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Database: UniProt
Entry: A0A150LDR9_9BACI
LinkDB: A0A150LDR9_9BACI
Original site: A0A150LDR9_9BACI 
ID   A0A150LDR9_9BACI        Unreviewed;       743 AA.
AC   A0A150LDR9;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, 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   ORFNames=B4135_3545 {ECO:0000313|EMBL:KYD10370.1}, C6P37_14380
GN   {ECO:0000313|EMBL:REJ25826.1};
OS   Caldibacillus debilis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Caldibacillus.
OX   NCBI_TaxID=301148 {ECO:0000313|EMBL:KYD10370.1, ECO:0000313|Proteomes:UP000075683};
RN   [1] {ECO:0000313|EMBL:KYD10370.1, ECO:0000313|Proteomes:UP000075683}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B4135 {ECO:0000313|EMBL:KYD10370.1,
RC   ECO:0000313|Proteomes:UP000075683};
RA   Berendsen E.M., Wells-Bennik M.H., Krawcyk A.O., De Jong A., Holsappel S.,
RA   Eijlander R.T., Kuipers O.P.;
RT   "Draft Genome Sequences of Seven Thermophilic Sporeformers Isolated from
RT   Foods.";
RL   Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:REJ25826.1, ECO:0000313|Proteomes:UP000257014}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ZCTH4_d {ECO:0000313|EMBL:REJ25826.1};
RA   Keele B.F.;
RL   Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the conversion of pyruvate to formate and acetyl-
CC       CoA. {ECO:0000256|ARBA:ARBA00034302}.
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:KYD10370.1}.
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DR   EMBL; LQYT01000119; KYD10370.1; -; Genomic_DNA.
DR   EMBL; QEWE01000030; REJ25826.1; -; Genomic_DNA.
DR   RefSeq; WP_020153286.1; NZ_QEWE01000030.1.
DR   AlphaFoldDB; A0A150LDR9; -.
DR   STRING; 301148.B4135_3545; -.
DR   PATRIC; fig|301148.3.peg.1583; -.
DR   OrthoDB; 9803969at2; -.
DR   UniPathway; UPA00920; UER00891.
DR   Proteomes; UP000075683; Unassembled WGS sequence.
DR   Proteomes; UP000257014; 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:0016829; F:lyase activity; IEA:UniProtKB-KW.
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}; Lyase {ECO:0000313|EMBL:KYD10370.1};
KW   Organic radical {ECO:0000256|ARBA:ARBA00022818,
KW   ECO:0000256|PIRSR:PIRSR000379-2}; Pyruvate {ECO:0000313|EMBL:KYD10370.1};
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          605..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;  84180 MW;  57E18702E44CF452 CRC64;
     MNAWEGFKGG KWQEEIDVRD FILKNYTLYE GDESFLEGPT EATKKLWDQV MELSKKEREA
     GGVLDMDTKI VSTITSHGPG YLNKDLEKIV GFQTDKPFKR ALMPFGGIRM AVQAAESYGY
     KVDDEVKHIF TEYRKTHNQG VFDVYTPEMR LARKAGIITG LPDAYGRGRI IGDYRRVPLY
     GVDFLIEQKQ KDMALIGGDG VMTDDVIRDR EEHAEQIKAL QELKEMAKSY GFDISKPATN
     AREAIQWLYF AYLAAIKEQN GAAMSLGRVS TFLDIYIERD LQRGILTEKE AQELMDHFVM
     KLRLVKFART PEYNELFSGD PTWVTEAIGG VALDGRPLVT KNSFRILHTL DNLGPAPEPN
     LTVLWSVKLP ENFKRYCAKM SMKTSAIQYE NDDMMREIYG DDYGIACCVS AMRIGKQMQF
     FGARANLAKA LLYAINGGVD EKLKVQVGPA YSPITSEYLD YDEVMEKYDR MLDWLAGLYI
     NTLNVIHYMH DKYCYERLEM ALHDRDVIRT MACGVAGLSV VADSLSAIKY AKVRTIRDEN
     GIAVDYEVEG DFPKYGNNDD RVDQIAVELV KNFMNKLKKH KTYRNSIPTQ SILTITSNVV
     YGKKTGSTPD GRKAGQPFAP GANPMHGRDT KGALASLSSV SKLPYEYSLD GISNTFTVVP
     KALGRDEETR IQNLVSMLDG YMTKRGHHLN INVLNRETLL DAMDHPEKYP QLTIRVSGYA
     VNFIKLTREQ QIDVINRTFH QSM
//
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