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

From

Actinobacillus actinomycetemcomitans (Haemophilus actinomycetemcomitans)

[TaxID: 714]

Taxonomy

Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; Pasteurellaceae; Aggregatibacter.

Protein existence

3: Inferred from homology;

References

[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Mintz K.P., Wu H., Shao M., Fives-Taylor P.M.; "Actinobacillus actinomycetemcomitans msrA."; Submitted (JAN-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

AY026361; AAK07680.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

P14930; 1L1D. [HSSP ENTRY / PDB]

ModBase

Q9AL99.

Ontologies

GO:0033743;	Molecular function: peptide-methionine (R)-S-oxide reductase activity (inferred from electronic annotation from EC).
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`	`1 356`	`356`	`Peptide methionine sulfoxide reductase msrA/msrB.`	`PRO_0000138511`
`REGION`	`46 199`	`154`	`Peptide methionine sulfoxide reductase A.`
`REGION`	`216 339`	`124`	`Peptide methionine sulfoxide reductase B.`
`ACT_SITE`	`54 54`		`By similarity.`
`ACT_SITE`	`328 328`		`By similarity.`

Sequence information

Length: 356 AA [This is the length of the unprocessed precursor]

Molecular weight: 40476 Da [This is the MW of the unprocessed precursor]

CRC64: 3882FA423CEAE7C7 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKKSKLVVAL AAILSCAAIP TTVMAESNVQ QTMEKSNMSE AKKDLHEIYL AGGCFWGIEA 

        70         80         90        100        110        120 
YMERIYGVED AISGYANGKS DKTNYQKIGI TDHAETVKVT YDRNKVSLDK LLKYYFQVID 

       130        140        150        160        170        180 
PTSVNKQGND RGRQYRTGIY YQDTADKSII EKEITALQGK YKNKIQIEVE PLHNYIVAEE 

       190        200        210        220        230        240 
YHQDYLKKNP NGYCHIDLEQ ANYVIIDEKD YPKPSDAELK AKLTPLQYSV TQNKNTEHSF 

       250        260        270        280        290        300 
SNEYWDNFKP GIYVDVTTGE PLFSSKDKFE SGCGWPSFTK PITKEVVTYQ DDHSFNMLRT 

       310        320        330        340        350 
EVISRSGKAH LGHVFDDGPK DKGGLRYCIN SAAVKFIPLE DMVKENYGYL TNAVKE

Q9AL99 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