ID C6Q323_9CLOT Unreviewed; 422 AA.
AC C6Q323;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=formate C-acetyltransferase {ECO:0000256|ARBA:ARBA00013214};
DE EC=2.3.1.54 {ECO:0000256|ARBA:ARBA00013214};
DE Flags: Fragment;
GN ORFNames=CcarbDRAFT_5442 {ECO:0000313|EMBL:EET84108.1};
OS Clostridium carboxidivorans P7.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=536227 {ECO:0000313|EMBL:EET84108.1, ECO:0000313|Proteomes:UP000004198};
RN [1] {ECO:0000313|EMBL:EET84108.1, ECO:0000313|Proteomes:UP000004198}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P7 {ECO:0000313|EMBL:EET84108.1,
RC ECO:0000313|Proteomes:UP000004198};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Larimer F., Land M.L., Hauser L., Hemme C.L.;
RT "The draft genome of Clostridium carboxidivorans P7.";
RL Submitted (JUN-2009) 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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the glycyl radical enzyme (GRE) family. PFL
CC subfamily. {ECO:0000256|ARBA:ARBA00008375}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00493}.
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:EET84108.1}.
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DR EMBL; ACVI01000234; EET84108.1; -; Genomic_DNA.
DR AlphaFoldDB; C6Q323; -.
DR eggNOG; COG1882; Bacteria.
DR Proteomes; UP000004198; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008861; F:formate C-acetyltransferase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.20.70.20; -; 1.
DR InterPro; IPR001150; Gly_radical.
DR InterPro; IPR004184; PFL_dom.
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 SUPFAM; SSF51998; PFL-like glycyl radical enzymes; 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:0000313|EMBL:EET84108.1}; Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Organic radical {ECO:0000256|ARBA:ARBA00022818};
KW Reference proteome {ECO:0000313|Proteomes:UP000004198};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EET84108.1}.
FT DOMAIN 1..388
FT /note="PFL"
FT /evidence="ECO:0000259|PROSITE:PS51554"
FT DOMAIN 395..422
FT /note="Glycine radical"
FT /evidence="ECO:0000259|PROSITE:PS51149"
FT REGION 379..409
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EET84108.1"
FT NON_TER 422
FT /evidence="ECO:0000313|EMBL:EET84108.1"
SQ SEQUENCE 422 AA; 46929 MW; 0B83F85B0B7DAED8 CRC64;
IDISKPASNA VEAAQFLYFG YLAGVKENNG AAMSIGRNTT FLDIYIERDL KSGIITEAEA
QEIIDQLVIK LRMVRHLRTP EYNDLFAGDP NWVTESIGGI GVNGKSLVTK TAYRFLHTLT
NLGPAPEPNM TVLWSEKLPQ NFKNYCAEMS IKTDSLQYEN DDIMRPIYGD DYGIACCVSA
MEIGKRMQFF GARANLAKSL LYAINGGYDE KKKAKDGSLI KVVPDIEKME DEVLDFNKVV
KSYNKVMEYV AELYVDTMNT IHYMHDKYAY ESGQMALHDT AVKRFMAFGI AGLSVAADSL
SAIKYAKVKP IRNEDGITVD FEIEGNFPKY GNDDDRVDDL AVQLVKKFSN ELKKHKTYRD
AEHSLSVLTI TSNVVYGKKT GTTPDGRKVG EPLAPGANPM HGRDENGALA SLNSVAKIPY
RT
//
