ID   A0A380LJ64_9FIRM        Unreviewed;       748 AA.
AC   A0A380LJ64;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   RecName: Full=Formate acetyltransferase {ECO:0000256|ARBA:ARBA00013897, ECO:0000256|RuleBase:RU368075};
DE            EC=2.3.1.54 {ECO:0000256|ARBA:ARBA00013214, ECO:0000256|RuleBase:RU368075};
DE   AltName: Full=Pyruvate formate-lyase {ECO:0000256|ARBA:ARBA00031063, ECO:0000256|RuleBase:RU368075};
GN   Name=pflB {ECO:0000313|EMBL:SUO03225.1};
GN   ORFNames=NCTC11087_00077 {ECO:0000313|EMBL:SUO03225.1};
OS   Faecalicoccus pleomorphus.
OC   Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC   Erysipelotrichaceae; Faecalicoccus.
OX   NCBI_TaxID=1323 {ECO:0000313|EMBL:SUO03225.1, ECO:0000313|Proteomes:UP000255523};
RN   [1] {ECO:0000313|EMBL:SUO03225.1, ECO:0000313|Proteomes:UP000255523}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC11087 {ECO:0000313|EMBL:SUO03225.1,
RC   ECO:0000313|Proteomes:UP000255523};
RG   Pathogen Informatics;
RA   Doyle S.;
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
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         Evidence={ECO:0000256|ARBA:ARBA00001179,
CC         ECO:0000256|RuleBase:RU368075};
CC   -!- PATHWAY: Fermentation; pyruvate fermentation; formate from pyruvate:
CC       step 1/1. {ECO:0000256|ARBA:ARBA00004809,
CC       ECO:0000256|RuleBase:RU368075}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|RuleBase:RU368075}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       ECO:0000256|RuleBase:RU368075}.
CC   -!- SIMILARITY: Belongs to the glycyl radical enzyme (GRE) family. PFL
CC       subfamily. {ECO:0000256|ARBA:ARBA00008375,
CC       ECO:0000256|RuleBase:RU368075}.
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; UHFX01000003; SUO03225.1; -; Genomic_DNA.
DR   RefSeq; WP_022790469.1; NZ_UHFX01000003.1.
DR   AlphaFoldDB; A0A380LJ64; -.
DR   GeneID; 77461078; -.
DR   OrthoDB; 9803969at2; -.
DR   UniPathway; UPA00920; UER00891.
DR   Proteomes; UP000255523; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008861; F:formate C-acetyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd01678; PFL1; 1.
DR   Gene3D; 3.20.70.20; -; 1.
DR   InterPro; IPR005949; Form_AcTrfase.
DR   InterPro; IPR019777; Form_AcTrfase_GR_CS.
DR   InterPro; IPR001150; Gly_radical.
DR   InterPro; IPR004184; PFL_dom.
DR   NCBIfam; TIGR01255; pyr_form_ly_1; 1.
DR   PANTHER; PTHR30191; FORMATE ACETYLTRANSFERASE; 1.
DR   PANTHER; PTHR30191:SF0; FORMATE ACETYLTRANSFERASE 1; 1.
DR   Pfam; PF01228; Gly_radical; 1.
DR   Pfam; PF02901; PFL-like; 1.
DR   PIRSF; PIRSF000379; For_Ac_trans_1; 1.
DR   SUPFAM; SSF51998; PFL-like glycyl radical enzymes; 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 {ECO:0000256|ARBA:ARBA00023315,
KW   ECO:0000256|RuleBase:RU368075};
KW   Carbohydrate metabolism {ECO:0000256|RuleBase:RU368075};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|RuleBase:RU368075};
KW   Glucose metabolism {ECO:0000256|ARBA:ARBA00022526,
KW   ECO:0000256|RuleBase:RU368075}; Lyase {ECO:0000313|EMBL:SUO03225.1};
KW   Organic radical {ECO:0000256|ARBA:ARBA00022818,
KW   ECO:0000256|PIRSR:PIRSR000379-2}; Pyruvate {ECO:0000313|EMBL:SUO03225.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000255523};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU368075}.
FT   DOMAIN          1..616
FT                   /note="PFL"
FT                   /evidence="ECO:0000259|PROSITE:PS51554"
FT   DOMAIN          623..748
FT                   /note="Glycine radical"
FT                   /evidence="ECO:0000259|PROSITE:PS51149"
FT   ACT_SITE        410
FT                   /note="S-acetylcysteine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000379-1"
FT   ACT_SITE        411
FT                   /note="Cysteine radical intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000379-1"
FT   MOD_RES         723
FT                   /note="Glycine radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000379-2,
FT                   ECO:0000256|PROSITE-ProRule:PRU00493"
SQ   SEQUENCE   748 AA;  84651 MW;  15D3A68DE1DD2BAF CRC64;
     MFEQWTGFKG NKWQEEVNVR DFIQNNYEPY DGDEAFLADP TEATNTLWDA LQKLQKEERA
     KGGVLDMETE VVSSLTSYGP GYIDENLKDL EQIVGLQTDK PLKRAFMPYG GIRMSIEACE
     TYGYTPSDKL KEIFTKYHKT HNDAVFGAYT PEMRLARKNK IITGLPDTYG RGRIVGDYRR
     VALYGIDFLI EEKQKDFDLC GDGTMLDHII RQREELSDQI KALKEMKEMA AIYGYDISKP
     AKNAKEAVQW LYFGYLAAIK TQNGAAMSVG RISTFLDIYM QRDLKNGTLT EEKAQELIDH
     MVMKFRMVKF ARIPSYNQLF SGDPVWATLD VAGIGMDGRH MVTKTCFRFL HTLENMGPSP
     EPNLTVLYSS HLPEPFKKYA AKVSVATSSL QYENDDVMRP EWGDDYAVCC CVSATQTGKE
     MQFFGARANL AKCLLYAING GVDERTKMQV GPEYKPITSD VLDFDEVMHK YDLMMDWLSG
     LYVNTLNLIQ YMHDKYYYEA AEMALIDTDV RRTFATGIAG FSHVVDSLCA IKYAKVTPIR
     DEDGIVVDYK VEGDFPRYGN DDDRADDIAV WLLKTFMNKI RKHHTYRNSE PTTSILTITS
     NVVYGKATGT LPDGRKAGEP LSPGANPSYG AEKNGLLASL NSVAKLPYEY ALDGISNTQT
     INPGALGHSD TERAENLVHV MDGYFDQGAH HLNVNVFGVE KLKDAMEHPE KEEYQNFTIR
     VSGYAVKFID LTREQQLDVI ARTCHDHL
//