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Entry: A0A0B5CQJ4_NEIEG
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ID   A0A0B5CQJ4_NEIEG        Unreviewed;       135 AA.
AC   A0A0B5CQJ4;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 33.
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   ORFNames=NELON_06170 {ECO:0000313|EMBL:AJE18516.1};
OS   Neisseria elongata subsp. glycolytica ATCC 29315.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=546263 {ECO:0000313|EMBL:AJE18516.1, ECO:0000313|Proteomes:UP000031392};
RN   [1] {ECO:0000313|Proteomes:UP000031392}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29315 {ECO:0000313|Proteomes:UP000031392};
RA   Veyrier F.J., Taha M.-K.;
RT   "Complete Genome sequence of Neisseria elongata subsp. glycolytica.";
RL   Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AJE18516.1, ECO:0000313|Proteomes:UP000031392}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29315 {ECO:0000313|EMBL:AJE18516.1,
RC   ECO:0000313|Proteomes:UP000031392};
RX   PubMed=26162030;
RA   Veyrier F.J., Biais N., Morales P., Belkacem N., Guilhen C., Ranjeva S.,
RA   Sismeiro O., Pehau-Arnaudet G., Rocha E.P., Werts C., Taha M.K.,
RA   Boneca I.G.;
RT   "Common Cell Shape Evolution of Two Nasopharyngeal Pathogens.";
RL   PLoS Genet. 11:E1005338-E1005338(2015).
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; CP007726; AJE18516.1; -; Genomic_DNA.
DR   RefSeq; WP_041961386.1; NZ_CP007726.1.
DR   AlphaFoldDB; A0A0B5CQJ4; -.
DR   KEGG; nel:NELON_06170; -.
DR   PATRIC; fig|546263.7.peg.1315; -.
DR   HOGENOM; CLU_046006_8_1_4; -.
DR   UniPathway; UPA00619; UER00675.
DR   Proteomes; UP000031392; 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:UP000031392};
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;  15346 MW;  5D4414BE2BF872D1 CRC64;
     MRMLHTMLRV GDLKKSLEFY QDVLGMRLLR QKDYPEGRFT LAFVGYGSEA KSTVLELTHN
     WDTESYDLGN AYGHIAIEVD DAYKACDRVK EKGGKVVREA GPMMHGTTVI AFVEDPDGYK
     IEFIQKNTGK DSVQY
//
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