ID   LSRG_SALPB              Reviewed;          96 AA.
AC   A9MZG6;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 2.
DT   25-MAY-2022, entry version 62.
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=SPAB_05053;
OS   Salmonella paratyphi B (strain ATCC BAA-1250 / SPB7).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=1016998;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1250 / SPB7;
RG   The Salmonella enterica serovar Paratyphi B Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA   Fulton R., Cordes M., Wollam A., Shah N., Pepin K., Bhonagiri V., Nash W.,
RA   Johnson M., Thiruvilangam P., Wilson R.;
RL   Submitted (NOV-2007) 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   -!- SEQUENCE CAUTION:
CC       Sequence=ABX70344.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; CP000886; ABX70344.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_001543603.1; NC_010102.1.
DR   AlphaFoldDB; A9MZG6; -.
DR   SMR; A9MZG6; -.
DR   KEGG; spq:SPAB_05053; -.
DR   PATRIC; fig|1016998.12.peg.4743; -.
DR   HOGENOM; CLU_131496_3_0_6; -.
DR   Proteomes; UP000008556; 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_0000351571"
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