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Database: UniProt
Entry: A0A377KMD0_9ENTE
LinkDB: A0A377KMD0_9ENTE
Original site: A0A377KMD0_9ENTE 
ID   A0A377KMD0_9ENTE        Unreviewed;       743 AA.
AC   A0A377KMD0;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 28.
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:STP29912.1};
GN   ORFNames=EA71_01074 {ECO:0000313|EMBL:RCA10324.1}, GUJ97_00185
GN   {ECO:0000313|EMBL:NAA79026.1}, NCTC8129_02143
GN   {ECO:0000313|EMBL:STP29912.1};
OS   Enterococcus durans.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=53345 {ECO:0000313|EMBL:STP29912.1, ECO:0000313|Proteomes:UP000254070};
RN   [1] {ECO:0000313|EMBL:RCA10324.1, ECO:0000313|Proteomes:UP000252797}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=4EA1 {ECO:0000313|EMBL:RCA10324.1,
RC   ECO:0000313|Proteomes:UP000252797};
RG   The Broad Institute Genomics Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Earl A.M., Van Tyne D., Lebreton F., Saavedra J.T., Gilmore M.S.,
RA   Manson Mcguire A., Clock S., Crupain M., Rangan U., Young S.,
RA   Abouelleil A., Cao P., Chapman S.B., Griggs A., Priest M., Shea T.,
RA   Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Enterococcus durans 4EA1.";
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:STP29912.1, ECO:0000313|Proteomes:UP000254070}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC8129 {ECO:0000313|EMBL:STP29912.1,
RC   ECO:0000313|Proteomes:UP000254070};
RG   Pathogen Informatics;
RA   Doyle S.;
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:NAA79026.1, ECO:0000313|Proteomes:UP000444134}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BIOML-A60 {ECO:0000313|EMBL:NAA79026.1,
RC   ECO:0000313|Proteomes:UP000444134};
RX   PubMed=31477907; DOI=.1038/s41591-019-0559-3;
RA   Poyet M., Groussin M., Gibbons S.M., Avila-Pacheco J., Jiang X.,
RA   Kearney S.M., Perrotta A.R., Berdy B., Zhao S., Lieberman T.D.,
RA   Swanson P.K., Smith M., Roesemann S., Alexander J.E., Rich S.A., Livny J.,
RA   Vlamakis H., Clish C., Bullock K., Deik A., Scott J., Pierce K.A.,
RA   Xavier R.J., Alm E.J.;
RT   "A library of human gut bacterial isolates paired with longitudinal
RT   multiomics data enables mechanistic microbiome research.";
RL   Nat. Med. 25:1442-1452(2019).
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}.
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DR   EMBL; WXTH01000001; NAA79026.1; -; Genomic_DNA.
DR   EMBL; LEPB01000004; RCA10324.1; -; Genomic_DNA.
DR   EMBL; UGIF01000002; STP29912.1; -; Genomic_DNA.
DR   RefSeq; WP_005878172.1; NZ_WXTW01000001.1.
DR   STRING; 53345.LIU_06625; -.
DR   GeneID; 56743713; -.
DR   UniPathway; UPA00920; UER00891.
DR   Proteomes; UP000252797; Unassembled WGS sequence.
DR   Proteomes; UP000254070; Unassembled WGS sequence.
DR   Proteomes; UP000444134; 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          1..613
FT                   /note="PFL"
FT                   /evidence="ECO:0000259|PROSITE:PS51554"
FT   DOMAIN          620..743
FT                   /note="Glycine radical"
FT                   /evidence="ECO:0000259|PROSITE:PS51149"
FT   REGION          603..625
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         718
FT                   /note="Glycine radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000379-2,
FT                   ECO:0000256|PROSITE-ProRule:PRU00493"
SQ   SEQUENCE   743 AA;  83795 MW;  B5A2C0B607A9EC22 CRC64;
     MEQWNGFKGT KWKEGVDTRD FIQNNYTEYR GDDSFLEKPT EATEKLWAEL QKLNDIQFER
     NGVYDMDTEI VSTITSHDAG YLDKDLEKVV GLQTDKPLKQ AFMPFGGINM ANNALKSNGY
     TPNDELTHIF TDWRKTHNQG VFDAYTAEMR AARKNKIITG LPDAYGRGRI IGDYRRIALY
     GIDYLMEQKK KDHDMTGYHT MSEDVIRLRE EITEQYRALA QMKEMAAKYG YDISKPAANA
     KEAVQWLYFG YLAAIKSQNG AAMSIGRVSA FLDIYIQRDL DNGVITEQEA QELIDHLVMK
     LRMVKFARTP EYNQLFSGFP IWATLSIAGM GLDGRSLVTK NDFRLLHTLT NMGPSPEPNL
     TVLYSEHLPE GFRTYASKIA IESSSIQFEN DNLLREQWGS DDCAIACCVS ATVVGKDMQF
     FGARANLAKA LLYAINGGVD EVTGAQVGPE YRPISSETLD FEEVKHNFMN VMDWLAELYV
     NTLNIIHYMH DKYSYEAAQL ALMDSELKRT FATGIAGISH AADSLAAIKY AKVKPIRNEK
     GIAVDFEVEG DFPKYGNDDD NADKLAEWIL EYFMTQIKRH KTYRNSTPTT SLLTITSNVV
     YGKNTGNTPD GREAGKPLAP GANPSYNAEQ NGLLASLNST AKINYAYARD GISNTQTINP
     TGLGKDEDTR IGNLRNVLDG YFSKGAYHLN VNVFSNDLLR DAMENPMKYP NLTIRVSGYA
     VKFRDLTREQ QLDVLMRTSH DRM
//
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