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Database: UniProt
Entry: Q607V5_METCA
LinkDB: Q607V5_METCA
Original site: Q607V5_METCA 
ID   Q607V5_METCA            Unreviewed;       130 AA.
AC   Q607V5;
DT   23-NOV-2004, integrated into UniProtKB/TrEMBL.
DT   23-NOV-2004, sequence version 1.
DT   24-JAN-2024, entry version 97.
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:AAU92327.1};
GN   OrderedLocusNames=MCA1648 {ECO:0000313|EMBL:AAU92327.1};
OS   Methylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Methylococcales;
OC   Methylococcaceae; Methylococcus.
OX   NCBI_TaxID=243233 {ECO:0000313|EMBL:AAU92327.1, ECO:0000313|Proteomes:UP000006821};
RN   [1] {ECO:0000313|EMBL:AAU92327.1, ECO:0000313|Proteomes:UP000006821}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33009 / NCIMB 11132 / Bath
RC   {ECO:0000313|Proteomes:UP000006821};
RX   PubMed=15383840; DOI=10.1371/journal.pbio.0020303;
RA   Ward N.L., Larsen O., Sakwa J., Bruseth L., Khouri H.M., Durkin A.S.,
RA   Dimitrov G., Jiang L., Scanlan D., Kang K.H., Lewis M.R., Nelson K.E.,
RA   Methe B.A., Wu M., Heidelberg J.F., Paulsen I.T., Fouts D.E., Ravel J.,
RA   Tettelin H., Ren Q., Read T.D., DeBoy R.T., Seshadri R., Salzberg S.L.,
RA   Jensen H.B., Birkeland N.K., Nelson W.C., Dodson R.J., Grindhaug S.H.,
RA   Holt I.E., Eidhammer I., Jonasen I., Vanaken S., Utterback T.R.,
RA   Feldblyum T.V., Fraser C.M., Lillehaug J.R., Eisen J.A.;
RT   "Genomic insights into methanotrophy: the complete genome sequence of
RT   Methylococcus capsulatus (Bath).";
RL   PLoS Biol. 2:1616-1628(2004).
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; AE017282; AAU92327.1; -; Genomic_DNA.
DR   RefSeq; WP_010960907.1; NC_002977.6.
DR   AlphaFoldDB; Q607V5; -.
DR   STRING; 243233.MCA1648; -.
DR   KEGG; mca:MCA1648; -.
DR   eggNOG; COG0346; Bacteria.
DR   HOGENOM; CLU_046006_8_1_6; -.
DR   OMA; NWGTESY; -.
DR   UniPathway; UPA00619; UER00675.
DR   Proteomes; UP000006821; 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:UP000006821};
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;  14514 MW;  FE76646D40ED91D7 CRC64;
     MRILHTMLRV GDLQKSLWFY TEVLGMRLLR QMEFPDGEFT LAFVGYGDEA HDAVIELTYN
     WGVSKYELGT GFGHIALGVD DIHAAVERIR ALGGEIVREP GPMKHGTTVI AFVADPDGYR
     IELIEHKPAG
//
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