ID B7NDJ3_ECOLU Unreviewed; 217 AA.
AC B7NDJ3;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=Glyoxalase {ECO:0000256|PIRNR:PIRNR006320};
GN Name=elbB {ECO:0000313|EMBL:CAR14843.1};
GN OrderedLocusNames=ECUMN_3689 {ECO:0000313|EMBL:CAR14843.1};
OS Escherichia coli O17:K52:H18 (strain UMN026 / ExPEC).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585056 {ECO:0000313|EMBL:CAR14843.1, ECO:0000313|Proteomes:UP000007097};
RN [1] {ECO:0000313|Proteomes:UP000007097}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UMN026 / ExPEC {ECO:0000313|Proteomes:UP000007097};
RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT "Organised genome dynamics in the Escherichia coli species results in
RT highly diverse adaptive paths.";
RL PLoS Genet. 5:E1000344-E1000344(2009).
CC -!- FUNCTION: Displays glyoxalase activity, catalyzing the conversion of
CC glyoxal to glycolate. {ECO:0000256|PIRNR:PIRNR006320}.
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:0000256|PIRNR:PIRNR006320};
CC -!- SIMILARITY: Belongs to the peptidase C56 family.
CC {ECO:0000256|PIRNR:PIRNR006320}.
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DR EMBL; CU928163; CAR14843.1; -; Genomic_DNA.
DR RefSeq; WP_001300411.1; NC_011751.1.
DR RefSeq; YP_002414348.1; NC_011751.1.
DR AlphaFoldDB; B7NDJ3; -.
DR SMR; B7NDJ3; -.
DR STRING; 585056.ECUMN_3689; -.
DR MEROPS; C56.975; -.
DR KEGG; eum:ECUMN_3689; -.
DR PATRIC; fig|585056.7.peg.3869; -.
DR HOGENOM; CLU_072952_1_0_6; -.
DR Proteomes; UP000007097; Chromosome.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-UniRule.
DR CDD; cd03133; GATase1_ES1; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR026041; ElbB.
DR PANTHER; PTHR10224; ES1 PROTEIN HOMOLOG, MITOCHONDRIAL; 1.
DR PANTHER; PTHR10224:SF12; GLYOXALASE ELBB; 1.
DR PIRSF; PIRSF006320; Elb2; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|PIRNR:PIRNR006320}.
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
//
