Tag | Content |
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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 |
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22 | RSIDFYTKVLGMKLL | acetylation | [1] | 27 | YTKVLGMKLLRTSEN | acetylation | [1] | 127 | KIELIEEKDAGRGLG | acetylation | [1] |
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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. |
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