Q9K1N8 · MSRAB_NEIMB
- ProteinPeptide methionine sulfoxide reductase MsrA/MsrB
- GenemsrAB
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids522 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
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).
Catalytic activity
- [thioredoxin]-disulfide + H2O + L-methionyl-[protein] = [thioredoxin]-dithiol + L-methionyl-(S)-S-oxide-[protein]
RHEA-COMP:10700 CHEBI:50058 Position: n/n+3+ CHEBI:15377 + RHEA-COMP:12313 = RHEA-COMP:10698 CHEBI:29950 Position: nCHEBI:29950 Position: n+3+ RHEA-COMP:12315
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 207 | |||||
Sequence: C | ||||||
Active site | 495 | Nucleophile | ||||
Sequence: C |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | L-methionine-(S)-S-oxide reductase activity | |
Molecular Function | peptide-methionine (R)-S-oxide reductase activity | |
Molecular Function | peptide-methionine (S)-S-oxide reductase activity | |
Biological Process | cellular response to oxidative stress | |
Biological Process | protein modification process | |
Biological Process | protein repair |
Keywords
- Molecular function
- Biological process
Names & Taxonomy
Protein names
- Recommended namePeptide methionine sulfoxide reductase MsrA/MsrB
Including 3 domains:
- Recommended nameThioredoxin
- Recommended namePeptide methionine sulfoxide reductase MsrA
- EC number
- Short namesProtein-methionine-S-oxide reductase
- Alternative names
- Recommended namePeptide methionine sulfoxide reductase MsrB
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Betaproteobacteria > Neisseriales > Neisseriaceae > Neisseria
Accessions
- Primary accessionQ9K1N8
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000138510 | 1-522 | Peptide methionine sulfoxide reductase MsrA/MsrB | |||
Sequence: MKHRTFFSLCAKFGCLLALGACSPKIVDAGAATVPHTLSTLKTADNRPASVYLKKDKPTLIKFWASWCPLCLSELGQTEKWAQDAKFSSANLITVASPGFLHEKKDGDFQKWYAGLNYPKLPVVTDNGGTIAQSLNISVYPSWALIGKDSDVQRIVKGSINEAQALALIRDPNADLGSLKHSFYKPDTQKKDSKIMNTRTIYLAGGCFWGLEAYFQRIDGVVDAVSGYANGNTKNPSYEDVSYRHTGHAETVKVTYDADKLSLDDILQYFFRVVDPTSLNKQGNDTGTQYRSGVYYTDPAEKAVIAAALKREQQKYQLPLVVENEPLKNFYDAEEYHQDYLIKNPNGYCHIDIRKADEPLPGKTKTAPQGKGFDAATYKKPSDAELKRTLTEEQYQVTQNSATEYAFSHEYDHLFKPGIYVDVVSGEPLFSSADKYDSGCGWPSFTRPIDAKSVTEHDDFSYNMRRTEVRSHAADSHLGHVFPDGPRDKGGLRYCINGASLKFIPLEQMDAAGYGALKGKVK | ||||||
Disulfide bond | 68↔71 | Redox-active | ||||
Sequence: CPLC | ||||||
Disulfide bond | 440↔495 | |||||
Sequence: CGWPSFTRPIDAKSVTEHDDFSYNMRRTEVRSHAADSHLGHVFPDGPRDKGGLRYC |
Keywords
- PTM
Proteomic databases
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 17-174 | Thioredoxin | ||||
Sequence: LALGACSPKIVDAGAATVPHTLSTLKTADNRPASVYLKKDKPTLIKFWASWCPLCLSELGQTEKWAQDAKFSSANLITVASPGFLHEKKDGDFQKWYAGLNYPKLPVVTDNGGTIAQSLNISVYPSWALIGKDSDVQRIVKGSINEAQALALIRDPNA | ||||||
Region | 199-354 | Peptide methionine sulfoxide reductase A | ||||
Sequence: RTIYLAGGCFWGLEAYFQRIDGVVDAVSGYANGNTKNPSYEDVSYRHTGHAETVKVTYDADKLSLDDILQYFFRVVDPTSLNKQGNDTGTQYRSGVYYTDPAEKAVIAAALKREQQKYQLPLVVENEPLKNFYDAEEYHQDYLIKNPNGYCHIDIR | ||||||
Domain | 383-506 | MsrB | ||||
Sequence: DAELKRTLTEEQYQVTQNSATEYAFSHEYDHLFKPGIYVDVVSGEPLFSSADKYDSGCGWPSFTRPIDAKSVTEHDDFSYNMRRTEVRSHAADSHLGHVFPDGPRDKGGLRYCINGASLKFIPL |
Domain
Possesses 2 methionine sulfoxide reductase domains (A/MsrA and B/MsrB) and 1 N-terminal thioredoxin domain. The domain B exhibits a thioredoxin dependent methionine sulfoxide reductase activity; the Cys-495 is probably involved in the reduction of MetSO and in formation of the sulfenic acid derivative. The regeneration of Cys-495 is probably done via formation of a disulfide bond with Cys-440 followed by its reduction by thioredoxin.
Sequence similarities
In the N-terminal section; belongs to the thioredoxin family.
In the central section; belongs to the MsrA Met sulfoxide reductase family.
In the C-terminal section; belongs to the MsrB Met sulfoxide reductase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length522
- Mass (Da)58,015
- Last updated2000-10-01 v1
- Checksum535A823EDB76BFD1
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AE002098 EMBL· GenBank· DDBJ | AAF40515.1 EMBL· GenBank· DDBJ | Genomic DNA |