ID LSRF_ECO24 Reviewed; 291 AA.
AC A7ZLX4;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE RecName: Full=3-hydroxy-5-phosphonooxypentane-2,4-dione thiolase {ECO:0000255|HAMAP-Rule:MF_02052};
DE EC=2.3.1.245 {ECO:0000255|HAMAP-Rule:MF_02052};
GN Name=lsrF {ECO:0000255|HAMAP-Rule:MF_02052};
GN OrderedLocusNames=EcE24377A_1717;
OS Escherichia coli O139:H28 (strain E24377A / ETEC).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=331111;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E24377A / ETEC;
RX PubMed=18676672; DOI=10.1128/jb.00619-08;
RA Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F.,
RA Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R.,
RA Henderson I.R., Sperandio V., Ravel J.;
RT "The pangenome structure of Escherichia coli: comparative genomic analysis
RT of E. coli commensal and pathogenic isolates.";
RL J. Bacteriol. 190:6881-6893(2008).
CC -!- FUNCTION: Involved in the degradation of phospho-AI-2, thereby
CC terminating induction of the lsr operon and closing the AI-2 signaling
CC cycle. Catalyzes the transfer of an acetyl moiety from 3-hydroxy-5-
CC phosphonooxypentane-2,4-dione to CoA to form glycerone phosphate and
CC acetyl-CoA. {ECO:0000255|HAMAP-Rule:MF_02052}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + dihydroxyacetone phosphate = 3-hydroxy-2,4-
CC dioxopentyl phosphate + CoA; Xref=Rhea:RHEA:44736, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57288, ChEBI:CHEBI:57642, ChEBI:CHEBI:84359;
CC EC=2.3.1.245; Evidence={ECO:0000255|HAMAP-Rule:MF_02052};
CC -!- SUBUNIT: Homodecamer. {ECO:0000255|HAMAP-Rule:MF_02052}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02052}.
CC -!- SIMILARITY: Belongs to the DeoC/FbaB aldolase family.
CC {ECO:0000255|HAMAP-Rule:MF_02052}.
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DR EMBL; CP000800; ABV18111.1; -; Genomic_DNA.
DR RefSeq; WP_000774189.1; NC_009801.1.
DR AlphaFoldDB; A7ZLX4; -.
DR SMR; A7ZLX4; -.
DR KEGG; ecw:EcE24377A_1717; -.
DR HOGENOM; CLU_057069_1_0_6; -.
DR Proteomes; UP000001122; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:UniProtKB-UniRule.
DR GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IEA:InterPro.
DR CDD; cd00958; DhnA; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR HAMAP; MF_02052; LsrF; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR002915; DeoC/FbaB/LacD_aldolase.
DR InterPro; IPR041720; FbaB-like.
DR InterPro; IPR033673; LsrF.
DR PANTHER; PTHR47916:SF1; 3-HYDROXY-5-PHOSPHONOOXYPENTANE-2,4-DIONE THIOLASE-RELATED; 1.
DR PANTHER; PTHR47916; FRUCTOSE-BISPHOSPHATE ALDOLASE CLASS 1; 1.
DR Pfam; PF01791; DeoC; 1.
DR PIRSF; PIRSF038992; Aldolase_Ia; 1.
DR SMART; SM01133; DeoC; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Reference proteome; Schiff base; Transferase.
FT CHAIN 1..291
FT /note="3-hydroxy-5-phosphonooxypentane-2,4-dione thiolase"
FT /id="PRO_0000351521"
FT ACT_SITE 203
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02052"
SQ SEQUENCE 291 AA; 31851 MW; C2D3750C864C00CE CRC64;
MADLDDIKDG KDFRTDQPQQ NIPFTLKGCG ALDWGMQSRL SRIFNPKTGN TVMLAFDHGY
FQGPTTGLER IDINIAPLFE HADVLMCTRG ILRSVVPPAT NKPVVLRASG ANSILAELSN
EAVALSMDDA VRLNSCAVAA QVYIGSEYEH QSIKNIIQLV DAGMKVGMPT MAVTGVGKDM
VRDQRYFSLA TRIAAEMGAQ IIKTYYVEKG FERIVAGCPV PIVIAGGKKL PEREALEMCW
QAIDQGASGV DMGRNIFQSD HPVAMMKAVQ AVVHHNETAD RAYELYLSEK Q
//
