Reviewed,
UniProtKB/Swiss-Prot B0VR86 (MSRB_ACIBS)
Last modified
February 9, 2010.
Version 17.
History...
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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents
Names and origin
| Protein names | Recommended name: Peptide methionine sulfoxide reductase msrB EC=1.8.4.12 Alternative name(s): Peptide-methionine (R)-S-oxide reductase | ||||
| Gene names |
| ||||
| Organism | Acinetobacter baumannii (strain SDF) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 509170 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Moraxellaceae › Acinetobacter |
Protein attributes
| Sequence length | 139 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Catalytic activity | Peptide-L-methionine + thioredoxin disulfide + H2O = peptide-L-methionine (R)-S-oxide + thioredoxin. HAMAP MF_01400 |
| Cofactor | Binds 1 zinc ion per subunit. The zinc ion is important for the structural integrity of the protein By similarity. HAMAP MF_01400 |
| Sequence similarities | Belongs to the msrB Met sulfoxide reductase family. |
Ontologies
| Keywords | |
|---|---|
| Ligand | Metal-binding Zinc |
| Molecular function | Oxidoreductase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | peptide-methionine (R)-S-oxide reductase activity Inferred from electronic annotation. Source: EC peptide-methionine-(S)-S-oxide reductase activityInferred 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 – 139 | 139 | Peptide methionine sulfoxide reductase msrB HAMAP MF_01400 | PRO_1000145346 | |||||
Sites | |||||||||
| Active site | 119 | 1 | Nucleophile By similarity | ||||||
| Metal binding | 47 | 1 | Zinc By similarity | ||||||
| Metal binding | 50 | 1 | Zinc By similarity | ||||||
| Metal binding | 96 | 1 | Zinc By similarity | ||||||
| Metal binding | 99 | 1 | Zinc By similarity | ||||||
Sequences
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References
| [1] | "Comparative analysis of Acinetobacters: three genomes for three lifestyles." Vallenet D., Nordmann P., Barbe V., Poirel L., Mangenot S., Bataille E., Dossat C., Gas S., Kreimeyer A., Lenoble P., Oztas S., Poulain J., Segurens B., Robert C., Abergel C., Claverie J.-M., Raoult D., Medigue C., Weissenbach J., Cruveiller S. PLoS ONE 3:E1805-E1805(2008) [PubMed: 18350144] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CU468230 Genomic DNA. Translation: CAP01505.1. |
| RefSeq | YP_001707473.1. |
3D structure databases | |
| SMR | B0VR86. Positions 3-128. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 5986835. |
| GenomeReviews | Gene locus ABSDF2180 in contig CU468230_GR. |
| KEGG | abm:ABSDF2180. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | HBG715255. |
| OMA | VEVRCNH. |
Family and domain databases | |
| HAMAP | MF_01400. MsrB. [Tree] |
| InterPro | IPR002579. Methionine_sulphoxide_MsrB. IPR011057. Mss4-like. [Graphical view] |
| Gene3D | G3DSA:2.170.150.20. MsrB. 1 hit. |
| Pfam | PF01641. SelR. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR00357. MsrB. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | MSRB_ACIBS | ||||||||
| Accession | Primary (citable) accession number: B0VR86 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||

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