ID H0J2R0_9GAMM Unreviewed; 219 AA.
AC H0J2R0;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE RecName: Full=Glyoxalase {ECO:0000256|PIRNR:PIRNR006320};
GN ORFNames=MOY_09610 {ECO:0000313|EMBL:EHK60758.1};
OS Halomonas sp. GFAJ-1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=1118153 {ECO:0000313|EMBL:EHK60758.1, ECO:0000313|Proteomes:UP000004512};
RN [1] {ECO:0000313|EMBL:EHK60758.1, ECO:0000313|Proteomes:UP000004512}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GFAJ-1 {ECO:0000313|EMBL:EHK60758.1,
RC ECO:0000313|Proteomes:UP000004512};
RX PubMed=22408239; DOI=10.1128/JB.06664-11;
RA Phung le T., Silver S., Trimble W.L., Gilbert J.A.;
RT "Draft Genome of Halomonas Species Strain GFAJ-1 (ATCC BAA-2256).";
RL J. Bacteriol. 194:1835-1836(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:EHK60758.1}.
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DR EMBL; AHBC01000035; EHK60758.1; -; Genomic_DNA.
DR RefSeq; WP_009099109.1; NZ_CP016490.1.
DR AlphaFoldDB; H0J2R0; -.
DR STRING; 1118153.MOY_09610; -.
DR KEGG; hag:BB497_06600; -.
DR PATRIC; fig|1118153.6.peg.1951; -.
DR eggNOG; COG3155; Bacteria.
DR OrthoDB; 5605062at2; -.
DR Proteomes; UP000004512; 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:UP000004512};
KW Transferase {ECO:0000313|EMBL:EHK60758.1}.
SQ SEQUENCE 219 AA; 23475 MW; 9FA8CB4F73494D23 CRC64;
MTKQVAIVLA GCGVFDGSEI YETTLTLLRL DQLGIGYRCF APDVEQHHVI NHVTQSPVER
EARNVLQESA RLARGEISPI TELNADEFDA VIVPGGFGAA KNLSDFATQG DSMQVLESLK
DALAGFKQDA KPIGLMCIAP VMVPRLLGEG IAVTIGHDPA VSGAISAMGG LHRSCSVEDI
VVDLEHRVVT TPAYMLATRI SEAATGIFKL VDRIDEMME
//
