ID A0A1U7NNY3_9FIRM Unreviewed; 748 AA.
AC A0A1U7NNY3;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-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=BO225_03900 {ECO:0000313|EMBL:OLU47049.1};
OS Dubosiella newyorkensis.
OC Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC Erysipelotrichaceae; Dubosiella.
OX NCBI_TaxID=1862672 {ECO:0000313|EMBL:OLU47049.1, ECO:0000313|Proteomes:UP000186705};
RN [1] {ECO:0000313|EMBL:OLU47049.1, ECO:0000313|Proteomes:UP000186705}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NYU-BL-A4 {ECO:0000313|EMBL:OLU47049.1,
RC ECO:0000313|Proteomes:UP000186705};
RA Cox L.M., Sohn J., Tyrrell K.L., Citron D.M., Lawson P.A., Patel N.B.,
RA Iizumi T., Perez-Perez G.I., Goldstein E.J., Blaser M.J.;
RT "Description of two novel members of the family Erysipelotrichaceae:
RT Ileibacterium lipovorans gen. nov., sp. nov. and Dubosiella newyorkensis,
RT gen. nov., sp. nov.";
RL Submitted (NOV-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:OLU47049.1}.
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DR EMBL; MPKA01000055; OLU47049.1; -; Genomic_DNA.
DR RefSeq; WP_076340973.1; NZ_MPKA01000055.1.
DR AlphaFoldDB; A0A1U7NNY3; -.
DR STRING; 1862672.BO225_03900; -.
DR GeneID; 78275091; -.
DR OrthoDB; 9803969at2; -.
DR UniPathway; UPA00920; UER00891.
DR Proteomes; UP000186705; 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:UP000186705};
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; 84982 MW; 633D5D7D8AEA4A15 CRC64;
MREQWRSFQG TKWQEEVDVR DFIQKNYTPY DDDETFLSDP TEATNALWSK LQELQKEERA
KGGVLDMETE IVSSLTAYGP GYINEELKEL EQIVGLQTDR PLKRAFMPYG GIRMSEEACT
TYDYTPSEKL HEIFTKYHKT HNDAVFSAYT PEMRLARKNK IVTGLPDTYG RGRIVGDYRR
VALYGIDFLI KEKEEDLAYC GDGVMSDDVI RQREEIAEQI KALKGMKEMA AMYGYDISKP
ANNAREAAQW LYFGYLAAIK TQNGAAMSVG RISTFLDIYF ERDLKEGTLT EQEAQEIIDH
MTMKFRMVKF ARIPSYNQLF SGDPVWATLD VAGLGTDGRS MVTKTCFRFL HTLENMGPSP
EPNLTVLYSS RLPEPFKLYA AKVSIDTSSV QYENDEVMRV EWGDDYAVCC CVSATQTGKE
MQFFGARANL AKCLLYAING GVDEKTKMQV GPEYKPITSE YLDYKEVMHK YDQMMEWLAG
LYVNILNLIQ YFHDKYYYEA SQMALIDTDV RRTFATGIAG FSHVVDSLSA IKYAKVKTIR
DEDGLVIDYE IEGDFPRYGN DDDRADEIAI WLLKEFMKKI RKHHTYRNSE PTTSILTITS
NVVYGKATGA LPDGRKAGEP LSPGANPAYG AEQNGLLASL NSVAKLPYEY ALDGISNTQT
MNPSALGHDP LERIENLVHV LDGYFDQGAH HLNVNVFGVE KLIDAMEHPE KEEYANFTIR
VSGYAVKFID LTREQQLDVI SRTCHSSL
//