ID   PFLA_STRMU              Reviewed;         263 AA.
AC   O68575;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   27-MAR-2024, entry version 151.
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; Synonyms=pflA, pflC; OrderedLocusNames=SMU_1692;
OS   Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=210007;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=LT11;
RX   PubMed=11029425; DOI=10.1128/jb.182.21.6055-6065.2000;
RA   Boyd D.A., Cvitkovitch D.G., Bleiweis A.S., Kiriukhin M.Y., Debabov D.V.,
RA   Neuhaus F.C., Hamilton I.R.;
RT   "Defects in D-alanyl-lipoteichoic acid synthesis in Streptococcus mutans
RT   results in acid sensitivity.";
RL   J. Bacteriol. 182:6055-6065(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=GS-5;
RX   PubMed=10899886; DOI=10.1128/iai.68.8.4773-4777.2000;
RA   Yamamoto Y., Sato Y., Takahashi-Abbe S., Takahashi N., Kizaki H.;
RT   "Characterization of the Streptococcus mutans pyruvate formate-lyase (PFL)-
RT   activating enzyme gene by complementary reconstitution of the in vitro PFL-
RT   reactivating system.";
RL   Infect. Immun. 68:4773-4777(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700610 / UA159;
RX   PubMed=12397186; DOI=10.1073/pnas.172501299;
RA   Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA   Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S.,
RA   Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.;
RT   "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT   pathogen.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
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; AF051356; AAC05773.1; -; Genomic_DNA.
DR   EMBL; AB018417; BAA34998.1; -; Genomic_DNA.
DR   EMBL; AE014133; AAN59329.1; -; Genomic_DNA.
DR   RefSeq; NP_722023.1; NC_004350.2.
DR   RefSeq; WP_002262580.1; NC_004350.2.
DR   AlphaFoldDB; O68575; -.
DR   SMR; O68575; -.
DR   STRING; 210007.SMU_1692; -.
DR   DNASU; 1028925; -.
DR   GeneID; 66818930; -.
DR   KEGG; smu:SMU_1692; -.
DR   PATRIC; fig|210007.7.peg.1512; -.
DR   eggNOG; COG1180; Bacteria.
DR   HOGENOM; CLU_058969_1_1_9; -.
DR   OrthoDB; 9782387at2; -.
DR   PhylomeDB; O68575; -.
DR   Proteomes; UP000002512; Chromosome.
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   Reference proteome; S-adenosyl-L-methionine.
FT   CHAIN           1..263
FT                   /note="Pyruvate formate-lyase-activating enzyme"
FT                   /id="PRO_0000200533"
FT   DOMAIN          23..260
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT   BINDING         37
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         41
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         43..45
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9N4"
FT   BINDING         44
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         87
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9N4"
FT   BINDING         142..144
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9N4"
FT   BINDING         215
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9N4"
SQ   SEQUENCE   263 AA;  30150 MW;  575405F3EE248EFC CRC64;
     MIEKVDYEKV TGLVNSTESF GSVDGPGIRF VVFMQGCQMR CQYCHNPDTW AMKNDRATER
     TAGDVFKEAL RFKDFWGDTG GITVSGGEAT LQMDFLIALF SLAKEKGIHT TLDTCALTFR
     NTPKYLEKYE KLMAVTDLVL LDIKEINPDQ HKIVTGHSNK TILACARYLS DIGKPVWIRH
     VLVPGLTDRD EDLIKLGEYV KTLKNVQRFE ILPYHTMGEF KWRELGIPYP LEGVKPPTPD
     RVRNAKKLMH TETYEEYKKR INH
//