ID H2FWA2_OCESG Unreviewed; 135 AA.
AC H2FWA2;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 27-MAR-2024, entry version 59.
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 OrderedLocusNames=GU3_10640 {ECO:0000313|EMBL:AEY01884.1};
OS Oceanimonas sp. (strain GK1 / IBRC-M 10197).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales;
OC Aeromonadaceae; Oceanimonas.
OX NCBI_TaxID=511062 {ECO:0000313|EMBL:AEY01884.1, ECO:0000313|Proteomes:UP000007742};
RN [1] {ECO:0000313|EMBL:AEY01884.1, ECO:0000313|Proteomes:UP000007742}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GK1 {ECO:0000313|EMBL:AEY01884.1,
RC ECO:0000313|Proteomes:UP000007742};
RX PubMed=22461556; DOI=10.1128/JB.00023-12;
RA Parsa Yeganeh L., Azarbaijani R., Sarikhan S., Mousavi H., Ramezani M.,
RA Amoozegar M.A., Shahzadeh Fazeli A., Salekdeh G.H.;
RT "Complete genome sequence of Oceanimonas sp. GK1, a halotolerant bacterium
RT from Gavkhouni Wetland in Iran.";
RL J. Bacteriol. 194:2123-2124(2012).
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; CP003171; AEY01884.1; -; Genomic_DNA.
DR RefSeq; WP_014292603.1; NC_016745.1.
DR AlphaFoldDB; H2FWA2; -.
DR STRING; 511062.GU3_10640; -.
DR KEGG; oce:GU3_10640; -.
DR eggNOG; COG0346; Bacteria.
DR HOGENOM; CLU_046006_8_1_6; -.
DR OrthoDB; 9789841at2; -.
DR UniPathway; UPA00619; UER00675.
DR Proteomes; UP000007742; 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 Reference proteome {ECO:0000313|Proteomes:UP000007742};
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 135 AA; 14863 MW; 34122618E005F9D9 CRC64;
MRILHTMLRV GNLDKSIAFY TNIMGMKLLR TSENAEYQYT LAFVGYGEEK DQAVLELTYN
WGTDSYDLGN AYGHIAIEAE DIYGMCEQIR AAGGKVTREP GPVKGGTTVI AFVEDPDGYK
IELIAKKDAG KGLGE
//