ID D3VE96_XENNA Unreviewed; 294 AA.
AC D3VE96;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE RecName: Full=3-hydroxy-5-phosphonooxypentane-2,4-dione thiolase {ECO:0000256|HAMAP-Rule:MF_02052};
DE EC=2.3.1.245 {ECO:0000256|HAMAP-Rule:MF_02052};
GN Name=lsrF {ECO:0000256|HAMAP-Rule:MF_02052,
GN ECO:0000313|EMBL:CBJ92347.1};
GN OrderedLocusNames=XNC1_4325 {ECO:0000313|EMBL:CBJ92347.1};
OS Xenorhabdus nematophila (strain ATCC 19061 / DSM 3370 / CCUG 14189 / LMG
OS 1036 / NCIMB 9965 / AN6).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Xenorhabdus.
OX NCBI_TaxID=406817 {ECO:0000313|EMBL:CBJ92347.1, ECO:0000313|Proteomes:UP000008075};
RN [1] {ECO:0000313|EMBL:CBJ92347.1, ECO:0000313|Proteomes:UP000008075}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19061 / DSM 3370 / CCUG 14189 / LMG 1036 / NCIMB 9965 /
RC AN6 {ECO:0000313|Proteomes:UP000008075};
RX PubMed=22125637; DOI=10.1371/journal.pone.0027909;
RA Chaston J.M., Suen G., Tucker S.L., Andersen A.W., Bhasin A., Bode E.,
RA Bode H.B., Brachmann A.O., Cowles C.E., Cowles K.N., Darby C., de Leon L.,
RA Drace K., Du Z., Givaudan A., Herbert Tran E.E., Jewell K.A., Knack J.J.,
RA Krasomil-Osterfeld K.C., Kukor R., Lanois A., Latreille P.,
RA Leimgruber N.K., Lipke C.M., Liu R., Lu X., Martens E.C., Marri P.R.,
RA Medigue C., Menard M.L., Miller N.M., Morales-Soto N., Norton S.,
RA Ogier J.C., Orchard S.S., Park D., Park Y., Qurollo B.A., Sugar D.R.,
RA Richards G.R., Rouy Z., Slominski B., Slominski K., Snyder H., Tjaden B.C.,
RA van der Hoeven R., Welch R.D., Wheeler C., Xiang B., Barbazuk B.,
RA Gaudriault S., Goodner B., Slater S.C., Forst S., Goldman B.S.,
RA Goodrich-Blair H.;
RT "The entomopathogenic bacterial endosymbionts xenorhabdus and photorhabdus:
RT convergent lifestyles from divergent genomes.";
RL PLoS ONE 6:E27909-E27909(2011).
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:0000256|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:0000256|HAMAP-Rule:MF_02052};
CC -!- SUBUNIT: Homodecamer. {ECO:0000256|HAMAP-Rule:MF_02052}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02052}.
CC -!- SIMILARITY: Belongs to the DeoC/FbaB aldolase family.
CC {ECO:0000256|HAMAP-Rule:MF_02052}.
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DR EMBL; FN667742; CBJ92347.1; -; Genomic_DNA.
DR RefSeq; WP_010848504.1; NC_014228.1.
DR AlphaFoldDB; D3VE96; -.
DR STRING; 406817.XNC1_4325; -.
DR KEGG; xne:XNC1_4325; -.
DR eggNOG; COG1830; Bacteria.
DR HOGENOM; CLU_057069_1_0_6; -.
DR Proteomes; UP000008075; 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; Aldolase class I; 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 PANTHER; PTHR47916:SF1; 3-HYDROXY-5-PHOSPHONOOXYPENTANE-2,4-DIONE THIOLASE-RELATED; 1.
DR PANTHER; PTHR47916; FRUCTOSE-BISPHOSPHATE ALDOLASE CLASS 1; 1.
DR Pfam; PF01791; DeoC; 1.
DR PIRSF; PIRSF038992; Aldolase_Ia; 1.
DR SMART; SM01133; DeoC; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02052};
KW Reference proteome {ECO:0000313|Proteomes:UP000008075};
KW Schiff base {ECO:0000256|HAMAP-Rule:MF_02052};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_02052}.
FT ACT_SITE 203
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02052"
SQ SEQUENCE 294 AA; 31901 MW; 70345A3CCD539A38 CRC64;
MADLDDIKDG KDFGIDTPQK NTLFELKGCG ALDWGMQSRL SRIFNPATNK TVMLAFDHGY
FQGPTTGLER IDINIAPLFA HTDVLMCTRG ILRSQVPPAT NKPVVLRASG ANSILTELSN
EAVAVAMEDA LRLNVCAVAA QVYIGSEHEH QSIKNIIKLV DQGTRYGMPT MAVTGVGKDM
ARDQRYFSLA TRIAAEMGAH IIKTYYVDTG FERIAAGCPV PIVIAGGKKL PELDALEMCY
QAIDQGASGV DMGRNIFQSE APVAMLKAVQ AVVHHNEKPA QAYELFLSEK AKGE
//
