ID A0A2S4MW07_SHIFL Unreviewed; 760 AA.
AC A0A2S4MW07; Q7C294; Q83LP6;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 30.
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:AAN42528.1};
GN OrderedLocusNames=SF0898 {ECO:0000313|EMBL:AAN42528.1};
OS Shigella flexneri.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623 {ECO:0000313|EMBL:AAN42528.1, ECO:0000313|Proteomes:UP000001006};
RN [1] {ECO:0000313|EMBL:AAN42528.1, ECO:0000313|Proteomes:UP000001006}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a {ECO:0000313|Proteomes:UP000001006};
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
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; AE005674; AAN42528.1; -; Genomic_DNA.
DR RefSeq; NP_706821.1; NC_004337.2.
DR RefSeq; WP_001292813.1; NZ_WPGW01000209.1.
DR AlphaFoldDB; A0A2S4MW07; -.
DR PaxDb; 198214-SF0898; -.
DR GeneID; 1023824; -.
DR KEGG; sfl:SF0898; -.
DR PATRIC; fig|198214.7.peg.1045; -.
DR OMA; DTAIACC; -.
DR UniPathway; UPA00920; UER00891.
DR Proteomes; UP000001006; 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 Reference proteome {ECO:0000313|Proteomes:UP000001006};
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; 85323 MW; 05D3CB3F956BD800 CRC64;
MSELNEKLAT AWEGFTKGDW QNEVNVRDFI QKNYTPYEGD ESFLAGATEA TTTLWDKVME
GVKLENRTHA PVDFDTAVAS TITSHDAGYI NKALEKVVGL QTEAPLKRAL IPFGGIKMIE
GSCKAYNREL DPMIKKIFTE YRKTHNQGVF DVYTPDILRC RKSGVLTGLP DAYGRGRIIG
DYRRVALYGI DYLMKDKYAQ FTSLQADLEN GVNLEQTIRL REEIAEQHRA LGQMKEMAAK
YGYDISGPAT NAQEAIQWTY FGYLAAVKSQ NGAAMSFGRT STFLDVYIER DLKAGKITEQ
EAQEMVDHLV MKLRMVRFLR TPEYDELFSG DPIWATESIG GMGLDGRTLV TKNSFRFLNT
LYTMGPSPEP NMTILWSEKL PLNFKKFAAK VSIDTSSLQY ENDDLMRPDF NNDDYAIACC
VSPMIVGKQM QFFGARANLA KTMLYAINGG VDEKLKMQVG PKSEPIKGDL LSYDEVMERM
DHFMDWLAKQ YITALNIIHY MHDKYSYEAS LMALHDRDVI RTMACGIAGL SVAADSLSAI
KYAKVKPIRD EDGLAIDFEI EGEYPQFGNN DPRVDDLAVD LVERFMKKIQ KLHTYRDAIP
TQSVLTITSN VVYGKKTGNT PDGRRAGAPF GPGANPMHGR DQKGAVASLT SVAKLPFAYA
KDGISYTFSI VPNALGKDDE VRKTNLAGLM DGYFHHEASI EGGQHLNVNV MNREMLLDAM
ENPEKYPQLT IRVSGYAVRF NSLTKEQQQD VITRTFTQSM
//
