ID Q4ZZQ9_PSEU2 Unreviewed; 222 AA.
AC Q4ZZQ9;
DT 07-JUN-2005, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2005, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE RecName: Full=Glyoxalase {ECO:0000256|PIRNR:PIRNR006320};
GN OrderedLocusNames=Psyr_0290 {ECO:0000313|EMBL:AAY35363.1};
OS Pseudomonas syringae pv. syringae (strain B728a).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX NCBI_TaxID=205918 {ECO:0000313|EMBL:AAY35363.1, ECO:0000313|Proteomes:UP000000426};
RN [1] {ECO:0000313|EMBL:AAY35363.1, ECO:0000313|Proteomes:UP000000426}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B728a {ECO:0000313|EMBL:AAY35363.1,
RC ECO:0000313|Proteomes:UP000000426};
RX PubMed=16043691; DOI=10.1073/pnas.0504930102;
RA Feil H., Feil W.S., Chain P., Larimer F., Dibartolo G., Copeland A.,
RA Lykidis A., Trong S., Nolan M., Goltsman E., Thiel J., Malfatti S.,
RA Loper J.E., Lapidus A., Detter J.C., Land M., Richardson P.M.,
RA Kyrpides N.C., Ivanova N., Lindow S.E.;
RT "Comparison of the complete genome sequences of Pseudomonas syringae pv.
RT syringae B728a and pv. tomato DC3000.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:11064-11069(2005).
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; CP000075; AAY35363.1; -; Genomic_DNA.
DR RefSeq; WP_011266301.1; NC_007005.1.
DR RefSeq; YP_233401.1; NC_007005.1.
DR AlphaFoldDB; Q4ZZQ9; -.
DR STRING; 205918.Psyr_0290; -.
DR KEGG; psb:Psyr_0290; -.
DR PATRIC; fig|205918.7.peg.292; -.
DR eggNOG; COG3155; Bacteria.
DR HOGENOM; CLU_072952_1_0_6; -.
DR OrthoDB; 5605062at2; -.
DR Proteomes; UP000000426; 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 16..153
FT /note="DJ-1/PfpI"
FT /evidence="ECO:0000259|Pfam:PF01965"
SQ SEQUENCE 222 AA; 23298 MW; A4272ACA947F49ED CRC64;
MQKKVAVILS GCGVYDGAEI HESVLTLLRL DQRGAQVQCF APDINQHHVV NHLTGEEMPE
SRNVLVESAR IARGEVKDIR EANAEDFDAL IIPGGFGSAK NLSDLALQGP ACQVEAGLLE
LAEAFAEAGK PVGLICITPA LAAKIYGPGV TCTIGNDPET AAAITKMGGS HAECAVDDIV
EDEARKLVST PAYMVAKSIS EAASGINKLV DRVLELTHEG DA
//
