ID A0A430ARE1_9ENTE Unreviewed; 748 AA.
AC A0A430ARE1;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 08-NOV-2023, entry version 16.
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=CBF27_09910 {ECO:0000313|EMBL:RSU10624.1};
OS Vagococcus acidifermentans.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae; Vagococcus.
OX NCBI_TaxID=564710 {ECO:0000313|EMBL:RSU10624.1, ECO:0000313|Proteomes:UP000286773};
RN [1] {ECO:0000313|EMBL:RSU10624.1, ECO:0000313|Proteomes:UP000286773}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 24798 {ECO:0000313|EMBL:RSU10624.1,
RC ECO:0000313|Proteomes:UP000286773};
RA Gulvik C.A.;
RT "Vagococcus spp. assemblies.";
RL Submitted (MAY-2017) 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:RSU10624.1}.
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DR EMBL; NGKC01000011; RSU10624.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A430ARE1; -.
DR OrthoDB; 9803969at2; -.
DR UniPathway; UPA00920; UER00891.
DR Proteomes; UP000286773; 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:UP000286773};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU368075}.
FT DOMAIN 1..613
FT /note="PFL"
FT /evidence="ECO:0000259|PROSITE:PS51554"
FT DOMAIN 625..748
FT /note="Glycine radical"
FT /evidence="ECO:0000259|PROSITE:PS51149"
FT REGION 606..627
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 407
FT /note="S-acetylcysteine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000379-1"
FT ACT_SITE 408
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; 84126 MW; F3A5B506F38E1F91 CRC64;
MGHWDGFKGT KWRDHVNVRD FIQNNYTEYT GDDSFLEPAA PSTDKLWTKL QELFEVQHEN
NGVYDMDNNI PSTITSHEPG YLIKEEETIV GLQTDVPLKQ AFMPFGGINM ANNALKTNGY
DVDEDMTKIF TEWRKTHNQG VFDAYTPEMR AARSNKIITG LPDAYGRGRI IGDYRRLALY
GIDFLIAEKK KDLANVGNKV MTDDVIRLRE EVSEQIKALN DIKEMATYYG FDVSQPAKNA
QEAIQWTYFG YLAAIKSQNG AAMSIGRISA FLDIYIQRDL DNGVITEFEA QEMIDHLIMK
LRMVKFARTP EYNELFSGYP IWATLSIAGM GVDGRSLVTK NDFRILHTLV NMGPSPEPNL
TVLYSSRLPE GFRTFAARIA KESSSIQFEN DDLLRANWGS DDCAIACCVS ATVMGKDMQF
FGARANLAKT VLYAINGGVD EITKKQVGPK FRPMTGDKLD YDEFIDRYKD MMDWLAELYV
NTLNVIHYMH DKYAYEAPQL AFMDTHLKRT FATGIAGISH AADSLMAIKH GDVKVIRDED
GLAIDYVPTK EFPTYGNDSE EADAAANWIL EYFMTQIKRQ HTYRNSTPTT SLLTITSNVV
YGKATGNTPD GRRAGKPLAP GANPSYQDGK YLGEKNGLLA SLNSTARLEY QCALDGISNT
QTINPNGLGK DDDTRIDNLR NVMDGYFDKG GYHLNVNVFT TDLLLDAQAH PEKYPNLTIR
VSGYAVKFRD LTPEQQADVI SRTAHDRM
//
