PFLA_STRMU
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 03-AUG-2022, entry version 145.
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; Firmicutes; 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 PRIDE; O68575; -.
DR DNASU; 1028925; -.
DR EnsemblBacteria; AAN59329; AAN59329; SMU_1692.
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 OMA; IGVPNKR; -.
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 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 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
