ID   LSRG_ECOLI              Reviewed;          96 AA.
AC   P64461; P76144; Q2MB98;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   10-JUN-2026, entry version 135.
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, ECO:0000269|PubMed:21454635};
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, ECO:0000303|PubMed:21454635};
DE   AltName: Full=Phospho-AI-2 isomerase {ECO:0000255|HAMAP-Rule:MF_02051};
GN   Name=lsrG {ECO:0000255|HAMAP-Rule:MF_02051}; Synonyms=yneC;
GN   OrderedLocusNames=b1518, JW1511;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [3]
RP   INDUCTION.
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=15601708; DOI=10.1128/jb.187.1.238-248.2005;
RA   Xavier K.B., Bassler B.L.;
RT   "Regulation of uptake and processing of the quorum-sensing autoinducer AI-2
RT   in Escherichia coli.";
RL   J. Bacteriol. 187:238-248(2005).
RN   [4]
RP   INDUCTION.
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=15743955; DOI=10.1128/jb.187.6.2066-2076.2005;
RA   Wang L., Hashimoto Y., Tsao C.-Y., Valdes J.J., Bentley W.E.;
RT   "Cyclic AMP (cAMP) and cAMP receptor protein influence both synthesis and
RT   uptake of extracellular autoinducer 2 in Escherichia coli.";
RL   J. Bacteriol. 187:2066-2076(2005).
RN   [5]
RP   FUNCTION IN PHOSPHO-AI-2 DEGRADATION.
RX   PubMed=17274596; DOI=10.1021/cb600444h;
RA   Xavier K.B., Miller S.T., Lu W., Kim J.H., Rabinowitz J., Pelczer I.,
RA   Semmelhack M.F., Bassler B.L.;
RT   "Phosphorylation and processing of the quorum-sensing molecule autoinducer-
RT   2 in enteric bacteria.";
RL   ACS Chem. Biol. 2:128-136(2007).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY,
RP   SUBUNIT, AND MUTAGENESIS OF ASN-25; GLU-54; HIS-65 AND HIS-70.
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=21454635; DOI=10.1074/jbc.m111.230227;
RA   Marques J.C., Lamosa P., Russell C., Ventura R., Maycock C.,
RA   Semmelhack M.F., Miller S.T., Xavier K.B.;
RT   "Processing the interspecies quorum-sensing signal autoinducer-2 (AI-2):
RT   characterization of phospho-(S)-4,5-dihydroxy-2,3-pentanedione
RT   isomerization by LsrG protein.";
RL   J. Biol. Chem. 286:18331-18343(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 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, ECO:0000269|PubMed:17274596,
CC       ECO:0000269|PubMed:21454635}.
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, ECO:0000269|PubMed:21454635};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_02051,
CC       ECO:0000269|PubMed:21454635}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02051}.
CC   -!- INDUCTION: In the absence of AI-2, repressed by LsrR. Induced by AI-2,
CC       via release of the LsrR repressor. In the absence of glucose, induced
CC       by cAMP-CRP by direct binding to the upstream region of the lsr
CC       promoter. {ECO:0000269|PubMed:15601708, ECO:0000269|PubMed:15743955}.
CC   -!- SIMILARITY: Belongs to the LsrG family. {ECO:0000255|HAMAP-
CC       Rule:MF_02051}.
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DR   EMBL; U00096; AAC74591.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE76458.1; -; Genomic_DNA.
DR   PIR; A64906; A64906.
DR   RefSeq; NP_416035.1; NC_000913.3.
DR   RefSeq; WP_000558527.1; NZ_CP009789.1.
DR   PDB; 3QMQ; X-ray; 1.80 A; A/B/C/D=1-96.
DR   AlphaFoldDB; P64461; -.
DR   SMR; P64461; -.
DR   BioGRID; 4260228; 16.
DR   BioGRID; 850433; 1.
DR   DIP; DIP-47853N; -.
DR   FunCoup; P64461; 113.
DR   IntAct; P64461; 6.
DR   STRING; 511145.b1518; -.
DR   jPOST; P64461; -.
DR   PaxDb; 511145-b1518; -.
DR   EnsemblBacteria; AAC74591; AAC74591; b1518.
DR   GeneID; 75057398; -.
DR   GeneID; 946073; -.
DR   KEGG; ecj:JW1511; -.
DR   KEGG; eco:b1518; -.
DR   KEGG; ecoc:C3026_08775; -.
