ID   ELBB_SHIFL              Reviewed;         217 AA.
AC   P0ABU6; P26428; P76673;
DT   25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2005, sequence version 1.
DT   25-MAY-2022, entry version 88.
DE   RecName: Full=Glyoxalase ElbB {ECO:0000250|UniProtKB:P0ABU5};
DE            EC=4.2.1.- {ECO:0000250|UniProtKB:P0ABU5};
GN   Name=elbB; OrderedLocusNames=SF3249, S3467;
OS   Shigella flexneri.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=301 / Serotype 2a;
RX   PubMed=12384590; DOI=10.1093/nar/gkf566;
RA   Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA   Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA   Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA   Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT   "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT   through comparison with genomes of Escherichia coli K12 and O157.";
RL   Nucleic Acids Res. 30:4432-4441(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX   PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA   Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA   Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA   Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT   "Complete genome sequence and comparative genomics of Shigella flexneri
RT   serotype 2a strain 2457T.";
RL   Infect. Immun. 71:2775-2786(2003).
CC   -!- FUNCTION: Displays glyoxalase activity, catalyzing the conversion of
CC       glyoxal to glycolate. However, this apparent glyoxalase activity may
CC       reflect a deglycase activity, which could be the primary function of
CC       this protein like other DJ-1 superfamily members such as PARK7, YajL,
CC       YhbO and HchA. Is not able to use methylglyoxal as substrate.
CC       {ECO:0000250|UniProtKB:P0ABU5}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glyoxal + H2O = glycolate + H(+); Xref=Rhea:RHEA:51672,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805,
CC         ChEBI:CHEBI:34779; Evidence={ECO:0000250|UniProtKB:P0ABU5};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P0ABU5}.
CC   -!- SIMILARITY: Belongs to the peptidase C56 family. {ECO:0000305}.
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DR   EMBL; AE005674; AAN44714.2; -; Genomic_DNA.
DR   EMBL; AE014073; AAP18528.1; -; Genomic_DNA.
DR   RefSeq; NP_709007.2; NC_004337.2.
DR   RefSeq; WP_001300411.1; NZ_WPGW01000004.1.
DR   AlphaFoldDB; P0ABU6; -.
DR   SMR; P0ABU6; -.
DR   STRING; 198214.SF3249; -.
DR   MEROPS; C56.975; -.
DR   EnsemblBacteria; AAN44714; AAN44714; SF3249.
DR   EnsemblBacteria; AAP18528; AAP18528; S3467.
DR   GeneID; 1027090; -.
DR   GeneID; 58388186; -.
DR   KEGG; sfl:SF3249; -.
DR   KEGG; sfx:S3467; -.
DR   PATRIC; fig|198214.7.peg.3851; -.
DR   HOGENOM; CLU_072952_1_0_6; -.
DR   OMA; AQVQCFA; -.
DR   OrthoDB; 1421548at2; -.
DR   Proteomes; UP000001006; Chromosome.
DR   Proteomes; UP000002673; Chromosome.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.880; -; 1.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR026041; ElbB.
DR   PANTHER; PTHR10224:SF12; PTHR10224:SF12; 1.
DR   PIRSF; PIRSF006320; Elb2; 1.
DR   SUPFAM; SSF52317; SSF52317; 1.
PE   3: Inferred from homology;
KW   Lyase; Reference proteome.
FT   CHAIN           1..217
FT                   /note="Glyoxalase ElbB"
FT                   /id="PRO_0000201682"
FT   ACT_SITE        135
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P31658"
SQ   SEQUENCE   217 AA;  22982 MW;  48A7957C29384DAC CRC64;
     MKKIGVILSG CGVYDGSEIH EAVLTLLAIS RSGAQAVCFA PDKQQVDVIN HLTGEAMTET
     RNVLIEAARI TRGEIRPLAQ ADAAELDALI VPGGFGAAKN LSNFASLGSE CTVDRELKAL
     AQAMHQAGKP LGFMCIAPAM LPKIFDFPLR LTIGTDIDTA EVLEEMGAEH VPCPVDDIVV
     DEDNKIVTTP AYMLAQNIAE AASGIDKLVS RVLVLAE