Reviewed,
UniProtKB/Swiss-Prot A9IZW8 (GLO2_BART1)
Last modified
February 9, 2010.
Version 18.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Hydroxyacylglutathione hydrolase EC=3.1.2.6 Alternative name(s): Glyoxalase II Short name=Glx II | ||||
| Gene names |
| ||||
| Organism | Bartonella tribocorum (strain CIP 105476 / IBS 506) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 382640 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Bartonellaceae › Bartonella |
Protein attributes
| Sequence length | 253 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid By similarity. HAMAP MF_01374 |
| Catalytic activity | S-(2-hydroxyacyl)glutathione + H2O = glutathione + a 2-hydroxy carboxylate. HAMAP MF_01374 |
| Cofactor | Binds 2 zinc ions per subunit By similarity. HAMAP MF_01374 |
| Pathway | Secondary metabolite metabolism; methylglyoxal degradation; (R)-lactate from methylglyoxal: step 2/2. HAMAP MF_01374 |
| Subunit structure | Monomer By similarity. HAMAP MF_01374 |
| Sequence similarities | Belongs to the metallo-beta-lactamase superfamily. Glyoxalase II family. |
Ontologies
| Keywords | |
|---|---|
| Ligand | Metal-binding Zinc |
| Molecular function | Hydrolase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Molecular function | hydroxyacylglutathione hydrolase activity Inferred from electronic annotation. Source: HAMAP zinc 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 – 253 | 253 | Hydroxyacylglutathione hydrolase HAMAP MF_01374 | PRO_1000087276 | |||||
Sites | |||||||||
| Metal binding | 54 | 1 | Zinc 1 By similarity | ||||||
| Metal binding | 56 | 1 | Zinc 1 By similarity | ||||||
| Metal binding | 58 | 1 | Zinc 2 By similarity | ||||||
| Metal binding | 59 | 1 | Zinc 2 By similarity | ||||||
| Metal binding | 112 | 1 | Zinc 1 By similarity | ||||||
| Metal binding | 131 | 1 | Zinc 1 By similarity | ||||||
| Metal binding | 131 | 1 | Zinc 2 By similarity | ||||||
| Metal binding | 169 | 1 | Zinc 2 By similarity | ||||||
Sequences
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References
| [1] | "Genomic analysis of Bartonella identifies type IV secretion systems as host adaptability factors." Saenz H.L., Engel P., Stoeckli M.C., Lanz C., Raddatz G., Vayssier-Taussat M., Birtles R., Schuster S.C., Dehio C. Nat. Genet. 39:1469-1476(2007) [PubMed: 18037886] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AM260525 Genomic DNA. Translation: CAK02633.1. |
| RefSeq | YP_001610628.1. |
3D structure databases | |
| SMR | A9IZW8. Positions 1-253. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 5829937. |
| GenomeReviews | Gene locus BT_2686 in contig AM260525_GR. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | HBG753931. |
| OMA | TSANARF. |
Family and domain databases | |
| HAMAP | MF_01374. Glyoxalase_2. [Tree] |
| InterPro | IPR001279. Blactmase-like. IPR017782. Hydroxyacylglutathione_Hdrlase. [Graphical view] |
| SMART | SM00849. Lactamase_B. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR03413. GSH_gloB. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | GLO2_BART1 | ||||||||
| Accession | Primary (citable) accession number: A9IZW8 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with