DR   PATRIC; fig|1411691.4.peg.749; -.
DR   EchoBASE; EB3572; -.
DR   eggNOG; COG1359; Bacteria.
DR   HOGENOM; CLU_131496_3_0_6; -.
DR   InParanoid; P64461; -.
DR   OMA; KETAHYQ; -.
DR   OrthoDB; 9812754at2; -.
DR   PhylomeDB; P64461; -.
DR   BioCyc; EcoCyc:G6805-MONOMER; -.
DR   BioCyc; MetaCyc:G6805-MONOMER; -.
DR   PHI-base; PHI:9997; -.
DR   PRO; PR:P64461; -.
DR   Proteomes; UP000000625; Chromosome.
DR   AbasyAtlas; P64461; -.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0002952; F:(4S)-4-hydroxy-5-phosphonooxypentane-2,3-dione isomerase activity; IDA:EcoCyc.
DR   GO; GO:0016853; F:isomerase activity; IDA:EcoCyc.
DR   GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR   GO; GO:0009372; P:quorum sensing; IC:EcoCyc.
DR   FunFam; 3.30.70.100:FF:000016; (4S)-4-hydroxy-5-phosphonooxypentane-2,3-dione isomerase; 1.
DR   Gene3D; 3.30.70.100; -; 1.
DR   HAMAP; MF_02051; LsrG; 1.
DR   InterPro; IPR007138; ABM_dom.
DR   InterPro; IPR050744; AI-2_Isomerase_LsrG.
DR   InterPro; IPR011008; Dimeric_a/b-barrel.
DR   InterPro; IPR033672; LsrG.
DR   NCBIfam; NF007791; PRK10486.1; 1.
DR   PANTHER; PTHR33336:SF1; (4S)-4-HYDROXY-5-PHOSPHONOOXYPENTANE-2,3-DIONE ISOMERASE; 1.
DR   PANTHER; PTHR33336; QUINOL MONOOXYGENASE YGIN-RELATED; 1.
DR   Pfam; PF03992; ABM; 1.
DR   SUPFAM; SSF54909; Dimeric alpha+beta barrel; 1.
DR   PROSITE; PS51725; ABM; 1.
DR   PDBsum; 3QMQ; -.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Isomerase; Reference proteome.
FT   CHAIN           1..96
FT                   /note="(4S)-4-hydroxy-5-phosphonooxypentane-2,3-dione
FT                   isomerase"
FT                   /id="PRO_0000168947"
FT   DOMAIN          2..91
FT                   /note="ABM"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02051"
FT   MUTAGEN         25
FT                   /note="N->A: 3-fold lower specific activity."
FT                   /evidence="ECO:0000269|PubMed:21454635"
FT   MUTAGEN         54
FT                   /note="E->A: No activity."
FT                   /evidence="ECO:0000269|PubMed:21454635"
FT   MUTAGEN         65
FT                   /note="H->A: No activity."
FT                   /evidence="ECO:0000269|PubMed:21454635"
FT   MUTAGEN         70
FT                   /note="H->A: 100-fold lower specific activity."
FT                   /evidence="ECO:0000269|PubMed:21454635"
FT   STRAND          1..10
FT                   /evidence="ECO:0007829|PDB:3QMQ"
FT   HELIX           12..14
FT                   /evidence="ECO:0007829|PDB:3QMQ"
FT   HELIX           15..29
FT                   /evidence="ECO:0007829|PDB:3QMQ"
FT   STRAND          35..42
FT                   /evidence="ECO:0007829|PDB:3QMQ"
FT   STRAND          49..58
FT                   /evidence="ECO:0007829|PDB:3QMQ"
FT   HELIX           59..65
FT                   /evidence="ECO:0007829|PDB:3QMQ"
FT   HELIX           69..78
FT                   /evidence="ECO:0007829|PDB:3QMQ"
FT   HELIX           79..81
FT                   /evidence="ECO:0007829|PDB:3QMQ"
FT   STRAND          82..84
FT                   /evidence="ECO:0007829|PDB:3QMQ"
FT   STRAND          87..95
FT                   /evidence="ECO:0007829|PDB:3QMQ"
SQ   SEQUENCE   96 AA;  11255 MW;  138099193F125EB8 CRC64;
     MHVTLVEINV HEDKVDEFIE VFRQNHLGSV QEEGNLRFDV LQDPEVNSRF YIYEAYKDED
     AVAFHKTTPH YKTCVAKLES LMTGPRKKRL FNGLMP
//