ID   LSRF_ENT38              Reviewed;         295 AA.
AC   A4WER0;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 89.
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}; OrderedLocusNames=Ent638_3532;
OS   Enterobacter sp. (strain 638).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Enterobacter.
OX   NCBI_TaxID=399742;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=638;
RX   PubMed=20485560; DOI=10.1371/journal.pgen.1000943;
RA   Taghavi S., van der Lelie D., Hoffman A., Zhang Y.B., Walla M.D.,
RA   Vangronsveld J., Newman L., Monchy S.;
RT   "Genome sequence of the plant growth promoting endophytic bacterium
RT   Enterobacter sp. 638.";
RL   PLoS Genet. 6:E1000943-E1000943(2010).
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; CP000653; ABP62190.1; -; Genomic_DNA.
DR   RefSeq; WP_015960516.1; NC_009436.1.
DR   AlphaFoldDB; A4WER0; -.
DR   SMR; A4WER0; -.
DR   STRING; 399742.Ent638_3532; -.
DR   PRIDE; A4WER0; -.
DR   EnsemblBacteria; ABP62190; ABP62190; Ent638_3532.
DR   KEGG; ent:Ent638_3532; -.
DR   eggNOG; COG1830; Bacteria.
DR   HOGENOM; CLU_057069_1_0_6; -.
DR   OMA; CEYWGMP; -.
DR   OrthoDB; 1560751at2; -.
DR   Proteomes; UP000000230; 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; -; 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   Pfam; PF01791; DeoC; 1.
DR   PIRSF; PIRSF038992; Aldolase_Ia; 1.
DR   SMART; SM01133; DeoC; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Schiff base; Transferase.
FT   CHAIN           1..295
FT                   /note="3-hydroxy-5-phosphonooxypentane-2,4-dione thiolase"
FT                   /id="PRO_0000351517"
FT   ACT_SITE        203
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02052"
SQ   SEQUENCE   295 AA;  31940 MW;  4401BC09D776EC36 CRC64;
     MADLDDIKDG KDFGIGTPQT NTPYTLKGCG ALDWGMQSRL ARIFNPKSNR TVMLAFDHGY
     FQGPTTGLER IDLSIAPLFA ETDVLMCTRG ILRSTVPPAT NKPVVLRASG GNSILGELSN
     ECVAVAMEDA LRLNVCAVAA QVYIGSEFEH QSINNIIKLV DAGNRYGIPT LAVTGVGKEM
     ARDARYFSLA SRIAAEMGAQ VVKTYFVEEG FEKVTASCPV PIVIAGGKKL PEHEALEMCF
     RAIDQGASGV DMGRNIFQSS APLAMLKAVK KVVHENMSAR EAFQFWQEEK QGEGQ