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Database: UniProt
Entry: A0A1U7NNY3_9FIRM
LinkDB: A0A1U7NNY3_9FIRM
Original site: A0A1U7NNY3_9FIRM 
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
//
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