P0A5L0 (MSRA_MYCTU) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 47.
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: Peptide methionine sulfoxide reductase MsrA Short name=Protein-methionine-S-oxide reductase EC=1.8.4.11 Alternative name(s): Peptide-methionine (S)-S-oxide reductase Short name=Peptide Met(O) reductase | ||||||
| Gene names |
| ||||||
| Organism | Mycobacterium tuberculosis | ||||||
| Taxonomic identifier | 1773 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex |
Protein attributes
| Sequence length | 182 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
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 | Peptide-L-methionine + thioredoxin disulfide + H2O = peptide-L-methionine (S)-S-oxide + thioredoxin. HAMAP MF_01401 L-methionine + thioredoxin disulfide + H2O = L-methionine (S)-S-oxide + thioredoxin. HAMAP MF_01401 |
| Sequence similarities | Belongs to the MsrA Met sulfoxide reductase family. |
Ontologies
| Keywords | |
|---|---|
| Molecular function | Oxidoreductase |
| Technical term | 3D-structure Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological process | protein metabolic process Inferred from electronic annotation. Source: InterPro response to nitrosative stressInferred from mutant phenotype. Source: MTBBASE response to oxidative stressInferred from mutant phenotype. Source: MTBBASE |
| Molecular function | L-methionine-(S)-S-oxide reductase activity Inferred from direct assay. Source: MTBBASE peptide-methionine-(S)-S-oxide reductase activityInferred from direct assay. Source: MTBBASE |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||||||||||||||||||||||||||||
Molecule processing | |||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 182 | 182 | Peptide methionine sulfoxide reductase MsrA HAMAP MF_01401 | PRO_0000138560 | |||||||||||||||||||||||||||||||||
Sites | |||||||||||||||||||||||||||||||||||||
| Active site | 13 | 1 | By similarity | ||||||||||||||||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||||||||||||||||
| Beta strand | 5 – 12 | 8 | |||||||||||||||||||||||||||||||||||
| Helix | 14 – 21 | 8 | |||||||||||||||||||||||||||||||||||
| Beta strand | 27 – 38 | 12 | |||||||||||||||||||||||||||||||||||
| Beta strand | 51 – 58 | 8 | |||||||||||||||||||||||||||||||||||
| Turn | 60 – 62 | 3 | |||||||||||||||||||||||||||||||||||
| Helix | 65 – 75 | 11 | |||||||||||||||||||||||||||||||||||
| Beta strand | 87 – 89 | 3 | |||||||||||||||||||||||||||||||||||
| Helix | 90 – 92 | 3 | |||||||||||||||||||||||||||||||||||
| Beta strand | 94 – 100 | 7 | |||||||||||||||||||||||||||||||||||
| Helix | 101 – 117 | 17 | |||||||||||||||||||||||||||||||||||
| Beta strand | 120 – 122 | 3 | |||||||||||||||||||||||||||||||||||
| Beta strand | 127 – 130 | 4 | |||||||||||||||||||||||||||||||||||
| Beta strand | 134 – 136 | 3 | |||||||||||||||||||||||||||||||||||
| Helix | 139 – 141 | 3 | |||||||||||||||||||||||||||||||||||
| Helix | 144 – 147 | 4 | |||||||||||||||||||||||||||||||||||
Sequences
| ||||||||||||||||||
References
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | BX842572 Genomic DNA. Translation: CAB07043.1. AE000516 Genomic DNA. Translation: AAK44369.1. | ||||||||||||
| PIR | D70616. | ||||||||||||
| RefSeq | NP_214651.1. NC_000962.2. NP_334555.1. NC_002755.2. | ||||||||||||
3D structure databases | |||||||||||||
| PDBe RCSB PDB PDBj |
| ||||||||||||
| ProteinModelPortal | P0A5L0. | ||||||||||||
| SMR | P0A5L0. Positions 1-166. | ||||||||||||
| ModBase | Search... | ||||||||||||
Protocols and materials databases | |||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||
Genome annotation databases | |||||||||||||
| EnsemblBacteria | EBMYCT00000000702; EBMYCP00000000702; EBMYCG00000000702. EBMYCT00000069579; EBMYCP00000067638; EBMYCG00000069574. | ||||||||||||
| GeneID | 886865. 923012. | ||||||||||||
| GenomeReviews | Gene locus MT0145 in contig AE000516_GR. Gene locus Rv0137c in contig AL123456_GR. | ||||||||||||
| KEGG | mtc:MT0145. mtu:Rv0137c. | ||||||||||||
| PATRIC | 18122047. VBIMycTub22151_0158. | ||||||||||||
| TIGR | MT0145. | ||||||||||||
Organism-specific databases | |||||||||||||
| TubercuList | Rv0137c. | ||||||||||||
Phylogenomic databases | |||||||||||||
| GeneTree | EBGT00050000017224. | ||||||||||||
| HOGENOM | HBG748152. | ||||||||||||
| OMA | YRQILEF. | ||||||||||||
| PhylomeDB | P0A5L0. | ||||||||||||
| ProtClustDB | PRK14054. | ||||||||||||
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 | MSRA_MYCTU | ||||||||
| Accession | Primary (citable) accession number: P0A5L0 Secondary accession number(s): P96814 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with