ID   PFLB_STAES              Reviewed;         748 AA.
AC   Q8CTX6;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   25-MAY-2022, entry version 96.
DE   RecName: Full=Formate acetyltransferase;
DE            EC=2.3.1.54;
DE   AltName: Full=Pyruvate formate-lyase;
GN   Name=pflB; OrderedLocusNames=SE_0214;
OS   Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=176280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 12228 / FDA PCI 1200;
RX   PubMed=12950922; DOI=10.1046/j.1365-2958.2003.03671.x;
RA   Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q.,
RA   Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H.,
RA   Zhao G.-P., Qu D., Danchin A., Wen Y.-M.;
RT   "Genome-based analysis of virulence genes in a non-biofilm-forming
RT   Staphylococcus epidermidis strain (ATCC 12228).";
RL   Mol. Microbiol. 49:1577-1593(2003).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + formate = CoA + pyruvate; Xref=Rhea:RHEA:11844,
CC         ChEBI:CHEBI:15361, ChEBI:CHEBI:15740, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57288; EC=2.3.1.54;
CC   -!- ACTIVITY REGULATION: Activated by pfl-activating enzyme under anaerobic
CC       conditions via generation of an organic free radical. {ECO:0000250}.
CC   -!- PATHWAY: Fermentation; pyruvate fermentation; formate from pyruvate:
CC       step 1/1.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- MISCELLANEOUS: Several mechanisms have been proposed based on complexes
CC       formed with substrate analogs. After activation by the glycine radical,
CC       the cysteine radical, Cys-413, can abstract hydrogen atoms from the
CC       other active site cysteine, Cys-412, and from coenzyme A, and it can
CC       also transfer hydrogen atoms to product radicals. The other active site
CC       cysteine can attack the central carbonyl of pyruvate and covalently
CC       bind the product acetyl group (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycyl radical enzyme (GRE) family. PFL
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AE015929; AAO03811.1; -; Genomic_DNA.
DR   RefSeq; NP_763769.1; NC_004461.1.
DR   RefSeq; WP_002485526.1; NZ_WBME01000011.1.
DR   AlphaFoldDB; Q8CTX6; -.
DR   SMR; Q8CTX6; -.
DR   STRING; 176280.SE_0214; -.
DR   EnsemblBacteria; AAO03811; AAO03811; SE_0214.
DR   KEGG; sep:SE_0214; -.
DR   PATRIC; fig|176280.10.peg.193; -.
DR   eggNOG; COG1882; Bacteria.
DR   HOGENOM; CLU_023898_0_0_9; -.
DR   OMA; PYGGIKM; -.
DR   UniPathway; UPA00920; UER00891.
DR   Proteomes; UP000001411; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008861; F:formate C-acetyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd01678; PFL1; 1.
DR   InterPro; IPR005949; Form_AcTrfase.
DR   InterPro; IPR019777; Form_AcTrfase_GR_CS.
DR   InterPro; IPR001150; Gly_radical.
DR   InterPro; IPR004184; PFL_dom.
DR   Pfam; PF01228; Gly_radical; 1.
DR   Pfam; PF02901; PFL-like; 1.
DR   TIGRFAMs; TIGR01255; pyr_form_ly_1; 1.
DR   PROSITE; PS00850; GLY_RADICAL_1; 1.
DR   PROSITE; PS51149; GLY_RADICAL_2; 1.
DR   PROSITE; PS51554; PFL; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Carbohydrate metabolism; Cytoplasm; Glucose metabolism;
KW   Organic radical; Transferase.
FT   CHAIN           1..748
FT                   /note="Formate acetyltransferase"
FT                   /id="PRO_0000271729"
FT   DOMAIN          5..618
FT                   /note="PFL"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00887"
FT   DOMAIN          625..748
FT                   /note="Glycine radical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00493"
FT   ACT_SITE        412
FT                   /note="S-acetylcysteine intermediate"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        413
FT                   /note="Cysteine radical intermediate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         723
FT                   /note="Glycine radical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00493"
SQ   SEQUENCE   748 AA;  85026 MW;  BBB9F767CE91976C CRC64;
     MLETNNHTNA WQGFKTGRWN KNIDVREFIQ LNYSLYEGDD EFLEGPTKAT ETLWDQVMQL
     SKEERERGGM WDMDTKVAST ITSHDAGYLD KDLEKVVGVQ TEKPFKRSMQ PFGGIRMAKA
     ACEAYGYELD PETEKIFTEY RKTHNQGVFD AYSREMLNCR KAGIITGLPD AYGRGRIIGD
     YRRVALYGVD FLMEQKLKDF NTMSTEMSED VIRLREELTE QYRSLQDLKE LGQKYGFDIS
     RPATNFKEAV QWLYLAYLAA IKEQNGAAMS LGRTSTFLDI YAERDLQNGD ITEQEVQEII
     DHFIMKLRIV KFARTPEYNE LFSGDPTWVT ESIGGVGIDG RPMVTKNSFR FLHSLDNLGP
     APEPNLTVLW STRLPENFKI YCAKMSIKTS SIQYENDDLM RESYGDDYGI ACCVSAMKIG
     KQMQFFGARA NLAKALLYAI NGGKDEKSGK QVGPSYEGIK SDVLDYDEVF ERYEKMMDWL
     AGVYINSLNI IHYMHDKYSY ERLEMALHDT EIIRTMATGI AGLSVAADSL SAIKYAQVKP
     IRNEEGLVTD FEIEGDFPKY GNNDSRVDEI AVDLVERFMT KLRSHKTYRN SEHTMSVLTI
     TSNVVYGKKT GNTPDGRKAG EPFAPGANPM HGRDQKGALS SLSSVAKIPY DCCKDGISNT
     FSIVPKSLGK EEADQNKNLT SMLDGYAMQH GHHLNINVFN RETLIDAMEH PEEYPQLTIR
     VSGYAVNFIK LTREQQLDVI SRTFHESM