ID A0A0F0CIH7_9CLOT Unreviewed; 702 AA.
AC A0A0F0CIH7;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 31.
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_2 {ECO:0000313|EMBL:KJJ77876.1};
GN ORFNames=CLFS41_00400 {ECO:0000313|EMBL:KJJ77876.1};
OS Clostridium sp. FS41.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1609975 {ECO:0000313|EMBL:KJJ77876.1, ECO:0000313|Proteomes:UP000033604};
RN [1] {ECO:0000313|EMBL:KJJ77876.1, ECO:0000313|Proteomes:UP000033604}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FS41 {ECO:0000313|EMBL:KJJ77876.1,
RC ECO:0000313|Proteomes:UP000033604};
RA Poehlein A., Daniel R.;
RT "Genome sequencing of Clostridium sp. FS41.";
RL Submitted (FEB-2015) 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 -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00493}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KJJ77876.1}.
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DR EMBL; JYHN01000005; KJJ77876.1; -; Genomic_DNA.
DR RefSeq; WP_007865661.1; NZ_JYHN01000005.1.
DR AlphaFoldDB; A0A0F0CIH7; -.
DR PATRIC; fig|1609975.3.peg.46; -.
DR UniPathway; UPA00920; UER00891.
DR Proteomes; UP000033604; 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: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; 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; 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};
KW Organic radical {ECO:0000256|ARBA:ARBA00022818,
KW ECO:0000256|RuleBase:RU368075};
KW Reference proteome {ECO:0000313|Proteomes:UP000033604};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU368075}.
FT DOMAIN 1..612
FT /note="PFL"
FT /evidence="ECO:0000259|PROSITE:PS51554"
FT DOMAIN 619..702
FT /note="Glycine radical"
FT /evidence="ECO:0000259|PROSITE:PS51149"
FT ACT_SITE 406
FT /note="S-acetylcysteine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000379-1"
FT ACT_SITE 407
FT /note="Cysteine radical intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000379-1"
SQ SEQUENCE 702 AA; 79037 MW; F416DAECD0BDBC6D CRC64;
MRTEWNTFKG GVWQREINVR DFIQKNYTPY DGNDQFLEGP TENTTELWDQ VMELSKKELE
AGGVLDMDTK VISTITSHGP GYLNKDKETI VGFQTDKPFK RSLQPYGGIR MAMKACQDNG
FEVDPEVVDF FTKHRKTHNA GVFDAYTDEM RACRSSHIIT GLPDAYGRGR IIGDYRRIAL
YGVDALIQEK KEEKDSTRTI MYSDVIRERE ELSEQIRALE DLKTLGTIYG FDISRPAADV
KEAIQWTYFG YLAAVKEQNG AAMSLGRTST FLDIYAERDL REGRYTEAQV QEFVDHFIMK
LRLVKFARTP EYNDLFSGDP TWVTESIGGI GIDGRHMVTK MSYRYLHTLH NLGTAPEPNL
TVLWSTRLPE NFKRFCAKTS IESSSIQYEN DDLMRTTHGD DYAIACCVSS MRVGKEMQFF
GARANLAKCL LYAINGGVDE ITGKQVGPKY RPITSEYLDF DEVMDKYKDM MKWLAKVYVN
ALNIIHYNHD KYSYERLQMA LHDKKVVRWF ATGIAGLSVV ADSLSAIKYA KVKTVRNEKG
IVTDYIVEGD FPKYGNNDDR VDQLAADLVH IFMSYIKGNH TYRGGIPTTS ILTITSNVVY
GKNTGSTPDG RKGGQPFAPG ANPMHHRDSH GAIASLASVA KLPFRDAQDG ISNTFSIIPG
ALGKDDQIFM GDLEVELSSC PSCDMGGNLF EGLDSESDIE ES
//
