ID A0A1E8EUW9_9CLOT Unreviewed; 748 AA.
AC A0A1E8EUW9;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
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:OFH98018.1};
GN ORFNames=CLOACE_22810 {ECO:0000313|EMBL:OFH98018.1};
OS Clostridium acetireducens DSM 10703.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1121290 {ECO:0000313|EMBL:OFH98018.1, ECO:0000313|Proteomes:UP000175744};
RN [1] {ECO:0000313|EMBL:OFH98018.1, ECO:0000313|Proteomes:UP000175744}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10703 {ECO:0000313|EMBL:OFH98018.1,
RC ECO:0000313|Proteomes:UP000175744};
RA Poehlein A., Fluechter S., Duerre P., Daniel R.;
RT "Genome sequence of Clostridium acetireducens DSM 10703.";
RL Submitted (JUN-2016) 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: 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:OFH98018.1}.
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DR EMBL; LZFO01000065; OFH98018.1; -; Genomic_DNA.
DR RefSeq; WP_070111374.1; NZ_LZFO01000065.1.
DR AlphaFoldDB; A0A1E8EUW9; -.
DR STRING; 1121290.CLAOCE_22810; -.
DR PATRIC; fig|1121290.3.peg.2306; -.
DR OrthoDB; 9803969at2; -.
DR UniPathway; UPA00920; UER00891.
DR Proteomes; UP000175744; 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; 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};
KW Organic radical {ECO:0000256|ARBA:ARBA00022818,
KW ECO:0000256|PIRSR:PIRSR000379-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000175744};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU368075}.
FT DOMAIN 1..617
FT /note="PFL"
FT /evidence="ECO:0000259|PROSITE:PS51554"
FT DOMAIN 624..748
FT /note="Glycine radical"
FT /evidence="ECO:0000259|PROSITE:PS51149"
FT ACT_SITE 405
FT /note="S-acetylcysteine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000379-1"
FT ACT_SITE 406
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; 85210 MW; 39B1CD592E225D88 CRC64;
MTHLWQGFRE GHWLEDIDVR DFIQKNYKLY EGDNSFLVGI TEKTKKVWDK AYKLIIKEIK
QGIMDIETEK FSGVDKFEAG YIDKDNEVIV GFQTDEPLKR IMNPYGGMRM VEQSLEEYGY
KMNSDLEKYF KEFRKTHNEG VFDAYTEETK VARHVGLLTG LPDAYGRGRI IGDYRRIALY
GIDYLIEKKK EDFKNLKGSA TEEMIRLREE VSEQIKAMHK IKNMAKVYDI DLSKPAKNAK
EAVQFLYMGY LAGVKEDNGA AMSLGRVSTF LDIYIERDLK EGIITEEEAQ ELIDQFVIKL
RLVRHLRTPE YNELFGGDPN WITEAIGGVS LNGKPLVTKT SYRFLHTLTN LGPAPEPNMT
VLWSEKLPES FKKYCAEMSI KTDSIQYEND DLMRPIYGDD YAIACCVSAM QVGKQMQFFG
ARANVAKSLL YAINGGIDER LKDKQGNLIK VVPGIDKIED EVLDFEKVRK NYWKVLDYVT
ELYVNTMNTI HYMHDKYAYE SAQMALHDTK VHIFMAFGIA GLSCAADSLS AMKYAKVKPI
RDENGIAVDF EIEGDFPKYG NDDDRVDDIA VQIVKNFSSG LKKNQTYRNA EHTLSALTIT
SNVVYGKKTG ATPDGRKAGE PLAPGANPMH GRDVNGALAS LNTVAKIPYR YWCQDGVSNT
FSIVPEALGK SIENQIENLV SLLDGYFSQS AFHLNVNVLR RETLIDAMKN PEKYPTLTIR
VSGYAVHFNR LSKDQQLEVI KRTFHEKM
//
