LSRG_YERPE
ID LSRG_YERPE Reviewed; 96 AA.
AC Q7CG46; Q74PW0;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 98.
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};
GN OrderedLocusNames=YPO0407, y3774, YP_3774;
OS Yersinia pestis.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=632;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CO-92 / Biovar Orientalis;
RX PubMed=11586360; DOI=10.1038/35097083;
RA Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G.,
RA Prentice M.B., Sebaihia M., James K.D., Churcher C.M., Mungall K.L.,
RA Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.-M.,
RA Chillingworth T., Cronin A., Davies R.M., Davis P., Dougan G., Feltwell T.,
RA Hamlin N., Holroyd S., Jagels K., Karlyshev A.V., Leather S., Moule S.,
RA Oyston P.C.F., Quail M.A., Rutherford K.M., Simmonds M., Skelton J.,
RA Stevens K., Whitehead S., Barrell B.G.;
RT "Genome sequence of Yersinia pestis, the causative agent of plague.";
RL Nature 413:523-527(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KIM10+ / Biovar Mediaevalis;
RX PubMed=12142430; DOI=10.1128/jb.184.16.4601-4611.2002;
RA Deng W., Burland V., Plunkett G. III, Boutin A., Mayhew G.F., Liss P.,
RA Perna N.T., Rose D.J., Mau B., Zhou S., Schwartz D.C., Fetherston J.D.,
RA Lindler L.E., Brubaker R.R., Plano G.V., Straley S.C., McDonough K.A.,
RA Nilles M.L., Matson J.S., Blattner F.R., Perry R.D.;
RT "Genome sequence of Yersinia pestis KIM.";
RL J. Bacteriol. 184:4601-4611(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=91001 / Biovar Mediaevalis;
RX PubMed=15368893; DOI=10.1093/dnares/11.3.179;
RA Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D.,
RA Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z., Jin L.,
RA Dai R., Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J., Yang H.,
RA Wang J., Huang P., Yang R.;
RT "Complete genome sequence of Yersinia pestis strain 91001, an isolate
RT avirulent to humans.";
RL DNA Res. 11:179-197(2004).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS), AND SUBUNIT.
RC STRAIN=D27;
RA de Carvalho-Kavanagh M., Schafer J., Lekin T., Toppani D., Coleman M.,
RA Chain P., Lao V., Zemla A., Motin V., Garcia E., Segelke B.;
RT "Crystal structure of lsrG from Yersinia pestis.";
RL Submitted (APR-2007) to the PDB data bank.
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; AL590842; CAL19088.1; -; Genomic_DNA.
DR EMBL; AE009952; AAM87319.1; -; Genomic_DNA.
DR EMBL; AE017042; AAS63922.1; -; Genomic_DNA.
DR PIR; AF0050; AF0050.
DR RefSeq; WP_002209186.1; NZ_WUCM01000002.1.
DR RefSeq; YP_002345484.1; NC_003143.1.
DR PDB; 2GFF; X-ray; 1.75 A; A/B=1-96.
DR PDBsum; 2GFF; -.
DR AlphaFoldDB; Q7CG46; -.
DR SMR; Q7CG46; -.
DR STRING; 214092.YPO0407; -.
DR PaxDb; Q7CG46; -.
DR DNASU; 1148721; -.
DR EnsemblBacteria; AAM87319; AAM87319; y3774.
DR EnsemblBacteria; AAS63922; AAS63922; YP_3774.
DR GeneID; 66843034; -.
DR KEGG; ype:YPO0407; -.
DR KEGG; ypk:y3774; -.
DR KEGG; ypm:YP_3774; -.
DR PATRIC; fig|214092.21.peg.647; -.
DR eggNOG; COG1359; Bacteria.
DR HOGENOM; CLU_131496_3_0_6; -.
DR OMA; DTVAPMM; -.
DR EvolutionaryTrace; Q7CG46; -.
DR Proteomes; UP000000815; Chromosome.
DR Proteomes; UP000001019; Chromosome.
DR Proteomes; UP000002490; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0003824; F:catalytic activity; IBA:GO_Central.
DR GO; GO:0016861; F:intramolecular oxidoreductase activity, interconverting aldoses and ketoses; IEA:UniProtKB-UniRule.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Isomerase; Reference proteome.
FT CHAIN 1..96
FT /note="(4S)-4-hydroxy-5-phosphonooxypentane-2,3-dione
FT isomerase"
FT /id="PRO_0000351577"
FT DOMAIN 2..91
FT /note="ABM"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02051"
FT CONFLICT 82
FT /note="M -> I (in Ref. 3; AAS63922)"
FT /evidence="ECO:0000305"
FT STRAND 2..10
FT /evidence="ECO:0007829|PDB:2GFF"
FT HELIX 12..14
FT /evidence="ECO:0007829|PDB:2GFF"
FT HELIX 15..30
FT /evidence="ECO:0007829|PDB:2GFF"
FT STRAND 35..45
FT /evidence="ECO:0007829|PDB:2GFF"
FT STRAND 49..58
FT /evidence="ECO:0007829|PDB:2GFF"
FT HELIX 59..65
FT /evidence="ECO:0007829|PDB:2GFF"
FT HELIX 69..78
FT /evidence="ECO:0007829|PDB:2GFF"
FT HELIX 79..81
FT /evidence="ECO:0007829|PDB:2GFF"
FT STRAND 82..84
FT /evidence="ECO:0007829|PDB:2GFF"
FT STRAND 87..95
FT /evidence="ECO:0007829|PDB:2GFF"
SQ SEQUENCE 96 AA; 11098 MW; FB8E869AEC86AA21 CRC64;
MHVTLVEINV KEDKVDQFIE VFRANHLGSI REAGNLRFDV LRDEHIPTRF YIYEAYTDEA
AVAIHKTTPH YLQCVEQLAP LMTGPRKKTV FIGLMP
