LSRF_SALTI
ID LSRF_SALTI Reviewed; 291 AA.
AC Q8Z2X9; Q7C6A2;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 114.
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=STY3792, t3540;
OS Salmonella typhi.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=90370;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CT18;
RX PubMed=11677608; DOI=10.1038/35101607;
RA Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA Barrell B.G.;
RT "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT serovar Typhi CT18.";
RL Nature 413:848-852(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700931 / Ty2;
RX PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT CT18.";
RL J. Bacteriol. 185:2330-2337(2003).
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; AE014613; AAO71047.1; -; Genomic_DNA.
DR EMBL; AL513382; CAD09545.1; -; Genomic_DNA.
DR RefSeq; NP_457974.1; NC_003198.1.
DR RefSeq; WP_000774152.1; NZ_WSUR01000010.1.
DR AlphaFoldDB; Q8Z2X9; -.
DR SMR; Q8Z2X9; -.
DR STRING; 220341.16504661; -.
DR EnsemblBacteria; AAO71047; AAO71047; t3540.
DR KEGG; stt:t3540; -.
DR KEGG; sty:STY3792; -.
DR PATRIC; fig|220341.7.peg.3870; -.
DR eggNOG; COG1830; Bacteria.
DR HOGENOM; CLU_057069_1_0_6; -.
DR OMA; CEYWGMP; -.
DR Proteomes; UP000000541; Chromosome.
DR Proteomes; UP000002670; 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_0000351529"
FT ACT_SITE 203
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02052"
SQ SEQUENCE 291 AA; 31757 MW; 5F33B0EFB67CAEE1 CRC64;
MADLDDIKDG KDFHTDKPQT NTLFSLKGCG ALDWGMQSRL ARIFNPRTRK TVMLAFDHGY
FQGPTTGLER IDINIAPLFE YADVLMCTRG ILRSVVPPAI NKPVVLRASG ANSILTELSN
EAVAVAMDDA VRLNSCAAAA QVYIGSEHEH QSIKNIIQLI DAGLRVGMPI MAVTGVGKDM
ARDQRYFSLA TRIAAEMGAQ IIKTYYVDKG FERIAAGCPV PIVIAGGKKL PEREALEMCY
QAIDQGASGV DMGRNIFQSE DPVAMIKAVH AVVHHNETAE RAYELFLSEK G
