Peptide methionine sulfoxide reductase msrA
     (Protein-methionine-S-oxide reductase)
     (EC 1.8.4.11)
     (Peptide-methionine (S)-S-oxide reductase)
     (Peptide Met(O) reductase)
Peptide methionine sulfoxide reductase msrB
     (EC 1.8.4.12)
     (Peptide-methionine (R)-S-oxide reductase)

Gene name

	Name:	msrAB
	Synonyms:	msrA

From

Campylobacter fetus

[TaxID: 196]

Taxonomy

Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; Campylobacteraceae; Campylobacter.

Protein existence

3: Inferred from homology;

References

[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=ATCC 27374 / CIP 5396 / DSM 5361 / LMG 6442 / NCTC 10842; Thies F.L., Trotha R., Koenig W.; "Identification of genes encoding exported proteins in Campylobacter jejuni and C. fetus."; Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.

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).
CATALYTIC ACTIVITY: Peptide-L-methionine + thioredoxin disulfide + H₂O = peptide-L-methionine (S)-S-oxide + thioredoxin.
CATALYTIC ACTIVITY: L-methionine + thioredoxin disulfide + H₂O = L-methionine (S)-S-oxide + thioredoxin.
CATALYTIC ACTIVITY: Peptide-L-methionine + thioredoxin disulfide + H₂O = peptide-L-methionine (R)-S-oxide + thioredoxin.
SIMILARITY: In the N-terminal section; belongs to the msrA Met sulfoxide reductase family.
SIMILARITY: In the C-terminal section; belongs to the msrB Met sulfoxide reductase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AJ312325; CAC42492.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

P14930; 1L1D. [HSSP ENTRY / PDB]

ModBase

Q93KF3.

Ontologies

GO:0008113;	Molecular function: peptide-methionine-(S)-S-oxide reductase activity (inferred from electronic annotation from HAMAP).
GO:0006464;	Biological process: protein modification process (inferred from electronic annotation from HAMAP).
QuickGo view.

Family and domain databases

HAMAP

MF_01400; fused; 1.
MF_01401; fused; 1.
PBIL [Tree]

InterPro

IPR002569; MsrA.
IPR002579; MsrB.
Graphical view of domain structure.

Gene3D

G3DSA:3.30.1060.10; MsrA; 1.
G3DSA:2.170.150.20; MsrB; 1.

Pfam

PF01625; PMSR; 1.
PF01641; SelR; 1.
Pfam graphical view of domain structure.

ProDom

PD004057; DUF25; 1.
PD003489; PMSR; 1.
[Domain structure / List of seq. sharing at least 1 domain]

TIGRFAMs

TIGR00401; msrA; 1.
TIGR00357; MsrB; 1.

Other

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Multifunctional enzyme; Oxidoreductase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 337`	`337`	`Peptide methionine sulfoxide reductase msrA/msrB.`	`PRO_0000138512`
`REGION`	`28 181`	`154`	`Peptide methionine sulfoxide reductase A.`
`REGION`	`198 321`	`124`	`Peptide methionine sulfoxide reductase B.`
`ACT_SITE`	`36 36`		`By similarity.`
`ACT_SITE`	`310 310`		`By similarity.`

Sequence information

Length: 337 AA [This is the length of the unprocessed precursor]

Molecular weight: 38342 Da [This is the MW of the unprocessed precursor]

CRC64: 4406FA3CC4BC236F [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKKILFVVAT IFMALFLNAK ENDMRNLKDI YLAGGCFWGT QAYFDKIRGV IKTDVGYANG 

        70         80         90        100        110        120 
KSDKTDYHSL HYSGHAETVH ITFDENIVSL AEILAHYFRI IDPFSVNKQG NDVGSQYRTG 

       130        140        150        160        170        180 
IYYNDSSLKN SISEFIKHEQ TKYDKKIAVE VEPLKNYVLA EDYHQKYLDK NPGGYCHVDL 

       190        200        210        220        230        240 
SLADKPLYNE SKFKAPSKDE LKAKLSDLQY SVTQEKATER PYSSEYDKFD KKGIYVDIVS 

       250        260        270        280        290        300 
KKPLFSSSDK FDAGCGWPSF TKPITTDALG YNRDLSHGME RVEVTSNLAN SHLGHVFTDG 

       310        320        330 
PKDKGGLRYC INGASLKFIP LEDMEKEGYK DYIIYVK

Q93KF3 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools