Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

A5I348 (MSRA_CLOBH) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 50. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
Name:msrA
Ordered Locus Names:CBO1923, CLC_1868
OrganismClostridium botulinum (strain Hall / ATCC 3502 / NCTC 13319 / Type A) [Reference proteome] [HAMAP]
Taxonomic identifier441771 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Protein attributes

Sequence length157 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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-Rule MF_01401

Catalytic activity

Peptide-L-methionine + thioredoxin disulfide + H2O = peptide-L-methionine (S)-S-oxide + thioredoxin. HAMAP-Rule MF_01401

L-methionine + thioredoxin disulfide + H2O = L-methionine (S)-S-oxide + thioredoxin. HAMAP-Rule MF_01401

Sequence similarities

Belongs to the MsrA Met sulfoxide reductase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 157157Peptide methionine sulfoxide reductase MsrA HAMAP-Rule MF_01401
PRO_1000068319

Sites

Active site101 By similarity

Sequences

Sequence LengthMass (Da)Tools
A5I348 [UniParc].

Last modified June 26, 2007. Version 1.
Checksum: E4458E31DD3FC694

FASTA15718,178
        10         20         30         40         50         60 
MKEIVLAGGC FWGVEEYMSR IEGIVETKVG YANGIKENPS YEEVCSGVTG HAEACYIKYD 

        70         80         90        100        110        120 
ESIISLEELL NKFWSIIDPT VLNKQGNDRG TQYRTGIFYL DEKDLNVIIK SKYQEQKNYR 

       130        140        150 
KPIVTEVEPL KCFYEAEEYH QKYLKKNPGG YCHIHLD 

« Hide

References

[1]"Genome sequence of a proteolytic (Group I) Clostridium botulinum strain Hall A and comparative analysis of the clostridial genomes."
Sebaihia M., Peck M.W., Minton N.P., Thomson N.R., Holden M.T.G., Mitchell W.J., Carter A.T., Bentley S.D., Mason D.R., Crossman L., Paul C.J., Ivens A., Wells-Bennik M.H.J., Davis I.J., Cerdeno-Tarraga A.M., Churcher C., Quail M.A., Chillingworth T. expand/collapse author list , Feltwell T., Fraser A., Goodhead I., Hance Z., Jagels K., Larke N., Maddison M., Moule S., Mungall K., Norbertczak H., Rabbinowitsch E., Sanders M., Simmonds M., White B., Whithead S., Parkhill J.
Genome Res. 17:1082-1092(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Hall / ATCC 3502 / NCTC 13319 / Type A.
[2]"Analysis of the neurotoxin complex genes in Clostridium botulinum A1-A4 and B1 strains: BoNT/A3, /Ba4 and /B1 clusters are located within plasmids."
Smith T.J., Hill K.K., Foley B.T., Detter J.C., Munk A.C., Bruce D.C., Doggett N.A., Smith L.A., Marks J.D., Xie G., Brettin T.S.
PLoS ONE 2:E1271-E1271(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Hall / ATCC 3502 / NCTC 13319 / Type A.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000727 Genomic DNA. Translation: ABS38947.1.
AM412317 Genomic DNA. Translation: CAL83465.1.
RefSeqYP_001254426.1. NC_009495.1.
YP_001387723.1. NC_009698.1.

3D structure databases

ProteinModelPortalA5I348.
SMRA5I348. Positions 1-156.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING413999.CBO1923.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABS38947; ABS38947; CLC_1868.
GeneID5186178.
5399299.
KEGGcbh:CLC_1868.
cbo:CBO1923.
PATRIC19365905. VBICloBot22612_1895.

Phylogenomic databases

eggNOGCOG0225.
HOGENOMHOG000263863.
KOK07304.
OMAGEWWDAE.
OrthoDBEOG6091JX.
ProtClustDBPRK14054.

Enzyme and pathway databases

BioCycCBOT413999:GJ72-1988-MONOMER.
CBOT441771:GIWX-1836-MONOMER.

Family and domain databases

Gene3D3.30.1060.10. 1 hit.
HAMAPMF_01401. MsrA.
InterProIPR028427. Met_Sox_Rdtase.
IPR002569. Met_Sox_Rdtase_MsrA.
[Graphical view]
PANTHERPTHR10173. PTHR10173. 1 hit.
PfamPF01625. PMSR. 1 hit.
[Graphical view]
SUPFAMSSF55068. SSF55068. 1 hit.
TIGRFAMsTIGR00401. msrA. 1 hit.
ProtoNetSearch...

Entry information

Entry nameMSRA_CLOBH
AccessionPrimary (citable) accession number: A5I348
Secondary accession number(s): A7G4K8
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: June 26, 2007
Last modified: February 19, 2014
This is version 50 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families