ID   LSRF_YERE8              Reviewed;         291 AA.
AC   A1JJ51;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   25-MAY-2022, 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}; OrderedLocusNames=YE0524;
OS   Yersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 /
OS   8081).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=393305;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 13174 / 8081;
RX   PubMed=17173484; DOI=10.1371/journal.pgen.0020206;
RA   Thomson N.R., Howard S., Wren B.W., Holden M.T.G., Crossman L.,
RA   Challis G.L., Churcher C., Mungall K., Brooks K., Chillingworth T.,
RA   Feltwell T., Abdellah Z., Hauser H., Jagels K., Maddison M., Moule S.,
RA   Sanders M., Whitehead S., Quail M.A., Dougan G., Parkhill J.,
RA   Prentice M.B.;
RT   "The complete genome sequence and comparative genome analysis of the high
RT   pathogenicity Yersinia enterocolitica strain 8081.";
RL   PLoS Genet. 2:2039-2051(2006).
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; AM286415; CAL10642.1; -; Genomic_DNA.
DR   RefSeq; WP_005175220.1; NC_008800.1.
DR   RefSeq; YP_001004884.1; NC_008800.1.
DR   AlphaFoldDB; A1JJ51; -.
DR   SMR; A1JJ51; -.
DR   STRING; 393305.YE0524; -.
DR   EnsemblBacteria; CAL10642; CAL10642; YE0524.
DR   KEGG; yen:YE0524; -.
DR   PATRIC; fig|393305.7.peg.614; -.
DR   eggNOG; COG1830; Bacteria.
DR   HOGENOM; CLU_057069_1_0_6; -.
DR   OMA; CEYWGMP; -.
DR   Proteomes; UP000000642; 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..291
FT                   /note="3-hydroxy-5-phosphonooxypentane-2,4-dione thiolase"
FT                   /id="PRO_0000351533"
FT   ACT_SITE        203
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02052"
SQ   SEQUENCE   291 AA;  31594 MW;  9925DFAEAA111B01 CRC64;
     MADLDDIKDG KDFGIGVPQQ NPAFTLKGCG SLDWGMQSRL ARIFNPKTNR TVMLAFDHGY
     FQGPTTGLER IDINIAPLFE YADVLMCTRG ILRSIVPAAA NRPVVLRASG ANSILTDLSN
     EAVAVAMEDA LRLNSCAVAA QVYIGTEHEH QSIKNIIQLV DQGIRYGMPT MAVTGVGKDM
     ARDQRYFSLA TRIAAEMGAQ VIKTYYVDSG FERIAAGCPV PIVIAGGKKL PERDALEMCY
     QAIDQGASGV DMGRNIFQSE APIAMLKAVH AVVHKNENAE TAYKLFLHEK G