ID   PFL_CLOPA               Reviewed;         740 AA.
AC   Q46266;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Formate acetyltransferase;
DE            EC=2.3.1.54;
DE   AltName: Full=Pyruvate formate-lyase;
GN   Name=pfl;
OS   Clostridium pasteurianum.
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1501;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8636053; DOI=10.1128/jb.178.8.2440-2444.1996;
RA   Weidner G., Sawers G.;
RT   "Molecular characterization of the genes encoding pyruvate formate-lyase
RT   and its activating enzyme of Clostridium pasteurianum.";
RL   J. Bacteriol. 178:2440-2444(1996).
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   -!- 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-406, can abstract hydrogen atoms from the
CC       other active site cysteine, Cys-405, 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; X93463; CAA63748.1; -; Genomic_DNA.
DR   PIR; JC6010; JC6010.
DR   RefSeq; WP_003448207.1; NZ_CP013019.1.
DR   AlphaFoldDB; Q46266; -.
DR   SMR; Q46266; -.
DR   PRIDE; Q46266; -.
DR   BioCyc; MetaCyc:MON-12106; -.
DR   BRENDA; 2.3.1.54; 1502.
DR   UniPathway; UPA00920; UER00891.
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..740
FT                   /note="Formate acetyltransferase"
FT                   /id="PRO_0000166692"
FT   DOMAIN          1..610
FT                   /note="PFL"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00887"
FT   DOMAIN          617..740
FT                   /note="Glycine radical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00493"
FT   ACT_SITE        405
FT                   /note="S-acetylcysteine intermediate"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        406
FT                   /note="Cysteine radical intermediate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         715
FT                   /note="Glycine radical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00493"
SQ   SEQUENCE   740 AA;  83217 MW;  19F666ACD19205D8 CRC64;
     MFKQWEGFQD GEWTNDVNVR DFIQKNYKEY TGDKSFLKGP TEKTKKVWDK AVSLILEELK
     KGILDVDTET ISGINSFKPG YLDKDNEVIV GFQTDAPLKR ITNPFGGIRM AEQSLKEYGF
     KISDEMHNIF TNYRKTHNQG VFDAYSEETR IARSAGVLTG LPDAYGRGRI IGDYRRVALY
     GIDFLIQEKK KDLSNLKGDM LDELIRLREE VSEQIRALDE IKKMALSYGV DISRPAVNAK
     EAAQFLYFGY LAGVKENNGA AMSLGRTSTF LDIYIERDLE QGLITEDEAQ EVIDQFIIKL
     RLVRHLRTPE YNELFAGDPT WVTESIAGVG IDGRSLVTKN SFRYLHTLIN LGSAPEPNMT
     VLWSENLPES FKKFCAEMSI LTDSIQYEND DIMRPIYGDD YAIACCVSAM RVGKDMQFFG
     ARCNLAKCLL LAINGGVDEK KGIKVVPDIE PITDEVLDYE KVKENYFKVL EYMAGLYVNT
     MNIIHFMHDK YAYEASQMAL HDTKVGRLMA FGIAGFSVAA DSLSAIRYAK VKPIRENGIT
     VDFVKEGDFP KYGNDDDRVD SIAVEIVEKF SDELKKHPTY RNAKHTLSVL TITSNVMYGK
     KTGTTPDGRK VGEPLAPGAN PMHGRDMEGA LASLNSVAKV PYVCCEDGVS NTFSIVPDAL
     GNDHDVRINN LVSIMGGYFG QGAHHLNVNV LNRETLIDAM NNPDKYPTLT IRVSGYAVNF
     NRLSKDHQKE VISRTFHEKL