ID   PFLB_STAEQ              Reviewed;         748 AA.
AC   Q5HKH9;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Formate acetyltransferase;
DE            EC=2.3.1.54;
DE   AltName: Full=Pyruvate formate-lyase;
GN   Name=pflB; OrderedLocusNames=SERP2366;
OS   Staphylococcus epidermidis (strain ATCC 35984 / RP62A).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=176279;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35984 / RP62A;
RX   PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA   Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA   Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA   Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA   Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA   Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA   Fraser C.M.;
RT   "Insights on evolution of virulence and resistance from the complete genome
RT   analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT   a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT   strain.";
RL   J. Bacteriol. 187:2426-2438(2005).
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; CP000029; AAW53179.1; -; Genomic_DNA.
DR   RefSeq; WP_002500535.1; NC_002976.3.
DR   AlphaFoldDB; Q5HKH9; -.
DR   SMR; Q5HKH9; -.
DR   STRING; 176279.SERP2366; -.
DR   PRIDE; Q5HKH9; -.
DR   EnsemblBacteria; AAW53179; AAW53179; SERP2366.
DR   KEGG; ser:SERP2366; -.
DR   eggNOG; COG1882; Bacteria.
DR   HOGENOM; CLU_023898_0_0_9; -.
DR   OMA; PYGGIKM; -.
DR   OrthoDB; 116406at2; -.
DR   UniPathway; UPA00920; UER00891.
DR   Proteomes; UP000000531; 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; Reference proteome; Transferase.
FT   CHAIN           1..748
FT                   /note="Formate acetyltransferase"
FT                   /id="PRO_0000271728"
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;  85040 MW;  6CE86189394A85F5 CRC64;
     MLETNNHTNA WQGFKTGRWN KNIDVREFIQ LNYSLYEGDD EFLEGPTKAT ETLWDQVMQL
     SKEERERGGM WDMDTKVAST ITSHDAGYLD KDLEKVVGVQ TEKPFKRSMQ PFGGIRMAKA
     ACEAYGYELD PETEKIFTEY RKTHNQGVFD AYSREMLNCR KAGIITGLPD AYGRGRIIGD
     YRRVALYGVD FLMEQKLKDF NTMSTEMSED VIRLREELSE 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 EEVDQNKNLT SMLDGYAMQH GHHLNINVFN RETLIDAMEH PEEYPQLTIR
     VSGYAVNFIK LTREQQLDVI SRTFHESM