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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//