Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Peptide methionine sulfoxide reductase MsrA

Gene

msrA

Organism
Mycobacterium vanbaalenii (strain DSM 7251 / PYR-1)
Status
Reviewed-Annotation score: -Protein inferred from homologyi

Functioni

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.UniRule annotation

Catalytic activityi

Peptide-L-methionine + thioredoxin disulfide + H2O = peptide-L-methionine (S)-S-oxide + thioredoxin.UniRule annotation
L-methionine + thioredoxin disulfide + H2O = L-methionine (S)-S-oxide + thioredoxin.UniRule annotation

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei13UniRule annotation1

GO - Molecular functioni

Keywordsi

Molecular functionOxidoreductase

Enzyme and pathway databases

BioCyciMVAN350058:G1G7S-5804-MONOMER

Names & Taxonomyi

Protein namesi
Recommended name:
Peptide methionine sulfoxide reductase MsrAUniRule annotation (EC:1.8.4.11UniRule annotation)
Short name:
Protein-methionine-S-oxide reductaseUniRule annotation
Alternative name(s):
Peptide-methionine (S)-S-oxide reductaseUniRule annotation
Short name:
Peptide Met(O) reductaseUniRule annotation
Gene namesi
Name:msrAUniRule annotation
Ordered Locus Names:Mvan_5709
OrganismiMycobacterium vanbaalenii (strain DSM 7251 / PYR-1)
Taxonomic identifieri350058 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacteriumMycobacterium fortuitum complex
Proteomesi
  • UP000009159 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10001454221 – 169Peptide methionine sulfoxide reductase MsrAAdd BLAST169

Interactioni

Protein-protein interaction databases

STRINGi350058.Mvan_5709

Structurei

3D structure databases

ProteinModelPortaliA1TH24
SMRiA1TH24
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the MsrA Met sulfoxide reductase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0225 LUCA
HOGENOMiHOG000263863
KOiK07304
OMAiGYCAFVV
OrthoDBiPOG091H059H

Family and domain databases

Gene3Di3.30.1060.10, 1 hit
HAMAPiMF_01401 MsrA, 1 hit
InterProiView protein in InterPro
IPR002569 Met_Sox_Rdtase_MsrA
IPR036509 Met_Sox_Rdtase_MsrA_sf
PfamiView protein in Pfam
PF01625 PMSR, 1 hit
SUPFAMiSSF55068 SSF55068, 1 hit
TIGRFAMsiTIGR00401 msrA, 1 hit

Sequencei

Sequence statusi: Complete.

A1TH24-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSDHKRAVLA GGCFWGMQDL IRKQPGVVST RVGYTGGQND HPTYRNHPGH
60 70 80 90 100
AEAIEIVYDP AQTDYRALLE FFFQIHDPTT KNRQGNDVGT SYRSEIFYVD
110 120 130 140 150
DEQRRIALDT IADVDASGLW PGKVVTDVSP APEFWEAEPE HQDYLERYPS
160
GYTCHFPRPG WKLPKRAEV
Length:169
Mass (Da):19,268
Last modified:February 6, 2007 - v1
Checksum:i1A361D810042C205
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000511 Genomic DNA Translation: ABM16474.1
RefSeqiWP_011782826.1, NC_008726.1

Genome annotation databases

EnsemblBacteriaiABM16474; ABM16474; Mvan_5709
KEGGimva:Mvan_5709

Similar proteinsi

Entry informationi

Entry nameiMSRA_MYCVP
AccessioniPrimary (citable) accession number: A1TH24
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: February 6, 2007
Last modified: May 23, 2018
This is version 78 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Cookie policy

We would like to use anonymized google analytics cookies to gather statistics on how uniprot.org is used in aggregate. Learn more

UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health