Q6P7Q4 (LGUL_RAT) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 80.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Lactoylglutathione lyase EC=4.4.1.5 Alternative name(s): Aldoketomutase Glyoxalase I Short name=Glx I Ketone-aldehyde mutase Methylglyoxalase S-D-lactoylglutathione methylglyoxal lyase | ||
| Gene names |
| ||
| Organism | Rattus norvegicus (Rat) [Reference proteome] | ||
| Taxonomic identifier | 10116 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus![]() |
Protein attributes
| Sequence length | 184 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione. Involved in the regulation of TNF-induced transcriptional activity of NF-kappa-B By similarity. |
| Catalytic activity | (R)-S-lactoylglutathione = glutathione + methylglyoxal. |
| Cofactor | Binds 1 zinc ion per subunit By similarity. |
| Pathway | Secondary metabolite metabolism; methylglyoxal degradation; (R)-lactate from methylglyoxal: step 1/2. |
| Subunit structure | Homodimer By similarity. |
| Post-translational modification | Glutathionylation at Cys-139 inhibits enzyme activity By similarity. Phosphorylated at Thr-107 in the presence of CaMK2. However, this is a consensus site for phosphorylation by CK2 so phosphorylation may be mediated by CK2 rather than CaMK2. Phosphorylation is induced by TNF and suppresses the TNF-induced transcriptional activity of NF-kappa-B By similarity. Exists in a nitric oxide (NO)-modified form. The exact nature of the modification is unknown, but it suppresses the TNF-induced transcriptional activity of NF-kappa-B By similarity. |
| Sequence similarities | Belongs to the glyoxalase I family. |
Ontologies
| Keywords | |
|---|---|
| Ligand | Metal-binding Zinc |
| Molecular function | Lyase |
| PTM | Acetylation Disulfide bond Glutathionylation Phosphoprotein |
| Technical term | Complete proteome Direct protein sequencing Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | carbohydrate metabolic process Inferred from direct assay PubMed 8719777PubMed 8903102. Source: RGD glutathione metabolic processInferred from direct assay PubMed 8719777PubMed 8903102. Source: RGD methylglyoxal metabolic processInferred from direct assay PubMed 10712823PubMed 8719777PubMed 8903102. Source: RGD negative regulation of apoptotic processInferred from sequence or structural similarity. Source: UniProtKB regulation of transcription from RNA polymerase II promoterInferred from electronic annotation. Source: Compara |
| Molecular_function | lactoylglutathione lyase activity Inferred from sequence or structural similarity. Source: UniProtKB metal ion bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed By similarity | ||||||||
| Chain | 2 – 184 | 183 | Lactoylglutathione lyase | PRO_0000168079 | |||||||
Sites | |||||||||||
| Metal binding | 34 | 1 | Zinc By similarity | ||||||||
| Metal binding | 100 | 1 | Zinc By similarity | ||||||||
| Metal binding | 127 | 1 | Zinc By similarity | ||||||||
| Metal binding | 173 | 1 | Zinc By similarity | ||||||||
Amino acid modifications | |||||||||||
| Modified residue | 2 | 1 | N-acetylalanine By similarity | ||||||||
| Modified residue | 107 | 1 | Phosphothreonine By similarity | ||||||||
| Modified residue | 139 | 1 | S-glutathionyl cysteine By similarity | ||||||||
| Modified residue | 148 | 1 | N6-acetyllysine By similarity | ||||||||
| Disulfide bond | 19 ↔ 20 | By similarity | |||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Pituitary. |
| [2] | Lubec G., Afjehi-Sadat L., Chen W.-Q. Submitted (APR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 29-38; 44-83; 89-95 AND 124-148, MASS SPECTROMETRY. Strain: Sprague-Dawley. Tissue: Hippocampus and Spinal cord. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | BC061570 mRNA. Translation: AAH61570.1. |
| IPI | IPI00188304. |
| RefSeq | NP_997477.1. NM_207594.2. |
| UniGene | Rn.108014. |
3D structure databases | |
| ProteinModelPortal | Q6P7Q4. |
| SMR | Q6P7Q4. Positions 4-183. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 10116.ENSRNOP00000000650. |
Proteomic databases | |
| PaxDb | Q6P7Q4. |
| PRIDE | Q6P7Q4. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENSRNOT00000000650; ENSRNOP00000000650; ENSRNOG00000000541. |
| GeneID | 294320. |
| KEGG | rno:294320. |
| UCSC | RGD:2702. rat. |
Organism-specific databases | |
| CTD | 2739. |
| RGD | 2702. Glo1. |
Phylogenomic databases | |
| eggNOG | COG0346. |
| GeneTree | ENSGT00390000009312. |
| HOGENOM | HOG000232011. |
| HOVERGEN | HBG025852. |
| InParanoid | Q6P7Q4. |
| KO | K01759. |
| OMA | WALSRKA. |
| OrthoDB | EOG4TQMB3. |
Enzyme and pathway databases | |
| SABIO-RK | Q6P7Q4. |
| UniPathway | UPA00619; UER00675. |
Gene expression databases | |
| Genevestigator | Q6P7Q4. |
| GermOnline | ENSRNOG00000000541. Rattus norvegicus. |
Family and domain databases | |
| InterPro | IPR004360. Glyas_Fos-R_dOase_dom. IPR004361. Glyoxalase_1. IPR018146. Glyoxalase_1_CS. [Graphical view] |
| Pfam | PF00903. Glyoxalase. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR00068. glyox_I. 1 hit. |
| PROSITE | PS00934. GLYOXALASE_I_1. 1 hit. PS00935. GLYOXALASE_I_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other | |
| ChEMBL | CHEMBL2306. |
| NextBio | 637974. |
Entry information
| Entry name | LGUL_RAT | ||||||||
| Accession | Primary (citable) accession number: Q6P7Q4 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with
