LSRF_SALPA
ID LSRF_SALPA Reviewed; 291 AA.
AC Q5PJE3;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 25-MAY-2022, entry version 87.
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=SPA3921;
OS Salmonella paratyphi A (strain ATCC 9150 / SARB42).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=295319;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 9150 / SARB42;
RX PubMed=15531882; DOI=10.1038/ng1470;
RA McClelland M., Sanderson K.E., Clifton S.W., Latreille P., Porwollik S.,
RA Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., Harkins C.R.,
RA Wang C., Nguyen C., Berghoff A., Elliott G., Kohlberg S., Strong C., Du F.,
RA Carter J., Kremizki C., Layman D., Leonard S., Sun H., Fulton L., Nash W.,
RA Miner T., Minx P., Delehaunty K., Fronick C., Magrini V., Nhan M.,
RA Warren W., Florea L., Spieth J., Wilson R.K.;
RT "Comparison of genome degradation in Paratyphi A and Typhi, human-
RT restricted serovars of Salmonella enterica that cause typhoid.";
RL Nat. Genet. 36:1268-1274(2004).
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; CP000026; AAV79686.1; -; Genomic_DNA.
DR RefSeq; WP_000774146.1; NC_006511.1.
DR AlphaFoldDB; Q5PJE3; -.
DR SMR; Q5PJE3; -.
DR EnsemblBacteria; AAV79686; AAV79686; SPA3921.
DR KEGG; spt:SPA3921; -.
DR HOGENOM; CLU_057069_1_0_6; -.
DR OMA; CEYWGMP; -.
DR Proteomes; UP000008185; 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_0000351527"
FT ACT_SITE 203
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02052"
SQ SEQUENCE 291 AA; 31713 MW; 0303B51480C29ED9 CRC64;
MADLDDIKDG KDFHTDKPQT NTLFALKGCG ALDWGMQSRL ARIFNPKTRK 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
