LSRG_YERPN
ID LSRG_YERPN Reviewed; 96 AA.
AC Q1CN20; C4GNH7;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 1.
DT 25-MAY-2022, entry version 77.
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=YPN_0277;
GN ORFNames=YP516_0274;
OS Yersinia pestis bv. Antiqua (strain Nepal516).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=377628;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nepal516;
RX PubMed=16740952; DOI=10.1128/jb.00124-06;
RA Chain P.S.G., Hu P., Malfatti S.A., Radnedge L., Larimer F., Vergez L.M.,
RA Worsham P., Chu M.C., Andersen G.L.;
RT "Complete genome sequence of Yersinia pestis strains Antiqua and Nepal516:
RT evidence of gene reduction in an emerging pathogen.";
RL J. Bacteriol. 188:4453-4463(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nepal516;
RA Plunkett G. III, Anderson B.D., Baumler D.J., Burland V., Cabot E.L.,
RA Glasner J.D., Mau B., Neeno-Eckwall E., Perna N.T., Munk A.C., Tapia R.,
RA Green L.D., Rogers Y.C., Detter J.C., Bruce D.C., Brettin T.S.;
RT "Yersinia pestis Nepal516A whole genome shotgun sequencing project.";
RL Submitted (APR-2009) 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}.
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DR EMBL; CP000305; ABG16610.1; -; Genomic_DNA.
DR EMBL; ACNQ01000006; EEO78059.1; -; Genomic_DNA.
DR RefSeq; WP_002209186.1; NZ_ACNQ01000006.1.
DR AlphaFoldDB; Q1CN20; -.
DR SMR; Q1CN20; -.
DR EnsemblBacteria; ABG16610; ABG16610; YPN_0277.
DR GeneID; 66843034; -.
DR KEGG; ypn:YPN_0277; -.
DR HOGENOM; CLU_131496_3_0_6; -.
DR OMA; DTVAPMM; -.
DR Proteomes; UP000008936; 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_0000351581"
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