ID D2TS40_CITRI Unreviewed; 760 AA.
AC D2TS40;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 76.
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 Name=pflB {ECO:0000313|EMBL:CBG87751.1};
GN OrderedLocusNames=ROD_09721 {ECO:0000313|EMBL:CBG87751.1};
OS Citrobacter rodentium (strain ICC168) (Citrobacter freundii biotype 4280).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Citrobacter.
OX NCBI_TaxID=637910 {ECO:0000313|EMBL:CBG87751.1, ECO:0000313|Proteomes:UP000001889};
RN [1] {ECO:0000313|EMBL:CBG87751.1, ECO:0000313|Proteomes:UP000001889}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ICC168 {ECO:0000313|EMBL:CBG87751.1,
RC ECO:0000313|Proteomes:UP000001889};
RX PubMed=19897651; DOI=10.1128/JB.01144-09;
RA Petty N.K., Bulgin R., Crepin V.F., Cerdeno-Tarraga A.M., Schroeder G.N.,
RA Quail M.A., Lennard N., Corton C., Barron A., Clark L., Toribio A.L.,
RA Parkhill J., Dougan G., Frankel G., Thomson N.R.;
RT "The Citrobacter rodentium genome sequence reveals convergent evolution
RT with human pathogenic Escherichia coli.";
RL J. Bacteriol. 192:525-538(2010).
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}.
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DR EMBL; FN543502; CBG87751.1; -; Genomic_DNA.
DR RefSeq; WP_012905296.1; NC_013716.1.
DR AlphaFoldDB; D2TS40; -.
DR STRING; 637910.ROD_09721; -.
DR KEGG; cro:ROD_09721; -.
DR eggNOG; COG1882; Bacteria.
DR HOGENOM; CLU_023898_0_0_6; -.
DR OrthoDB; 9803969at2; -.
DR UniPathway; UPA00920; UER00891.
DR Proteomes; UP000001889; Chromosome.
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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU368075}.
FT DOMAIN 3..625
FT /note="PFL"
FT /evidence="ECO:0000259|PROSITE:PS51554"
FT DOMAIN 632..760
FT /note="Glycine radical"
FT /evidence="ECO:0000259|PROSITE:PS51149"
FT ACT_SITE 419
FT /note="S-acetylcysteine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000379-1"
FT ACT_SITE 420
FT /note="Cysteine radical intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000379-1"
FT MOD_RES 735
FT /note="Glycine radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR000379-2,
FT ECO:0000256|PROSITE-ProRule:PRU00493"
SQ SEQUENCE 760 AA; 85035 MW; 9D397A64B46210B9 CRC64;
MSELNEKLAT AWEGFTKGDW QNEVNVRDFI QKNYTPYEGD ESFLAGATEA TTTLWDSVME
GVKQENRTHA PVDFDTSVAS TITSHDAGYI NKALEKIVGL QTEAPLKRAI IPFGGIKMVE
GSCKAYNREL DPMLKKIFTE YRKTHNQGVF DVYTPDILRC RKSGVLTGLP DAYGRGRIIG
DYRRVALYGI DYLMKDKFAQ FTSLQSDLEN GVNLEATIRL REEIAEQHRA LGQIKEMAAK
YGCDISGPAT NAQEAIQWTY FGYLAAVKSQ NGAAMSFGRV STFLDAYIER DLKAGKITEQ
DAQEMIDHLV MKLRMVRFLR TPEYDELFSG DPIWATESIG GMGVDGRTLV TKNSFRFLNT
LYTMGPSPEP NITVLWSEKL PLNFKKFAAK VSIDTSSLQY ENDDLMRPDF NNDDYAIACC
VSPMVVGKQM QFFGARANLA KTMLYAINGG VDEKLKMQVG PKSEPIKGDV LNFDEVMERM
DHFMDWLAKQ YVTALNVIHY MHDKYSYEAS LMALHDRDVI RTMACGIAGL SVAADSLSAI
KYAKVKPIRD EDGLAVDFEI EGEYPQFGNN DARVDDMAVD LVERFMKKIQ KLTTYRNAIP
TQSVLTITSN VVYGKKTGNT PDGRRAGAPF GPGANPMHGR DQKGAVASLT SVAKLPFAYA
KDGISYTFSI VPNALGKDDE VRKTNLAGLM DGYFHHEASI EGGQHLNVNV MNREMLLDAM
EHPEKYPQLT IRVSGYAVRF NSLTKEQQQD VITRTFTQTM
//
