ID LGUL_ECOLI Reviewed; 135 AA. AC P0AC81; P77036; Q2MB62; Q59384; DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot. DT 08-NOV-2005, sequence version 1. DT 26-FEB-2008, entry version 26. DE Lactoylglutathione lyase (EC 4.4.1.5) (Methylglyoxalase) DE (Aldoketomutase) (Glyoxalase I) (Glx I) (Ketone-aldehyde mutase) (S-D- DE lactoylglutathione methylglyoxal lyase). GN Name=gloA; OrderedLocusNames=b1651, JW1643; OS Escherichia coli (strain K12). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83333; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX MEDLINE=97199376; PubMed=9047352; DOI=10.1016/S0378-1119(96)00691-9; RA Clugston S.L., Daub E., Kinach R., Miedema D., Barnard J.F.J., RA Honek J.F.; RT "Isolation and sequencing of a gene coding for glyoxalase I activity RT from Salmonella typhimurium and comparison with other glyoxalase I RT sequences."; RL Gene 186:103-111(1997). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-11, RP CHARACTERIZATION, AND MASS SPECTROMETRY. RX MEDLINE=98292407; PubMed=9628737; DOI=10.1021/bi972791w; RA Clugston S.L., Barnard J.F.J., Kinach R., Miedema D., Ruman R., RA Daub E., Honek J.F.; RT "Overproduction and characterization of a dimeric non-zinc glyoxalase RT I from Escherichia coli: evidence for optimal activation by nickel RT ions."; RL Biochemistry 37:8754-8763(1998). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX MEDLINE=97426617; PubMed=9278503; DOI=10.1126/science.277.5331.1453; RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., RA Mau B., Shao Y.; RT "The complete genome sequence of Escherichia coli K-12."; RL Science 277:1453-1474(1997). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=16738553; DOI=10.1038/msb4100049; RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; RT "Highly accurate genome sequences of Escherichia coli K-12 strains RT MG1655 and W3110."; RL Mol. Syst. Biol. 2:E1-E5(2006). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-20. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RA Mizugaki M., Miura K., Yonezawa M., Hishinuma T., Tomioka Y.; RL Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases. RN [6] RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS). RX MEDLINE=20374551; PubMed=10913283; DOI=10.1021/bi000856g; RA He M.M., Clugston S.L., Honek J.F., Matthews B.W.; RT "Determination of the structure of Escherichia coli glyoxalase I RT suggests a structural basis for differential metal activation."; RL Biochemistry 39:8719-8727(2000). CC -!- FUNCTION: Catalyzes the conversion of hemimercaptal, formed from CC methylglyoxal and glutathione, to S-lactoylglutathione. CC -!- CATALYTIC ACTIVITY: (R)-S-lactoylglutathione = glutathione + CC methylglyoxal. CC -!- COFACTOR: Binds 1 nickel ion per subunit. CC -!- PATHWAY: Secondary metabolite metabolism; methylglyoxal CC degradation; D-lactate from methylglyoxal: step 1/2. CC -!- SUBUNIT: Homodimer. CC -!- INTERACTION: CC P0A6Y8:dnaK; NbExp=1; IntAct=EBI-551143, EBI-542092; CC P32156:yiiL; NbExp=1; IntAct=EBI-551143, EBI-1134000; CC -!- MASS SPECTROMETRY: Mass=14919; Method=Electrospray; Range=1-135; CC Source=PubMed:9628737; CC -!- SIMILARITY: Belongs to the glyoxalase I family. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U57363; AAC27133.1; -; Genomic_DNA. DR EMBL; U00096; AAC74723.1; -; Genomic_DNA. DR EMBL; AP009048; BAE76494.1; -; Genomic_DNA. DR EMBL; D86931; BAA13187.1; -; Genomic_DNA. DR PIR; E64922; E64922. DR RefSeq; AP_002273.1; -. DR RefSeq; NP_416168.1; -. DR PDB; 1F9Z; X-ray; 1.50 A; A/B=1-135. DR PDB; 1FA5; X-ray; 1.80 A; A/B=1-135. DR PDB; 1FA6; X-ray; 1.90 A; A/B=1-135. DR PDB; 1FA7; X-ray; 1.90 A; A/B=1-135. DR PDB; 1FA8; X-ray; 1.70 A; A/B=1-135. DR PDBsum; 1F9Z; -. DR PDBsum; 1FA5; -. DR PDBsum; 1FA6; -. DR PDBsum; 1FA7; -. DR PDBsum; 1FA8; -. DR IntAct; P0AC81; -. DR GeneID; 946161; -. DR GenomeReviews; U00096_GR; b1651. DR GenomeReviews; AP009048_GR; JW1643. DR KEGG; ecj:JW1643; -. DR KEGG; eco:b1651; -. DR EchoBASE; EB3197; -. DR EcoGene; EG13421; gloA. DR BioCyc; EcoCyc:GLYOXI-MON; -. DR LinkHub; P0AC81; -. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR InterPro; IPR011588; Gly_Xdiol_dOase. DR InterPro; IPR004360; Glyas_bleo-R_dOase. DR InterPro; IPR004361; Glyoxalase_1. DR Pfam; PF00903; Glyoxalase; 1. DR ProDom; PD002334; Gly_diox; 1. DR TIGRFAMs; TIGR00068; glyox_I; 1. DR PROSITE; PS00934; GLYOXALASE_I_1; 1. DR PROSITE; PS00935; GLYOXALASE_I_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Direct protein sequencing; Lyase; KW Metal-binding; Nickel. FT CHAIN 1 135 Lactoylglutathione lyase. FT /FTId=PRO_0000168088. FT METAL 5 5 Nickel. FT METAL 56 56 Nickel. FT METAL 74 74 Nickel. FT METAL 122 122 Nickel. FT STRAND 3 9 FT HELIX 13 22 FT STRAND 27 34 FT TURN 35 38 FT STRAND 39 47 FT TURN 49 51 FT STRAND 54 60 FT STRAND 70 78 FT HELIX 82 91 FT STRAND 95 102 FT STRAND 109 114 FT STRAND 120 125 SQ SEQUENCE 135 AA; 14920 MW; A53FC5412B9A6CE3 CRC64; MRLLHTMLRV GDLQRSIDFY TKVLGMKLLR TSENPEYKYS LAFVGYGPET EEAVIELTYN WGVDKYELGT AYGHIALSVD NAAEACEKIR QNGGNVTREA GPVKGGTTVI AFVEDPDGYK IELIEEKDAG RGLGN //