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Database: UniProt
Entry: A8GDW1_SERP5
LinkDB: A8GDW1_SERP5
Original site: A8GDW1_SERP5 
ID   A8GDW1_SERP5            Unreviewed;       135 AA.
AC   A8GDW1;
DT   13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2007, sequence version 1.
DT   24-JAN-2024, entry version 78.
DE   RecName: Full=Lactoylglutathione lyase {ECO:0000256|ARBA:ARBA00018701};
DE            EC=4.4.1.5 {ECO:0000256|ARBA:ARBA00012081};
DE   AltName: Full=Aldoketomutase {ECO:0000256|ARBA:ARBA00030892};
DE   AltName: Full=Glyoxalase I {ECO:0000256|ARBA:ARBA00030537};
DE   AltName: Full=Ketone-aldehyde mutase {ECO:0000256|ARBA:ARBA00030291};
DE   AltName: Full=Methylglyoxalase {ECO:0000256|ARBA:ARBA00032460};
DE   AltName: Full=S-D-lactoylglutathione methylglyoxal lyase {ECO:0000256|ARBA:ARBA00033298};
GN   OrderedLocusNames=Spro_2200 {ECO:0000313|EMBL:ABV41301.1};
OS   Serratia proteamaculans (strain 568).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Serratia.
OX   NCBI_TaxID=399741 {ECO:0000313|EMBL:ABV41301.1};
RN   [1] {ECO:0000313|EMBL:ABV41301.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=568 {ECO:0000313|EMBL:ABV41301.1};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Taghavi S., Newman L.,
RA   Vangronsveld J., van der Lelie D., Richardson P.;
RT   "Complete sequence of chromosome of Serratia proteamaculans 568.";
RL   Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases.
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   -!- COFACTOR:
CC       Name=Ni(2+); Xref=ChEBI:CHEBI:49786;
CC         Evidence={ECO:0000256|ARBA:ARBA00001967};
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}.
CC   -!- SIMILARITY: Belongs to the glyoxalase I family.
CC       {ECO:0000256|ARBA:ARBA00010363}.
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DR   EMBL; CP000826; ABV41301.1; -; Genomic_DNA.
DR   AlphaFoldDB; A8GDW1; -.
DR   STRING; 399741.Spro_2200; -.
DR   KEGG; spe:Spro_2200; -.
DR   eggNOG; COG0346; Bacteria.
DR   HOGENOM; CLU_046006_8_1_6; -.
DR   OMA; NWGTESY; -.
DR   OrthoDB; 9789841at2; -.
DR   UniPathway; UPA00619; UER00675.
DR   GO; GO:0004462; F:lactoylglutathione lyase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; PS51819; VOC; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:ABV41301.1};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR604361-3};
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;  14771 MW;  1CE9AC87A5276DA6 CRC64;
     MRLLHTMIRV GDLQRSIDFY TKVLGMRLLR TSENPEYKYS LAFVGYTDES EGAVIELTYN
     WGTDSYEMGT AFGHLALGVD DVAATCDSIR NAGGKVTREA GPVKGGTTVI AFVEDPDGYK
     IELIENKHAG HGLGH
//
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