ID   PFL_LACLM               Reviewed;         787 AA.
AC   O32799; A2RIY3;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Formate acetyltransferase;
DE            EC=2.3.1.54;
DE   AltName: Full=Pyruvate formate-lyase;
GN   Name=pfl; OrderedLocusNames=llmg_0629;
OS   Lactococcus lactis subsp. cremoris (strain MG1363).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus; Lactococcus cremoris subsp. cremoris.
OX   NCBI_TaxID=416870;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9294449; DOI=10.1128/jb.179.18.5884-5891.1997;
RA   Arnau J., Joergensen F., Madsen S.M., Vrang A., Israelsen H.;
RT   "Cloning, expression, and characterization of the Lactococcus lactis pfl
RT   gene, encoding pyruvate formate-lyase.";
RL   J. Bacteriol. 179:5884-5891(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MG1363;
RX   PubMed=17307855; DOI=10.1128/jb.01768-06;
RA   Wegmann U., O'Connell-Motherway M., Zomer A., Buist G., Shearman C.,
RA   Canchaya C., Ventura M., Goesmann A., Gasson M.J., Kuipers O.P.,
RA   van Sinderen D., Kok J.;
RT   "The complete genome sequence of the lactic acid bacterial paradigm
RT   Lactococcus lactis subsp. cremoris MG1363.";
RL   J. Bacteriol. 189:3256-3270(2007).
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-417, can abstract hydrogen atoms from the
CC       other active site cysteine, Cys-416, 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; AJ000325; CAA03991.1; -; Genomic_DNA.
DR   EMBL; AM406671; CAL97231.1; -; Genomic_DNA.
DR   RefSeq; WP_011834639.1; NZ_WJVF01000023.1.
DR   AlphaFoldDB; O32799; -.
DR   SMR; O32799; -.
DR   STRING; 416870.llmg_0629; -.
DR   EnsemblBacteria; CAL97231; CAL97231; llmg_0629.
DR   KEGG; llm:llmg_0629; -.
DR   eggNOG; COG1882; Bacteria.
DR   HOGENOM; CLU_023898_0_0_9; -.
DR   OMA; PYGGIKM; -.
DR   PhylomeDB; O32799; -.
DR   BioCyc; LLAC416870:LLMG_RS03285-MON; -.
DR   UniPathway; UPA00920; UER00891.
DR   Proteomes; UP000000364; 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..787
FT                   /note="Formate acetyltransferase"
FT                   /id="PRO_0000166694"
FT   DOMAIN          8..629
FT                   /note="PFL"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00887"
FT   DOMAIN          645..774
FT                   /note="Glycine radical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00493"
FT   ACT_SITE        416
FT                   /note="S-acetylcysteine intermediate"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        417
FT                   /note="Cysteine radical intermediate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         749
FT                   /note="Glycine radical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00493"
SQ   SEQUENCE   787 AA;  89107 MW;  66537F086BC82E7E CRC64;
     MKTEVTENIF EQAWDGFKGT NWRDKASVTR FVQENYKPYD GDESFLAGPT ERTLKVKKII
     EDTKNHYEEV GFPFDTDRVT SIDKIPAGYI DANDKELELI YGMQNSELFR LNFMPRGGLR
     VAEKILTEHG LSVDPGLHDV LSQTMTSVND GIFRAYTSAI RKARHAHTVT GLPDAYSRGR
     IIGVYARLAL YGADYLMKEK AKEWDAITEI NDDNIRLKEE INMQYQALQE VVNFGALYGL
     DVSRPAMNVK EAIQWVNIAY MAVCRVINGA ATSLGRVPIV LDIFAERDLA RGTFTEQEIQ
     EFVDDFILKL RTMKFARAAA YDELYSGDPT FITTSMAGMG NDGRHRVTKM DYRFLNTLDT
     IGNAPEPNLT VLWDSKLPYS FKRYSMSMSH KHSSIQYEGV ETMAKDGYGE MSCISCCVSP
     LDPENEEGRH NLQYFGARVN VLKAMLTGLN GGYDDVHKDY KVFDIEPVRD EILDYDTVME
     NFDKSLNWLT DTYVDAMNII HYMTDKYNYE AVQMAFLPTK VRANMGFGIC GFANTVDSLS
     AIKYAKVKTL RDENGYIYDY EVEGDFPRYG EDDDRADDIA KLVMKMYHEK LASHKLYKNA
     EATVSLLTIT SNVAYSKQTG NSPVHKGVFL NEDGTVNKSK LEFFSPGANP SNKAKGGWLQ
     NLRSLAKLEF KDANDGISLT TQVSPRALGK TRDEQVDNLV QILDGYFTPG ALINGTEFAG
     QHVNLNVMDL KDVYDKIMRG EDVIVRISGY CVNTKYLTPE QKQELTERVF HEVLSNDDEE
     VMHTSNI