ID   PFLB_STAAW              Reviewed;         749 AA.
AC   Q7A1W9;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-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=MW0201;
OS   Staphylococcus aureus (strain MW2).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=196620;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MW2;
RX   PubMed=12044378; DOI=10.1016/s0140-6736(02)08713-5;
RA   Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y.,
RA   Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K.;
RT   "Genome and virulence determinants of high virulence community-acquired
RT   MRSA.";
RL   Lancet 359:1819-1827(2002).
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-414, can abstract hydrogen atoms from the
CC       other active site cysteine, Cys-413, 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BA000033; BAB94066.1; -; Genomic_DNA.
DR   RefSeq; WP_000894660.1; NC_003923.1.
DR   AlphaFoldDB; Q7A1W9; -.
DR   SMR; Q7A1W9; -.
DR   EnsemblBacteria; BAB94066; BAB94066; BAB94066.
DR   KEGG; sam:MW0201; -.
DR   HOGENOM; CLU_023898_0_0_9; -.
DR   OMA; PYGGIKM; -.
DR   UniPathway; UPA00920; UER00891.
DR   Proteomes; UP000000418; 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..749
FT                   /note="Formate acetyltransferase"
FT                   /id="PRO_0000271727"
FT   DOMAIN          3..619
FT                   /note="PFL"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00887"
FT   DOMAIN          626..749
FT                   /note="Glycine radical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00493"
FT   ACT_SITE        413
FT                   /note="S-acetylcysteine intermediate"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        414
FT                   /note="Cysteine radical intermediate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         724
FT                   /note="Glycine radical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00493"
SQ   SEQUENCE   749 AA;  84862 MW;  F38EEC2D41FF03A5 CRC64;
     MLETNKNHAT AWQGFKNGRW NRHVDVREFI QLNYTLYEGN DSFLAGPTEA TSKLWEQVMQ
     LSKEERERGG MWDMDTKVAS TITSHDAGYL DKDLETIVGV QTEKPFKRSM QPFGGIRMAK
     AACEAYGYEL DEETEKIFTD YRKTHNQGVF DAYSREMLNC RKAGVITGLP DAYGRGRIIG
     DYRRVALYGV DFLMEEKMHD FNTMSTEMSE DVIRLREELS EQYRALKELK ELGQKYGFDL
     SRPAENFKEA VQWLYLAYLA AIKEQNGAAM SLGRTSTFLD IYAERDLKAG VITESEVQEI
     IDHFIMKLRI VKFARTPDYN ELFSGDPTWV TESIGGVGID GRPLVTKNSF RFLHSLDNLG
     PAPEPNLTVL WSVRLPDNFK TYCAKMSIKT SSIQYENDDI MRESYGDDYG IACCVSAMTI
     GKQMQFFGAR ANLAKTLLYA INGGKDEKSG AQVGPNFEGI NSEVLEYDEV FKKFDQMMDW
     LAGVYINSLN VIHYMHDKYS YERIEMALHD TEIVRTMATG IAGLSVAADS LSAIKYAQVK
     PIRNEEGLVV DFEIEGDFPK YGNNDDRVDD IAVDLVERFM TKLRSHKTYR DSEHTMSVLT
     ITSNVVYGKK TGNTPDGRKA GEPFAPGANP MHGRDQKGAL SSLSSVAKIP YDCCKDGISN
     TFSIVPKSLG KEPEDQNRNL TSMLDGYAMQ CGHHLNINVF NRETLIDAME HPEEYPQLTI
     RVSGYAVNFI KLTREQQLDV ISRTFHESM