ID A0A0A1MKQ1_9BACI Unreviewed; 751 AA.
AC A0A0A1MKQ1;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 24-JAN-2024, entry version 30.
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:CEI80277.1};
GN ORFNames=BN997_00076 {ECO:0000313|EMBL:CEI80277.1};
OS Oceanobacillus oncorhynchi.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Oceanobacillus.
OX NCBI_TaxID=545501 {ECO:0000313|EMBL:CEI80277.1, ECO:0000313|Proteomes:UP000040453};
RN [1] {ECO:0000313|EMBL:CEI80277.1, ECO:0000313|Proteomes:UP000040453}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Oc5 {ECO:0000313|EMBL:CEI80277.1,
RC ECO:0000313|Proteomes:UP000040453};
RA Urmite Genomes Urmite Genomes;
RL Submitted (NOV-2014) 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}.
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DR EMBL; CDGG01000001; CEI80277.1; -; Genomic_DNA.
DR RefSeq; WP_042528618.1; NZ_CDGG01000001.1.
DR AlphaFoldDB; A0A0A1MKQ1; -.
DR STRING; 545501.BN997_00076; -.
DR OrthoDB; 9803969at2; -.
DR UniPathway; UPA00920; UER00891.
DR Proteomes; UP000040453; 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:UP000040453};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU368075}.
FT DOMAIN 7..621
FT /note="PFL"
FT /evidence="ECO:0000259|PROSITE:PS51554"
FT DOMAIN 628..751
FT /note="Glycine radical"
FT /evidence="ECO:0000259|PROSITE:PS51149"
FT ACT_SITE 415
FT /note="S-acetylcysteine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000379-1"
FT ACT_SITE 416
FT /note="Cysteine radical intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000379-1"
FT MOD_RES 726
FT /note="Glycine radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR000379-2,
FT ECO:0000256|PROSITE-ProRule:PRU00493"
SQ SEQUENCE 751 AA; 84817 MW; A500CC8F17323473 CRC64;
MKVADEMVKR VPWDGFVEGN WQQEIDVRDF ILQNYHLYEG NESFLTDATQ ATKDLWEQVM
QLTREERENG GVYDLDTKIV STITSHGAGY LNKPLEKIIG VQTDAPFKRA LMPFGGIRMA
VAAAESYGYK VDDDVVHTFT EHRKTHNQGV FDAYTPEILK ARKAGIITGL PDAYGRGRII
GDYRRVALYG VDRLIEEKKK DLQLIGNGTM TDDVIRDREE TSEQIRSLMD LKKLGEKYEF
DLSKPATTAQ EAFQWLYLAY LAAIKEQNGA AMSLGRVSTF LDIYIERDIE NGVMTEQEAQ
ELVDHFVMKL RLVKFARTPD YNELFSGDPT WVTESLAGIA EDGRPLVTKS SYRFLHTLDN
LGPAPEPNLT VLWSAKLPEN YKKYCAKMSI KSSSIQYEND DIMRPIYGDD YGIACCVSAM
RIGKQMQFFG ARANLAKALL YAINGGVDEN LKMQVAPNYA PITSEYLDYD EVMEKYDNLL
DWLSGLYVNA LNIIHYMHDK YSYERLEMAL HDREVLRTMA CGVAGLSVIV DSLSAIKYAK
VRTIRDEDGL VVDYEIEGDY PKYGNNDDRA DEIAVSLVKD FMNKIKKHHM YRDATPTQSI
LTITSNVVYG KKTGNTPDGR KAGEPFAPGA NPLHGRDKNG SLASLSSVAK LPYKYALDGI
SNTFSIVPKA LGKDEETRKT NLAGILDGYA AKKGHHLNIN VFDRETLLDA MEHPEEYPQL
TIRVSGYAVN FIKLTREQQI DVINRTFHES L
//
