Q9LAM9 · MSRAB_STRGC
- ProteinPeptide methionine sulfoxide reductase MsrA/MsrB
- GenemsrAB
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids311 (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).
Involved in protection against oxidative stress when the bacterium enters the host bloodstream and required for maximal growth under aerobic and anaerobic conditions
Involved in protection against oxidative stress when the bacterium enters the host bloodstream and required for maximal growth under aerobic and anaerobic conditions
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 | 10 | |||||
Sequence: C | ||||||
Active site | 284 | Nucleophile | ||||
Sequence: C |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | L-methionine:thioredoxin-disulfide S-oxidoreductase activity | |
Molecular Function | peptide-methionine (R)-S-oxide reductase activity | |
Molecular Function | peptide-methionine (S)-S-oxide reductase activity | |
Biological Process | protein modification process | |
Biological Process | protein repair | |
Biological Process | response to oxidative stress |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePeptide methionine sulfoxide reductase MsrA/MsrB
Including 2 domains:
- 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 > Bacillota > Bacilli > Lactobacillales > Streptococcaceae > Streptococcus
Accessions
- Primary accessionQ9LAM9
- Secondary accessions
Proteomes
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000138516 | 1-311 | Peptide methionine sulfoxide reductase MsrA/MsrB | |||
Sequence: MAEIYLAGGCFWGLEEYFSRIEGVKKTTVGYANGQVESTNYQLIHQTDHAETVHLIYDEKRVSLREILLYYFRVIDPLSVNKQGNDVGRQYRTGVYYTNQADKAVIEQVFAEQEKQLGQKIAVELEPLRHYVLAEDYHQDYLKKNPGGYCHINVNDAYQPLVDPGQYEKPTDAELKEQLTQEQYQVTQLSATERPFHNAYNATFEEGIYVDVTTGEPLFFAGDKFESGCGWPSFSRPIAREVLRYYEDKSHGMERIEVRSRSGNAHLGHVFTDGPESAGGLRYCINSAALRFIPKEKMEAEGYAYLLQHMK |
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-155 | Peptide methionine sulfoxide reductase A | ||||
Sequence: MAEIYLAGGCFWGLEEYFSRIEGVKKTTVGYANGQVESTNYQLIHQTDHAETVHLIYDEKRVSLREILLYYFRVIDPLSVNKQGNDVGRQYRTGVYYTNQADKAVIEQVFAEQEKQLGQKIAVELEPLRHYVLAEDYHQDYLKKNPGGYCHINVN | ||||||
Domain | 172-295 | MsrB | ||||
Sequence: DAELKEQLTQEQYQVTQLSATERPFHNAYNATFEEGIYVDVTTGEPLFFAGDKFESGCGWPSFSRPIAREVLRYYEDKSHGMERIEVRSRSGNAHLGHVFTDGPESAGGLRYCINSAALRFIPK |
Sequence similarities
In the N-terminal section; belongs to the MsrA Met sulfoxide reductase family.
In the C-terminal section; belongs to the MsrB Met sulfoxide reductase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length311
- Mass (Da)35,672
- Last updated2000-10-01 v1
- Checksum7D4B7CAF81DBE692
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF128264 EMBL· GenBank· DDBJ | AAF36477.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP000725 EMBL· GenBank· DDBJ | ABV11083.1 EMBL· GenBank· DDBJ | Genomic DNA |