Q9K1N8 · MSRAB_NEIMB

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

Features

Showing features for active site.

TypeIDPosition(s)Description
Active site207
Active site495Nucleophile

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular FunctionL-methionine-(S)-S-oxide reductase activity
Molecular Functionpeptide-methionine (R)-S-oxide reductase activity
Molecular Functionpeptide-methionine (S)-S-oxide reductase activity
Biological Processcellular response to oxidative stress
Biological Processprotein modification process
Biological Processprotein repair

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Peptide methionine sulfoxide reductase MsrA/MsrB

Including 3 domains:

  • Recommended name
    Thioredoxin
  • Recommended name
    Peptide methionine sulfoxide reductase MsrA
  • EC number
  • Short names
    Protein-methionine-S-oxide reductase
  • Alternative names
    • Peptide-methionine (S)-S-oxide reductase (Peptide Met(O) reductase)
  • Recommended name
    Peptide methionine sulfoxide reductase MsrB
  • EC number
  • Alternative names
    • Peptide-methionine (R)-S-oxide reductase

Gene names

    • Name
      msrAB
    • Synonyms
      pilB
    • Ordered locus names
      NMB0044

Organism names

Accessions

  • Primary accession
    Q9K1N8

Proteomes

Subcellular Location

PTM/Processing

Features

Showing features for chain, disulfide bond.

TypeIDPosition(s)Description
ChainPRO_00001385101-522Peptide methionine sulfoxide reductase MsrA/MsrB
Disulfide bond68↔71Redox-active
Disulfide bond440↔495

Keywords

Proteomic databases

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain, region.

TypeIDPosition(s)Description
Domain17-174Thioredoxin
Region199-354Peptide methionine sulfoxide reductase A
Domain383-506MsrB

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

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    522
  • Mass (Da)
    58,015
  • Last updated
    2000-10-01 v1
  • Checksum
    535A823EDB76BFD1
MKHRTFFSLCAKFGCLLALGACSPKIVDAGAATVPHTLSTLKTADNRPASVYLKKDKPTLIKFWASWCPLCLSELGQTEKWAQDAKFSSANLITVASPGFLHEKKDGDFQKWYAGLNYPKLPVVTDNGGTIAQSLNISVYPSWALIGKDSDVQRIVKGSINEAQALALIRDPNADLGSLKHSFYKPDTQKKDSKIMNTRTIYLAGGCFWGLEAYFQRIDGVVDAVSGYANGNTKNPSYEDVSYRHTGHAETVKVTYDADKLSLDDILQYFFRVVDPTSLNKQGNDTGTQYRSGVYYTDPAEKAVIAAALKREQQKYQLPLVVENEPLKNFYDAEEYHQDYLIKNPNGYCHIDIRKADEPLPGKTKTAPQGKGFDAATYKKPSDAELKRTLTEEQYQVTQNSATEYAFSHEYDHLFKPGIYVDVVSGEPLFSSADKYDSGCGWPSFTRPIDAKSVTEHDDFSYNMRRTEVRSHAADSHLGHVFPDGPRDKGGLRYCINGASLKFIPLEQMDAAGYGALKGKVK

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AE002098
EMBL· GenBank· DDBJ
AAF40515.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp