Q9KT93 (LGUL_VIBCH) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 29, 2013.
Version 78.
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: Probable 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 | Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961) [Reference proteome] [HAMAP] | ||||
| Taxonomic identifier | 243277 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Vibrionales › Vibrionaceae › Vibrio › ![]() |
Protein attributes
| Sequence length | 138 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione By similarity. |
| Catalytic activity | (R)-S-lactoylglutathione = glutathione + methylglyoxal. |
| Cofactor | Binds 1 nickel ion per subunit By similarity. |
| Pathway | Secondary metabolite metabolism; methylglyoxal degradation; (R)-lactate from methylglyoxal: step 1/2. |
| Sequence similarities | Belongs to the glyoxalase I family. |
| Sequence caution | The sequence AAF94171.1 differs from that shown. Reason: Erroneous initiation. |
Ontologies
| Keywords | |
|---|---|
| Ligand | Metal-binding Nickel |
| Molecular function | Lyase |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | glutathione metabolic process Inferred from sequence or structural similarity Ref.1. Source: TIGR |
| Molecular_function | lactoylglutathione lyase activity Inferred from sequence or structural similarity Ref.1. Source: TIGR 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 | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 138 | 138 | Probable lactoylglutathione lyase | PRO_0000168097 | |||||
Sites | |||||||||
| Metal binding | 8 | 1 | Nickel By similarity | ||||||
| Metal binding | 59 | 1 | Nickel By similarity | ||||||
| Metal binding | 77 | 1 | Nickel By similarity | ||||||
| Metal binding | 125 | 1 | Nickel By similarity | ||||||
Sequences
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References
| [1] | "DNA sequence of both chromosomes of the cholera pathogen Vibrio cholerae." Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L., Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R., Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D., Vamathevan J.J., Bass S. Fraser C.M.Nature 406:477-483(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 39315 / El Tor Inaba N16961. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE003852 Genomic DNA. Translation: AAF94171.1. Different initiation. |
| PIR | H82251. |
| RefSeq | NP_230656.2. NC_002505.1. |
3D structure databases | |
| ProteinModelPortal | Q9KT93. |
| SMR | Q9KT93. Positions 5-128. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 243277.VC1010. |
Protocols and materials databases | |
| DNASU | 2614263. |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | AAF94171; AAF94171; VC_1010. |
| GeneID | 2614263. |
| KEGG | vch:VC1010. |
| PATRIC | 20081120. VBIVibCho83274_0964. |
Phylogenomic databases | |
| eggNOG | COG0346. |
| KO | K01759. |
| OMA | VREPGPM. |
| ProtClustDB | CLSK2484291. |
Enzyme and pathway databases | |
| UniPathway | UPA00619; UER00675. |
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... |
Entry information
| Entry name | LGUL_VIBCH | ||||||||
| Accession | Primary (citable) accession number: Q9KT93 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with
