ID   LSRG_YERPY              Reviewed;          96 AA.
AC   B1JLQ5;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 65.
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}; OrderedLocusNames=YPK_3655;
OS   Yersinia pseudotuberculosis serotype O:3 (strain YPIII).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=502800;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YPIII;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C.,
RA   Han C., Tapia R., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Challacombe J.F., Green L., Lindler L.E., Nikolich M.P., Richardson P.;
RT   "Complete sequence of Yersinia pseudotuberculosis YPIII.";
RL   Submitted (FEB-2008) 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 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000950; ACA69922.1; -; Genomic_DNA.
DR   RefSeq; WP_002209186.1; NZ_CP009792.1.
DR   AlphaFoldDB; B1JLQ5; -.
DR   SMR; B1JLQ5; -.
DR   EnsemblBacteria; ACA69922; ACA69922; YPK_3655.
DR   GeneID; 66843034; -.
DR   KEGG; ypy:YPK_3655; -.
DR   PATRIC; fig|502800.11.peg.4410; -.
DR   OMA; DTVAPMM; -.
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_0000351585"
FT   DOMAIN          2..91
FT                   /note="ABM"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02051"
SQ   SEQUENCE   96 AA;  11098 MW;  FB8E869AEC86AA21 CRC64;
     MHVTLVEINV KEDKVDQFIE VFRANHLGSI REAGNLRFDV LRDEHIPTRF YIYEAYTDEA
     AVAIHKTTPH YLQCVEQLAP LMTGPRKKTV FIGLMP