ID E3BML3_9VIBR Unreviewed; 216 AA.
AC E3BML3;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=Glyoxalase {ECO:0000256|PIRNR:PIRNR006320};
GN ORFNames=VIBC2010_17445 {ECO:0000313|EMBL:EFP95758.1};
OS Vibrio caribbeanicus ATCC BAA-2122.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=796620 {ECO:0000313|EMBL:EFP95758.1, ECO:0000313|Proteomes:UP000002943};
RN [1] {ECO:0000313|EMBL:EFP95758.1, ECO:0000313|Proteomes:UP000002943}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-2122 {ECO:0000313|EMBL:EFP95758.1,
RC ECO:0000313|Proteomes:UP000002943};
RX PubMed=21930677; DOI=10.1099/ijs.0.032375-0;
RA Hoffmann M., Monday S.R., Allard M.W., Strain E.A., Whittaker P., Naum M.,
RA McCarthy P.J., Lopez J.V., Fischer M., Brown E.W.;
RT "Vibrio caribbeanicus sp. nov., isolated from the marine sponge
RT Scleritoderma cyanea.";
RL Int. J. Syst. Evol. Microbiol. 62:1736-1743(2012).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EFP95758.1}.
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DR EMBL; AEIU01000088; EFP95758.1; -; Genomic_DNA.
DR RefSeq; WP_009602355.1; NZ_AEIU01000088.1.
DR AlphaFoldDB; E3BML3; -.
DR STRING; 796620.VIBC2010_17445; -.
DR eggNOG; COG3155; Bacteria.
DR OrthoDB; 5605062at2; -.
DR Proteomes; UP000002943; Unassembled WGS sequence.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000002943};
KW Transferase {ECO:0000313|EMBL:EFP95758.1}.
SQ SEQUENCE 216 AA; 23094 MW; AD00D1644DDCE6E3 CRC64;
MKKIAVVLSG SGVYDGSEIH EAVLSLLAIE KHGAQWHCFA PNINQHHVIN HITGEEMDTT
RNVLIESARI ARGNISDITT LDVNQYDALL LPGGFGAAKN LTDFAFKGAQ CTINESVATA
CRAFAEVKKP AGYICIAPVI IPMIYSKGVQ GTIGDNKEAS DAFNALGGQH ISSSIEDVVF
DPEHRVLSTS AYMATENLLE ASVGIESLVK QLVEIA
//
