ID A0A0A8E5R4_9GAMM Unreviewed; 219 AA.
AC A0A0A8E5R4;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=Glyoxalase {ECO:0000256|PIRNR:PIRNR006320};
GN ORFNames=SD28_06545 {ECO:0000313|EMBL:AJC49309.1};
OS Allofrancisella guangzhouensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Francisellaceae; Allofrancisella.
OX NCBI_TaxID=594679 {ECO:0000313|EMBL:AJC49309.1, ECO:0000313|Proteomes:UP000031104};
RN [1] {ECO:0000313|EMBL:AJC49309.1, ECO:0000313|Proteomes:UP000031104}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=08HL01032 {ECO:0000313|EMBL:AJC49309.1,
RC ECO:0000313|Proteomes:UP000031104};
RA Svensson D., Ohrman C., Backman S., Karlsson E., Nilsson E., Bystrom M.,
RA Larkeryd A., Stenberg P., Scholtz H.C., Forsman M., Sjodin A.;
RT "Complete genome sequence of Francisella guanzhouensis strain 08HL01032
RT isolated from air-conditioning system in China.";
RL Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases.
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; CP010427; AJC49309.1; -; Genomic_DNA.
DR RefSeq; WP_039125251.1; NZ_JACVKK010000016.1.
DR AlphaFoldDB; A0A0A8E5R4; -.
DR STRING; 594679.SD28_06545; -.
DR KEGG; fgu:SD28_06545; -.
DR HOGENOM; CLU_072952_1_0_6; -.
DR OrthoDB; 5605062at2; -.
DR Proteomes; UP000031104; 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; IPR002818; DJ-1/PfpI.
DR InterPro; IPR026041; ElbB.
DR PANTHER; PTHR10224; ES1 PROTEIN HOMOLOG, MITOCHONDRIAL; 1.
DR PANTHER; PTHR10224:SF12; GLYOXALASE ELBB; 1.
DR Pfam; PF01965; DJ-1_PfpI; 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}.
FT DOMAIN 15..164
FT /note="DJ-1/PfpI"
FT /evidence="ECO:0000259|Pfam:PF01965"
SQ SEQUENCE 219 AA; 23551 MW; 8546BA7D1722E14E CRC64;
MAKVAVVLSG CGHLDGTEIH EAILTILALE KQGVEWQGVA LNENQKQVVN HLNQSVDSKA
SPRNILEESA RITRGNVIDL AEADSDNYDA VIFPGGFGAA KNIMDFAFVG DDSYQMNEEV
LKFARAFYLA DKPAGYICIS PLMIPLVYPE GTKVTVGNDK NTAVILGKKG AEAVIMDATD
ICVDEGVKVV STPAYMCAKN ILEAAQGIEK LVEKVVSYI
//
