ID A0A1L8SWN4_9ENTE Unreviewed; 765 AA.
AC A0A1L8SWN4;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
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 ORFNames=RV00_GL001613 {ECO:0000313|EMBL:OJG36254.1};
OS Enterococcus devriesei.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=319970 {ECO:0000313|EMBL:OJG36254.1, ECO:0000313|Proteomes:UP000183700};
RN [1] {ECO:0000313|EMBL:OJG36254.1, ECO:0000313|Proteomes:UP000183700}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22802 {ECO:0000313|EMBL:OJG36254.1,
RC ECO:0000313|Proteomes:UP000183700};
RA Zhong Z., Sun Z., Liu W., Zhang W., Zhang H.;
RT "Draft genome sequences of 29 type strains of Enterococci.";
RL Submitted (DEC-2014) 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:OJG36254.1}.
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DR EMBL; JXKM01000003; OJG36254.1; -; Genomic_DNA.
DR RefSeq; WP_071861503.1; NZ_JXKM01000003.1.
DR AlphaFoldDB; A0A1L8SWN4; -.
DR STRING; 319970.RV00_GL001613; -.
DR OrthoDB; 9803969at2; -.
DR UniPathway; UPA00920; UER00891.
DR Proteomes; UP000183700; 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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU368075}.
FT DOMAIN 11..626
FT /note="PFL"
FT /evidence="ECO:0000259|PROSITE:PS51554"
FT DOMAIN 638..765
FT /note="Glycine radical"
FT /evidence="ECO:0000259|PROSITE:PS51149"
FT ACT_SITE 420
FT /note="S-acetylcysteine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000379-1"
FT ACT_SITE 421
FT /note="Cysteine radical intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000379-1"
FT MOD_RES 740
FT /note="Glycine radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR000379-2,
FT ECO:0000256|PROSITE-ProRule:PRU00493"
SQ SEQUENCE 765 AA; 86359 MW; 18ABC520B2D2EDA3 CRC64;
METTTIDKTV KQTNSPWEGF NEGRWQHEVN TLDFIKRNYT EYKGDDSFLE AAAPSTEKLW
EKLQELFEVQ HKKNGVYDMD SDVPATITSH APGYLIKEEE KIVGLQTDVP LKQAFMPFGG
INMANKALES NGYDVDDEMS FIFNKWRKTH NQGVFDAYTD EMRLARKNKI ITGLPDAYGR
GRIIGDYRRV ALYGIDFLMK EKKKDWKNVG SKVMTNDVIQ LREEVSEQYR ALLDMKEMAA
SYGYDISKPA ANAQEAIQWL YFGYLAAIKS QNGAAMSIGR ISAFLDIYIQ RDLNNGVITE
FEAQEMIDHL IMKLRMVKFA RTPEYNQLFS GYPIWATLSL AGMNMDGSSL VTKNDFRILH
TLTNMGPSPE PNLTVLYSSH LPEGFRTYAA KVAKVSSSIQ LENDDLLRQH WGSDDAAIAC
CVSATVIGKD MQFFGARANL AKAVLYAING GVDEMTKMQV GPRFRPLEGD SIDFNQFMDS
YKDVLDWLAE LYVNTLNVIH YMHDKYAYEA PQLALMDTDL KRTFATGIAG ISHATDSLMA
IKHGNVKVIR DENGLAIDYV PQNEFPTYGN DNDEADEMAN WILEYFMTQI KRQHTYREST
PTLSLLTITS NVVYGKNTGN TPDGRRAGKP LAPGANPSYQ DGKFLGEKNG LLASLNSTAK
LNYSCAQDGI SDTQTINPGA LGRTDDEAMQ VDNLRQVLDG YFDRGGYHLN VNVFGRELLE
EMDKDIDNPK YANFTIRVSG YAVKFRDLTA EQRRDVISRT DHTKM
//
