LGUL_PSEAE
ID LGUL_PSEAE Reviewed; 176 AA.
AC Q9HU72;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Lactoylglutathione lyase;
DE EC=4.4.1.5;
DE AltName: Full=Aldoketomutase;
DE AltName: Full=Glyoxalase I;
DE Short=Glx I;
DE AltName: Full=Ketone-aldehyde mutase;
DE AltName: Full=Methylglyoxalase;
DE AltName: Full=S-D-lactoylglutathione methylglyoxal lyase;
GN Name=gloA; OrderedLocusNames=PA5111;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
CC -!- FUNCTION: Catalyzes the conversion of hemimercaptal, formed from
CC methylglyoxal and glutathione, to S-lactoylglutathione. {ECO:0000250}.
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 -!- COFACTOR:
CC Name=Ni(2+); Xref=ChEBI:CHEBI:49786; Evidence={ECO:0000250};
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 nickel or zinc ion per subunit. {ECO:0000250};
CC -!- PATHWAY: Secondary metabolite metabolism; methylglyoxal degradation;
CC (R)-lactate from methylglyoxal: step 1/2.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glyoxalase I family. {ECO:0000305}.
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DR EMBL; AE004091; AAG08496.1; -; Genomic_DNA.
DR PIR; F83006; F83006.
DR RefSeq; NP_253798.1; NC_002516.2.
DR RefSeq; WP_003101793.1; NZ_QZGE01000002.1.
DR AlphaFoldDB; Q9HU72; -.
DR SMR; Q9HU72; -.
DR STRING; 287.DR97_2465; -.
DR PaxDb; Q9HU72; -.
DR PRIDE; Q9HU72; -.
DR DNASU; 882241; -.
DR EnsemblBacteria; AAG08496; AAG08496; PA5111.
DR GeneID; 882241; -.
DR KEGG; pae:PA5111; -.
DR PATRIC; fig|208964.12.peg.5356; -.
DR PseudoCAP; PA5111; -.
DR HOGENOM; CLU_046006_1_1_6; -.
DR InParanoid; Q9HU72; -.
DR OMA; FLQQTMF; -.
DR PhylomeDB; Q9HU72; -.
DR BioCyc; PAER208964:G1FZ6-5226-MON; -.
DR BRENDA; 4.4.1.5; 5087.
DR SABIO-RK; Q9HU72; -.
DR UniPathway; UPA00619; UER00675.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0004462; F:lactoylglutathione lyase activity; IDA:PseudoCAP.
DR GO; GO:0008270; F:zinc ion binding; IDA:PseudoCAP.
DR GO; GO:0019243; P:methylglyoxal catabolic process to D-lactate via S-lactoyl-glutathione; IDA:PseudoCAP.
DR Gene3D; 3.10.180.10; -; 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 Pfam; PF00903; Glyoxalase; 1.
DR SUPFAM; SSF54593; SSF54593; 1.
DR TIGRFAMs; TIGR00068; glyox_I; 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; Metal-binding; Nickel; Reference proteome; Zinc.
FT CHAIN 1..176
FT /note="Lactoylglutathione lyase"
FT /id="PRO_0000287775"
FT DOMAIN 23..167
FT /note="VOC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
FT ACT_SITE 163
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250"
FT BINDING 26
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000250"
FT BINDING 30
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 92
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000250"
FT BINDING 96
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 114
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 118
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000250"
FT BINDING 118
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 163
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000250"
SQ SEQUENCE 176 AA; 20215 MW; 9C85130839474892 CRC64;
MSFNTEVQPG ICMEPDAITQ EYVFNHTMLR VKDPKRSLDF YSRVLGMRLL RRLDFEEGRF
SLYFLAMTRG EEVPDAVDER QRYTFGRQSV LELTHNWGSE SDDSQYHNGN QDPRGFGHIC
FSVPDLVAAC ERFETLGVNF VKPLDRGMKN VAFISDPDGY WVEIVQASLN GEMGRG
