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LSRG_ECODH
ID   LSRG_ECODH              Reviewed;          96 AA.
AC   B1XEA6;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=(4S)-4-hydroxy-5-phosphonooxypentane-2,3-dione isomerase {ECO:0000255|HAMAP-Rule:MF_02051};
DE            EC=5.3.1.32 {ECO:0000255|HAMAP-Rule:MF_02051};
DE   AltName: Full=Autoinducer 2-degrading protein LsrG {ECO:0000255|HAMAP-Rule:MF_02051};
DE            Short=AI-2-degrading protein LsrG {ECO:0000255|HAMAP-Rule:MF_02051};
DE   AltName: Full=Phospho-(S)-4,5-dihydroxy-2,3-pentanedione isomerase {ECO:0000255|HAMAP-Rule:MF_02051};
DE   AltName: Full=Phospho-AI-2 isomerase {ECO:0000255|HAMAP-Rule:MF_02051};
GN   Name=lsrG {ECO:0000255|HAMAP-Rule:MF_02051};
GN   OrderedLocusNames=ECDH10B_1649;
OS   Escherichia coli (strain K12 / DH10B).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=316385;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / DH10B;
RX   PubMed=18245285; DOI=10.1128/jb.01695-07;
RA   Durfee T., Nelson R., Baldwin S., Plunkett G. III, Burland V., Mau B.,
RA   Petrosino J.F., Qin X., Muzny D.M., Ayele M., Gibbs R.A., Csorgo B.,
RA   Posfai G., Weinstock G.M., Blattner F.R.;
RT   "The complete genome sequence of Escherichia coli DH10B: insights into the
RT   biology of a laboratory workhorse.";
RL   J. Bacteriol. 190:2597-2606(2008).
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 conversion of (4S)-4-hydroxy-5-
CC       phosphonooxypentane-2,3-dione (P-DPD) to 3-hydroxy-5-
CC       phosphonooxypentane-2,4-dione (P-HPD). {ECO:0000255|HAMAP-
CC       Rule:MF_02051}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2S)-2-hydroxy-3,4-dioxopentyl phosphate = 3-hydroxy-2,4-
CC         dioxopentyl phosphate; Xref=Rhea:RHEA:44360, ChEBI:CHEBI:71677,
CC         ChEBI:CHEBI:84359; EC=5.3.1.32; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_02051};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_02051}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02051}.
CC   -!- SIMILARITY: Belongs to the LsrG family. {ECO:0000255|HAMAP-
CC       Rule:MF_02051}.
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DR   EMBL; CP000948; ACB02728.1; -; Genomic_DNA.
DR   RefSeq; WP_000558527.1; NC_010473.1.
DR   AlphaFoldDB; B1XEA6; -.
DR   SMR; B1XEA6; -.
DR   GeneID; 58461895; -.
DR   KEGG; ecd:ECDH10B_1649; -.
DR   HOGENOM; CLU_131496_3_0_6; -.
DR   OMA; DTVAPMM; -.
DR   BioCyc; ECOL316385:ECDH10B_RS08445-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016861; F:intramolecular oxidoreductase activity, interconverting aldoses and ketoses; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_02051; LsrG; 1.
DR   InterPro; IPR007138; ABM_dom.
DR   InterPro; IPR011008; Dimeric_a/b-barrel.
DR   InterPro; IPR033672; LsrG.
DR   Pfam; PF03992; ABM; 1.
DR   SUPFAM; SSF54909; SSF54909; 1.
DR   PROSITE; PS51725; ABM; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Isomerase.
FT   CHAIN           1..96
FT                   /note="(4S)-4-hydroxy-5-phosphonooxypentane-2,3-dione
FT                   isomerase"
FT                   /id="PRO_0000351564"
FT   DOMAIN          2..91
FT                   /note="ABM"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02051"
SQ   SEQUENCE   96 AA;  11255 MW;  138099193F125EB8 CRC64;
     MHVTLVEINV HEDKVDEFIE VFRQNHLGSV QEEGNLRFDV LQDPEVNSRF YIYEAYKDED
     AVAFHKTTPH YKTCVAKLES LMTGPRKKRL FNGLMP
 
 
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