ID A0A3N2BFW9_9MICO Unreviewed; 752 AA.
AC A0A3N2BFW9;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Formate acetyltransferase {ECO:0000256|RuleBase:RU368075};
DE EC=2.3.1.54 {ECO:0000256|RuleBase:RU368075};
DE AltName: Full=Pyruvate formate-lyase {ECO:0000256|RuleBase:RU368075};
GN ORFNames=EDD31_2537 {ECO:0000313|EMBL:ROR74137.1};
OS Bogoriella caseilytica.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Bogoriellaceae;
OC Bogoriella.
OX NCBI_TaxID=56055 {ECO:0000313|EMBL:ROR74137.1, ECO:0000313|Proteomes:UP000280668};
RN [1] {ECO:0000313|EMBL:ROR74137.1, ECO:0000313|Proteomes:UP000280668}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11294 {ECO:0000313|EMBL:ROR74137.1,
RC ECO:0000313|Proteomes:UP000280668};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (NOV-2018) 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|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:ROR74137.1}.
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; RKHK01000001; ROR74137.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N2BFW9; -.
DR OrthoDB; 9803969at2; -.
DR UniPathway; UPA00920; UER00891.
DR Proteomes; UP000280668; 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|RuleBase:RU368075};
KW Organic radical {ECO:0000256|ARBA:ARBA00022818,
KW ECO:0000256|PIRSR:PIRSR000379-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000280668};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU368075}.
FT DOMAIN 9..622
FT /note="PFL"
FT /evidence="ECO:0000259|PROSITE:PS51554"
FT DOMAIN 629..752
FT /note="Glycine radical"
FT /evidence="ECO:0000259|PROSITE:PS51149"
FT ACT_SITE 416
FT /note="S-acetylcysteine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000379-1"
FT ACT_SITE 417
FT /note="Cysteine radical intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000379-1"
FT MOD_RES 727
FT /note="Glycine radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR000379-2,
FT ECO:0000256|PROSITE-ProRule:PRU00493"
SQ SEQUENCE 752 AA; 83213 MW; E4489EA250E2DE4C CRC64;
MATTASTDAR ATTAWRGFHP GPWQEGVDVR DFIQRNYAPY DGESDFLAGA TERTTALWQR
LSDMFPTERE RGVYDIDATT PSTITSHAPG YIDRDSELIV GLQTDAPLKR AIMPFGGWRM
VATALTTYGF EVDPSLEEVF TRYRKTHNDG VFDVYPPEVR AARRSHLVTG LPDAYGRGRI
IGDYRRVALY GVDALIAAKG DERVLLDAKR STEDVIRDRE ENAEQIKALR ELKEMAAGYG
HDIGRPAANG REAVQWVYLA YLAAVKEQNG AAMSLGRVST FLDVYLQRDL DEGALTETQA
QELIDDFVIK LRIVRFLRTP EYDQLFSGDP TWVTESIGGI GEDGRHLVTK SSFRFLQTLY
NLGPAPEPNL TVLWSDALPE GFKRFCAAAS IDTSAIQYES DALIRSQSGD DAGIACCVSA
MTIGKQMQFF GARVNLAKAL LYAINGGRDE VSGAQVAPVS TTITSEVLDY DEVLDAYDML
LDWLAETYVD ALNCIHYMHD KYAYERIEMA LHDGDILRTM ACGIAGLSVA ADSLSAIKYA
EVRPIRDESG LVTDYAVEGE FPTFGNDDDR VDDIATMLVE RFMEKVRRVP TYRNAKHTQS
VLTITSNVVY GKHTGNTPDG RRAGEPFAPG ANPMNGRDTH GMLASALSVA KLPYDQAQDG
ISLTSTVVPS GLGRTREEQV THLAGLLDAY MGAQGFHMNV NVLNRDTLED AMEHPENYPQ
LTIRVSGYAV NFVRLTREQQ RDVISRTFHG SV
//
