P0AC85 (GLO2_ECO57) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 41.
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: Hydroxyacylglutathione hydrolase EC=3.1.2.6 Alternative name(s): Glyoxalase II Short name=Glx II | ||||
| Gene names |
| ||||
| Organism | Escherichia coli O157:H7 [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 83334 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia |
Protein attributes
| Sequence length | 251 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: EC zinc ion bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 251 | 251 | Hydroxyacylglutathione hydrolase HAMAP MF_01374 | PRO_0000192352 | |||||
Sites | |||||||||
| Metal binding | 53 | 1 | Zinc 1 By similarity | ||||||
| Metal binding | 55 | 1 | Zinc 1 By similarity | ||||||
| Metal binding | 57 | 1 | Zinc 2 By similarity | ||||||
| Metal binding | 58 | 1 | Zinc 2 By similarity | ||||||
| Metal binding | 110 | 1 | Zinc 1 By similarity | ||||||
| Metal binding | 127 | 1 | Zinc 1 By similarity | ||||||
| Metal binding | 127 | 1 | Zinc 2 By similarity | ||||||
| Metal binding | 165 | 1 | Zinc 2 By similarity | ||||||
Sequences
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References
| [1] | "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7." Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W. Blattner F.R.Nature 409:529-533(2001) [PubMed: 11206551] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC. |
| [2] | "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12." Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T. Shinagawa H.DNA Res. 8:11-22(2001) [PubMed: 11258796] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE005174 Genomic DNA. Translation: AAG54508.1. BA000007 Genomic DNA. Translation: BAB33631.1. |
| PIR | H85505. H90654. |
| RefSeq | NP_285900.1. NC_002655.2. NP_308235.1. NC_002695.1. |
3D structure databases | |
| ProteinModelPortal | P0AC85. |
| SMR | P0AC85. Positions 1-251. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBESCT00000028944; EBESCP00000027837; EBESCG00000027995. EBESCT00000056604; EBESCP00000054432; EBESCG00000055652. |
| GeneID | 914044. 956977. |
| GenomeReviews | Gene locus Z0236 in contig AE005174_GR. Gene locus ECs0208 in contig BA000007_GR. |
| KEGG | ece:Z0236. ecs:ECs0208. |
| PATRIC | 18349376. VBIEscCol44059_0212. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| GeneTree | EBGT00050000008983. |
| HOGENOM | HBG753931. |
| OMA | ITHHHRD. |
| ProtClustDB | PRK10241. |
Enzyme and pathway databases | |
| BioCyc | ECOL83334:ECS0208-MONOMER. |
Family and domain databases | |
| HAMAP | MF_01374. Glyoxalase_2. [Tree] |
| InterPro | IPR001279. Beta-lactamas-like. IPR017782. Hydroxyacylglutathione_Hdrlase. [Graphical view] |
| KO | K01069. |
| PANTHER | PTHR11935:SF7. PTHR11935:SF7. 1 hit. |
| Pfam | PF00753. Lactamase_B. 1 hit. [Graphical view] |
| SMART | SM00849. Lactamase_B. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR03413. GSH_gloB. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | GLO2_ECO57 | ||||||||
| Accession | Primary (citable) accession number: P0AC85 Secondary accession number(s): Q47677 | ||||||||
| 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 |

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