ID   LSRG_SALCH              Reviewed;          96 AA.
AC   Q57HD8;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 2.
DT   25-MAY-2022, entry version 79.
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=SCH_3968;
OS   Salmonella choleraesuis (strain SC-B67).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=321314;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC-B67;
RX   PubMed=15781495; DOI=10.1093/nar/gki297;
RA   Chiu C.-H., Tang P., Chu C., Hu S., Bao Q., Yu J., Chou Y.-Y., Wang H.-S.,
RA   Lee Y.-S.;
RT   "The genome sequence of Salmonella enterica serovar Choleraesuis, a highly
RT   invasive and resistant zoonotic pathogen.";
RL   Nucleic Acids Res. 33:1690-1698(2005).
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   -!- SEQUENCE CAUTION:
CC       Sequence=AAX67874.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AE017220; AAX67874.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_001543603.1; NC_006905.1.
DR   AlphaFoldDB; Q57HD8; -.
DR   SMR; Q57HD8; -.
DR   EnsemblBacteria; AAX67874; AAX67874; SCH_3968.
DR   KEGG; sec:SCH_3968; -.
DR   HOGENOM; CLU_131496_3_0_6; -.
DR   Proteomes; UP000000538; Chromosome.
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_0000351569"
FT   DOMAIN          2..91
FT                   /note="ABM"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02051"
SQ   SEQUENCE   96 AA;  11218 MW;  1594351E2310DA0B CRC64;
     MHVTLVEINV HDDKVEQFID VFRQNHLGSI KEPGNLRFDV LQDPQVPTRF YIYEAYVDEQ
     AVAFHKTTPH YKTCVEQLEP LMTGPRTKKV FMGLMP