ID   ELBB_KLEOX              Reviewed;          80 AA.
AC   Q48464;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   25-MAY-2022, entry version 52.
DE   RecName: Full=Putative glyoxalase ElbB {ECO:0000250|UniProtKB:P0ABU5};
DE            EC=4.2.1.- {ECO:0000250|UniProtKB:P0ABU5};
DE   Flags: Fragment;
GN   Name=elbB;
OS   Klebsiella oxytoca.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=571;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=M5a1;
RX   PubMed=8830253; DOI=10.1046/j.1365-2958.1996.442924.x;
RA   Spratt B.G., Zhou J., Taylor M., Merrick M.J.;
RT   "Monofunctional biosynthetic peptidoglycan transglycosylases.";
RL   Mol. Microbiol. 19:639-640(1996).
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; Z54198; CAA90902.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q48464; -.
DR   SMR; Q48464; -.
DR   STRING; 571.MC52_05325; -.
DR   eggNOG; COG3155; Bacteria.
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   SUPFAM; SSF52317; SSF52317; 1.
PE   3: Inferred from homology;
KW   Lyase.
FT   CHAIN           <1..80
FT                   /note="Putative glyoxalase ElbB"
FT                   /id="PRO_0000201683"
FT   NON_TER         1
SQ   SEQUENCE   80 AA;  8552 MW;  8913C95EEF93DC1B CRC64;
     SLHRPPGCRH CVGQLRLCDL DTADAVEEMG AEHVPCPVDD IVVDEDNKVV TTPAYMLAQN
     IAEAASGIEK LVARVLVLTA