ   SEQUENCE   238 AA;  27148 MW;  85E2ACED85C6B7D1 CRC64;
     MVMGRIHSIE SMGLVDGPGI RTVVFFQGCG LRCSYCHNPD TWNMAGGKEL TAEELLKKLL
     RFKPYFDRSG GGVTFSGGEV LLQPEFLIDI LKLCKEQGIH TAIDTAGYGY GNYEEILKHT
     DLVLLDIKHV DDDGYKCITG KGKRGFDDFL KAVENIGVKV WIRHVIVPTL TDSKENIRKL
     ANIIKNIRNV EKVELLPYHT LGINKYEKLN LDYKLRDIEA MDKEKRKKLE KYLKELLE