ID R6D9V2_9BACE Unreviewed; 740 AA.
AC R6D9V2;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 35.
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=BN697_01317 {ECO:0000313|EMBL:CDA74632.1};
OS Bacteroides sp. CAG:530.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=1262741 {ECO:0000313|EMBL:CDA74632.1, ECO:0000313|Proteomes:UP000018392};
RN [1] {ECO:0000313|EMBL:CDA74632.1, ECO:0000313|Proteomes:UP000018392}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:530 {ECO:0000313|Proteomes:UP000018392};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) 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:CDA74632.1}.
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DR EMBL; CBCL010000006; CDA74632.1; -; Genomic_DNA.
DR AlphaFoldDB; R6D9V2; -.
DR UniPathway; UPA00920; UER00891.
DR Proteomes; UP000018392; 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:UP000018392};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU368075}.
FT DOMAIN 1..610
FT /note="PFL"
FT /evidence="ECO:0000259|PROSITE:PS51554"
FT DOMAIN 617..740
FT /note="Glycine radical"
FT /evidence="ECO:0000259|PROSITE:PS51149"
FT ACT_SITE 404
FT /note="S-acetylcysteine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000379-1"
FT ACT_SITE 405
FT /note="Cysteine radical intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000379-1"
FT MOD_RES 715
FT /note="Glycine radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR000379-2,
FT ECO:0000256|PROSITE-ProRule:PRU00493"
SQ SEQUENCE 740 AA; 83386 MW; 7D5888CC6E81EBB8 CRC64;
MTQNFKEGRW NHEINVTDFV KTNITPYTGD ASFLVGPTQR TQAVWNKCLE ALAEERANNG
VRSLDPSTVS TITSFAAGYI DKENEVIVGL QTDEVLRRAI KPFGGIKVVE KACRENGVEV
DPHVKDIFTH YRKTHNDGVF DAYTEEIRSF RSLGFLTGLP DNYARGRVIG DYRRLALYGL
DRLIEVKQND LRDLTGPMTD ARIRLREEVA EQIKALKEIK IMGQQYGLDL SRPAYTAQEA
VQWVYMAYLA AVKEQDGAAM SLGNVSSFLD IYIEYDMHNG TLDETHAQEL IDQFVIKLRM
VRHLRMQAYT DIFAGDPTWV TESLGGRFND GRTKVTKTSF RFLQTLYNLG PSPEPNLTVL
WSPELPEGFK NFCAQVSIDT SSIQYENDDL MREVRNSDDY GIACCVSYQD IGRHIQFFGA
RCNLAKALLL AINGGRCENT GTLMVKDIPA LTGDVLNFEE VLANYKKVLH EVARVYNEAM
NIIHYMHDKY YYEKAQMAFV DTDPVINLAY GVAGMSIAVD SLSAIKYAKV TARRNEQGLT
EGFDIEGEFP CFGNDDDRVD HLAVDLIYYF DEELKKLPVY KNAKPTLSIL TITSNVMYGK
KTGATPDGRA KGVAFAPGAN PMHGRDKNGA VASLSSVAKL RYRDSQDGIS NTFSIVPKSL
GVDLETRIEN LVTMMDGYFV KGAHHLNVNV LNREMLEDAM VHPEKYPQLT IRVSGYAVNF
IKLSREHQLE VISRSFHERF
//
