LSRG_ECOHS
ID LSRG_ECOHS Reviewed; 96 AA.
AC A8A071;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 25-MAY-2022, entry version 72.
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=EcHS_A1600;
OS Escherichia coli O9:H4 (strain HS).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=331112;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HS;
RX PubMed=18676672; DOI=10.1128/jb.00619-08;
RA Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F.,
RA Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R.,
RA Henderson I.R., Sperandio V., Ravel J.;
RT "The pangenome structure of Escherichia coli: comparative genomic analysis
RT of E. coli commensal and pathogenic isolates.";
RL J. Bacteriol. 190:6881-6893(2008).
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; CP000802; ABV05925.1; -; Genomic_DNA.
DR RefSeq; WP_000558530.1; NC_009800.1.
DR AlphaFoldDB; A8A071; -.
DR SMR; A8A071; -.
DR KEGG; ecx:EcHS_A1600; -.
DR HOGENOM; CLU_131496_3_0_6; -.
DR OMA; DTVAPMM; -.
DR Proteomes; UP000001123; 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_0000351566"
FT DOMAIN 2..91
FT /note="ABM"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02051"
SQ SEQUENCE 96 AA; 11239 MW; 138099193F12430F CRC64;
MHVTLVEINV HEDKVDEFIE VFRQNHLGSV QEEGNLRFDV LQDPEVNSRF YIYEAYKDED
AVAFHKTTPH YKTSVAKLES LMTGPRKKRL FNGLMP
