ID F7JNS6_9FIRM Unreviewed; 750 AA.
AC F7JNS6;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 24-JAN-2024, entry version 52.
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=HMPREF0988_01980 {ECO:0000313|EMBL:EGN36979.1};
OS Lachnospiraceae bacterium 1_4_56FAA.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=658655 {ECO:0000313|EMBL:EGN36979.1, ECO:0000313|Proteomes:UP000004289};
RN [1] {ECO:0000313|EMBL:EGN36979.1, ECO:0000313|Proteomes:UP000004289}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1_4_56FAA {ECO:0000313|EMBL:EGN36979.1,
RC ECO:0000313|Proteomes:UP000004289};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Strauss J.,
RA Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Brown A.,
RA Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., Larson L., Lui A.,
RA MacDonald P.J.P., Mehta T., Montmayeur A., Murphy C., Neiman D.,
RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P.,
RA Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Lachnospiraceae bacterium 1_4_56FAA.";
RL Submitted (MAY-2011) 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|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:EGN36979.1}.
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; ACTN01000012; EGN36979.1; -; Genomic_DNA.
DR RefSeq; WP_009267925.1; NZ_JADMSO010000020.1.
DR AlphaFoldDB; F7JNS6; -.
DR STRING; 658655.HMPREF0988_01980; -.
DR GeneID; 82441745; -.
DR PATRIC; fig|658655.3.peg.2016; -.
DR eggNOG; COG1882; Bacteria.
DR HOGENOM; CLU_023898_0_0_9; -.
DR OrthoDB; 9803969at2; -.
DR UniPathway; UPA00920; UER00891.
DR Proteomes; UP000004289; 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:SF8; FORMATE ACETYLTRANSFERASE; 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:UP000004289};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU368075}.
FT DOMAIN 1..618
FT /note="PFL"
FT /evidence="ECO:0000259|PROSITE:PS51554"
FT DOMAIN 625..750
FT /note="Glycine radical"
FT /evidence="ECO:0000259|PROSITE:PS51149"
FT ACT_SITE 412
FT /note="S-acetylcysteine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000379-1"
FT ACT_SITE 413
FT /note="Cysteine radical intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000379-1"
FT MOD_RES 725
FT /note="Glycine radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR000379-2,
FT ECO:0000256|PROSITE-ProRule:PRU00493"
SQ SEQUENCE 750 AA; 85132 MW; 206DFB6DD644B428 CRC64;
MPNFEQWEGF AGKNWRNSVD VRDFIQENYT PYEGDESFLE GPTEATDKLW GRLQELQKEE
RAKGGVLDME TEVVSGLTAY GPGYIDDSMK DLEQVVGLQT DKPLKRAFMP YGGINMAVKA
CTTYGYEPSE RLKEIFTKYH KTHNQGVFDI YTPEMKKARH NKIITGLPDT YGRGRIVGDY
RRVALYGIDF LIEKKQYDFE RYARHGMKGT DFRLREEIAD QIRALQQMKE MAAIYGYDIS
KPAKDAKEAV QWLYFGYLAA IKTQNGAAMS VGRISTFLDI YIERDMKAGK LTESEAQELI
DHIVMKFRMV KFARVPSYNE LFSGDPVWAT LEMAGLGQDG RSMVTKNDYR FLHTLENMGP
SPEPNLTVLY SERLPENFKN YASLISVKTS SVQYENDDVM RPVWGDDYSI CCCVSATQTG
KEIQFFGARA NLAKCLLYAI NGGVDEKTKV QVSPAYRPIT SEYLDYDEVM EKYDEMMEWL
SKLYVDTLNM IHYMHDKYYY EAAEMALIDT DVRRTFATGI AGFSHVVDSL SAIKYAKVKV
IRDEDGIATD FEVEGDFPRY GNDDDRADDI AIWLLKTFMH KLSKCHTYRD SEPTTSILTI
TSNVVYGKAT GTLPDGRKAG EPLSPGANPS YGAEKNGLLA SLNSVAKLPY ELALDGISNT
QTISPSALGH DDEERKVNLT RVMDGYFRQG AHHLNVNVFG TDKLIDAMEH PEKPEYANFT
IRVSGYAVKF IDLTREQQLD VIARTCHESM
//
