LSRF_KLEP7
ID LSRF_KLEP7 Reviewed; 295 AA.
AC A6TEB4;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 25-MAY-2022, entry version 75.
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=KPN78578_34740; ORFNames=KPN_03503;
OS Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=272620;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700721 / MGH 78578;
RG The Klebsiella pneumonia Genome Sequencing Project;
RA McClelland M., Sanderson E.K., Spieth J., Clifton W.S., Latreille P.,
RA Sabo A., Pepin K., Bhonagiri V., Porwollik S., Ali J., Wilson R.K.;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000647; ABR78898.1; -; Genomic_DNA.
DR RefSeq; WP_002917724.1; NC_009648.1.
DR AlphaFoldDB; A6TEB4; -.
DR SMR; A6TEB4; -.
DR STRING; 272620.KPN_03503; -.
DR jPOST; A6TEB4; -.
DR EnsemblBacteria; ABR78898; ABR78898; KPN_03503.
DR GeneID; 56936752; -.
DR GeneID; 66602047; -.
DR KEGG; kpn:KPN_03503; -.
DR HOGENOM; CLU_057069_1_0_6; -.
DR OMA; CEYWGMP; -.
DR Proteomes; UP000000265; 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; Reference proteome; Schiff base; Transferase.
FT CHAIN 1..295
FT /note="3-hydroxy-5-phosphonooxypentane-2,4-dione thiolase"
FT /id="PRO_0000351524"
FT ACT_SITE 203
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02052"
SQ SEQUENCE 295 AA; 32411 MW; AC73D0FAEDD3CB3E CRC64;
MADLDDIKEG KDFGIDRPQQ NTLYTLKGCG SLDWGMQSRL ARIFNPHSNR TVMLAFDHGY
FQGPTTGLER IDLSIAPLFA DTDVLMCTRG VLRSQVPAAT NKPVVLRASG GNSILSELSN
ECVAVAMEDA LRLNVCAVAA QVYIGSEYEH QSINNIIKLV DAGNRYGMPV LAVTGVGKEM
TRDARYFSLA SRIAAEMGAQ FVKTYFVEEG FEKVTASCPV PIVIAGGKKL PEHEALEMCW
RAIDQGASGV DMGRNIFQSS APRAMLKAVK KVVHENLNAR EAYQFWQEEK QGELK
