ID A0A127MNR0_9PSED Unreviewed; 130 AA.
AC A0A127MNR0;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Lactoylglutathione lyase {ECO:0000256|ARBA:ARBA00012081, ECO:0000256|RuleBase:RU361179};
DE EC=4.4.1.5 {ECO:0000256|ARBA:ARBA00012081, ECO:0000256|RuleBase:RU361179};
DE AltName: Full=Glyoxalase I {ECO:0000256|RuleBase:RU361179};
GN Name=gloA {ECO:0000313|EMBL:WAB95246.1};
GN ORFNames=A9C11_07070 {ECO:0000313|EMBL:ANI13763.1}, OSS47_15115
GN {ECO:0000313|EMBL:WAB95246.1};
OS Pseudomonas citronellolis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=53408 {ECO:0000313|EMBL:WAB95246.1, ECO:0000313|Proteomes:UP001164666};
RN [1] {ECO:0000313|EMBL:ANI13763.1, ECO:0000313|Proteomes:UP000077748}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SJTE-3 {ECO:0000313|EMBL:ANI13763.1,
RC ECO:0000313|Proteomes:UP000077748};
RA Liang R.;
RT "Genome Sequence of Pseudomonas citronellolis Strain SJTE-3, an Estrogens
RT and Persistent Organic Pollutants degradation strain.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:WAB95246.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=G5Li.T10 {ECO:0000313|EMBL:WAB95246.1};
RA Leung K.M., Lai G.K.K., Leung F.C.C., Griffin S.D.J.;
RT "Complete genome sequence of Pseudomonas citronellolis G5Li.T10, a toluene-
RT degrading strain isolated from Hong Kong soil.";
RL Submitted (NOV-2022) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the conversion of hemimercaptal, formed from
CC methylglyoxal and glutathione, to S-lactoylglutathione.
CC {ECO:0000256|RuleBase:RU361179}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-S-lactoylglutathione = glutathione + methylglyoxal;
CC Xref=Rhea:RHEA:19069, ChEBI:CHEBI:17158, ChEBI:CHEBI:57474,
CC ChEBI:CHEBI:57925; EC=4.4.1.5;
CC Evidence={ECO:0000256|ARBA:ARBA00000817,
CC ECO:0000256|RuleBase:RU361179};
CC -!- COFACTOR:
CC Name=Ni(2+); Xref=ChEBI:CHEBI:49786;
CC Evidence={ECO:0000256|RuleBase:RU361179};
CC Note=Binds 1 nickel ion per subunit. {ECO:0000256|RuleBase:RU361179};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR604361-3};
CC Note=Binds 1 zinc ion per subunit. In the homodimer, two zinc ions are
CC bound between subunits. {ECO:0000256|PIRSR:PIRSR604361-3};
CC -!- PATHWAY: Secondary metabolite metabolism; methylglyoxal degradation;
CC (R)-lactate from methylglyoxal: step 1/2.
CC {ECO:0000256|ARBA:ARBA00005008, ECO:0000256|RuleBase:RU361179}.
CC -!- SIMILARITY: Belongs to the glyoxalase I family.
CC {ECO:0000256|ARBA:ARBA00010363, ECO:0000256|RuleBase:RU361179}.
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DR EMBL; CP015878; ANI13763.1; -; Genomic_DNA.
DR EMBL; CP113096; WAB95246.1; -; Genomic_DNA.
DR RefSeq; WP_009618415.1; NZ_PISI01000019.1.
DR STRING; 53408.A9C11_07070; -.
DR GeneID; 72994579; -.
DR KEGG; pcq:PcP3B5_14130; -.
DR UniPathway; UPA00619; UER00675.
DR Proteomes; UP000077748; Chromosome.
DR Proteomes; UP001164666; Chromosome.
DR GO; GO:0004462; F:lactoylglutathione lyase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR CDD; cd16358; GlxI_Ni; 1.
DR Gene3D; 3.10.180.10; 2,3-Dihydroxybiphenyl 1,2-Dioxygenase, domain 1; 1.
DR InterPro; IPR029068; Glyas_Bleomycin-R_OHBP_Dase.
DR InterPro; IPR004360; Glyas_Fos-R_dOase_dom.
DR InterPro; IPR004361; Glyoxalase_1.
DR InterPro; IPR018146; Glyoxalase_1_CS.
DR InterPro; IPR037523; VOC.
DR NCBIfam; TIGR00068; glyox_I; 1.
DR PANTHER; PTHR46036; LACTOYLGLUTATHIONE LYASE; 1.
DR PANTHER; PTHR46036:SF5; LACTOYLGLUTATHIONE LYASE; 1.
DR Pfam; PF00903; Glyoxalase; 1.
DR SUPFAM; SSF54593; Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase; 1.
DR PROSITE; PS00934; GLYOXALASE_I_1; 1.
DR PROSITE; PS00935; GLYOXALASE_I_2; 1.
DR PROSITE; PS51819; VOC; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU361179};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR604361-3,
KW ECO:0000256|RuleBase:RU361179}; Nickel {ECO:0000256|RuleBase:RU361179};
KW Zinc {ECO:0000256|PIRSR:PIRSR604361-3}.
FT DOMAIN 2..126
FT /note="VOC"
FT /evidence="ECO:0000259|PROSITE:PS51819"
FT ACT_SITE 122
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR604361-1"
FT BINDING 56
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000256|PIRSR:PIRSR604361-3"
FT BINDING 74
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000256|PIRSR:PIRSR604361-3"
FT BINDING 122
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000256|PIRSR:PIRSR604361-3"
SQ SEQUENCE 130 AA; 14712 MW; 9FBFA4BF4DC47BEE CRC64;
MRLLHTMLRV GDMDKSIAFY TEVLGMTLLR RKDYPDGQFT LAFVGYGAED ENSVIELTYN
WGVDKYELGT GYGHIALEVD DVYKACEDIR SRGGKITREP GPMKHGTSIL AFVEDPDGYK
IELLSPQRKD
//
