CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-003333
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Lactoylglutathione lyase 
Protein Synonyms/Alias
 Aldoketomutase; Glyoxalase I; Glx I; Ketone-aldehyde mutase; Methylglyoxalase; S-D-lactoylglutathione methylglyoxal lyase 
Gene Name
 gloA 
Gene Synonyms/Alias
 b1651; JW1643 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
22RSIDFYTKVLGMKLLacetylation[1]
27YTKVLGMKLLRTSENacetylation[1]
127KIELIEEKDAGRGLGacetylation[1]
Reference
 [1] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli.
 Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C.
 Mol Cell. 2013 Jul 25;51(2):265-72. [PMID: 23830618
Functional Description
 Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione. 
Sequence Annotation
 METAL 5 5 Nickel.
 METAL 56 56 Nickel.
 METAL 74 74 Nickel.
 METAL 122 122 Nickel.  
Keyword
 3D-structure; Complete proteome; Direct protein sequencing; Lyase; Metal-binding; Nickel; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 135 AA 
Protein Sequence
MRLLHTMLRV GDLQRSIDFY TKVLGMKLLR TSENPEYKYS LAFVGYGPET EEAVIELTYN 60
WGVDKYELGT AYGHIALSVD NAAEACEKIR QNGGNVTREA GPVKGGTTVI AFVEDPDGYK 120
IELIEEKDAG RGLGN 135 
Gene Ontology
 GO:0004462; F:lactoylglutathione lyase activity; IDA:EcoCyc.
 GO:0016151; F:nickel cation binding; IDA:EcoCyc.
 GO:0019243; P:methylglyoxal catabolic process to D-lactate; IMP:EcoCyc. 
Interpro
 IPR004360; Glyas_Fos-R_dOase_dom.
 IPR004361; Glyoxalase_1.
 IPR018146; Glyoxalase_1_CS. 
Pfam
 PF00903; Glyoxalase 
SMART
  
PROSITE
 PS00934; GLYOXALASE_I_1
 PS00935; GLYOXALASE_I_2 
PRINTS