A4F5Y6 (A4F5Y6_SACEN) Unreviewed, UniProtKB/TrEMBL
Last modified
December 14, 2011.
Version 39.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize orderNames and origin
| Protein names | Recommended name: Peptide methionine sulfoxide reductase MsrA HAMAP MF_01401 Short name=Protein-methionine-S-oxide reductase HAMAP MF_01401 EC=1.8.4.11 HAMAP MF_01401 Alternative name(s): Peptide-methionine (S)-S-oxide reductase HAMAP MF_01401 | ||||
| Gene names |
| ||||
| Organism | Saccharopolyspora erythraea (strain NRRL 23338) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 405948 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Pseudonocardineae › Pseudonocardiaceae › Saccharopolyspora |
Protein attributes
| Sequence length | 227 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine By similarity. HAMAP MF_01401 |
| Catalytic activity | L-methionine + thioredoxin disulfide + H2O = L-methionine (S)-S-oxide + thioredoxin. HAMAP MF_01401 SAAS SAAS002569 Peptide-L-methionine + thioredoxin disulfide + H2O = peptide-L-methionine (S)-S-oxide + thioredoxin. HAMAP MF_01401 SAAS SAAS002569 |
| Sequence similarities | Belongs to the MsrA Met sulfoxide reductase family. HAMAP MF_01401 |
Ontologies
| Keywords | |
|---|---|
| Molecular function | Oxidoreductase HAMAP MF_01401 SAAS SAAS002569 EMBL CAL99460.1 |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | protein modification process Inferred from electronic annotation. Source: HAMAP |
| Molecular function | peptide-methionine-(S)-S-oxide reductase activity Inferred from electronic annotation. Source: HAMAP |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Sites | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Active site | 60 | 1 | By similarity HAMAP MF_01401 | ||||||
Sequences
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References
| [1] | "Complete genome sequence of the erythromycin-producing bacterium Saccharopolyspora erythraea NRRL23338." Oliynyk M., Samborskyy M., Lester J.B., Mironenko T., Scott N., Dickens S., Haydock S.F., Leadlay P.F. Nat. Biotechnol. 25:447-453(2007) [PubMed: 17369815] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AM420293 Genomic DNA. Translation: CAL99460.1. |
| RefSeq | YP_001102386.1. NC_009142.1. |
3D structure databases | |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | A4F5Y6. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 4939971. |
| GenomeReviews | Gene locus SACE_0107 in contig AM420293_GR. |
| KEGG | sen:SACE_0107. |
| PATRIC | 23407554. VBISacEry28377_0106. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0225. |
| HOGENOM | HBG748152. |
| OMA | ERKIMTE. |
| PhylomeDB | A4F5Y6. |
Enzyme and pathway databases | |
| BioCyc | SERY405948:SACE_0107-MONOMER. |
Family and domain databases | |
| HAMAP | MF_01401. MsrA. [Tree] |
| InterPro | IPR002569. Peptide_Met_Sox_Rdtase_MsrA. [Graphical view] |
| Gene3D | G3DSA:3.30.1060.10. MsrA. 1 hit. |
| KO | K07304. |
| Pfam | PF01625. PMSR. 1 hit. [Graphical view] |
| SUPFAM | SSF55068. MsrA. 1 hit. |
| TIGRFAMs | TIGR00401. MsrA. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | A4F5Y6_SACEN | ||||||||
| Accession | Primary (citable) accession number: A4F5Y6 | ||||||||
| Entry history |
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| Entry status | Unreviewed (UniProtKB/TrEMBL) | ||||||||

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