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
	OrderedLocusNames:	spyM18_1571

From

Streptococcus pyogenes serotype M18

[TaxID: 301451]

[HAMAP proteome]

Taxonomy

Bacteria; Firmicutes; Lactobacillales; Streptococcaceae; Streptococcus.

Protein existence

3: Inferred from homology;

References

[1]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=MGAS8232 / Serotype M18;
DOI=10.1073/pnas.062526099; PubMed=11917108 [NCBI, ExPASy, EBI, Israel, Japan]
Smoot J.C., Barbian K.D., Van Gompel J.J., Smoot L.M., Chaussee M.S., Sylva G.L., Sturdevant D.E., Ricklefs S.M., Porcella S.F., Parkins L.D., Beres S.B., Campbell D.S., Smith T.M., Zhang Q., Kapur V., Daly J.A., Veasy L.G., Musser J.M.;
"Genome sequence and comparative microarray analysis of serotype M18 group A Streptococcus strains associated with acute rheumatic fever outbreaks.";
Proc. Natl. Acad. Sci. U.S.A. 99:4668-4673(2002).

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

AE010071; AAL98136.1; ALT_INIT; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_607637.1; -.

3D structure databases

HSSP

P14930; 1L1D. [HSSP ENTRY / PDB]

ModBase

Q8P046.

Enzyme and pathway databases

BioCyc

SPYO186103:SPYM18_1571-MON; -.

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:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
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.

ProtoNet

Q8P046.

Genome annotation databases

GeneID

994664; -.

GenomeReviews

AE009949_GR; spyM18_1571.

KEGG

spm:spyM18_1571; -.

Phylogenomic databases

HOGENOM

Q8P046; -.

Genome annotation databases

CMR

Q8P046; spyM18_1571.

Other

UniRef

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

Keywords

Complete proteome; Multifunctional enzyme; Oxidoreductase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 309`	`309`	`Peptide methionine sulfoxide reductase msrA/msrB.`	`PRO_0000138524`
`REGION`	`1 153`	`153`	`Peptide methionine sulfoxide reductase A.`
`REGION`	`170 293`	`124`	`Peptide methionine sulfoxide reductase B.`
`ACT_SITE`	`8 8`		`By similarity.`
`ACT_SITE`	`282 282`		`By similarity.`

Sequence information

Length: 309 AA [This is the length of the unprocessed precursor]

Molecular weight: 35133 Da [This is the MW of the unprocessed precursor]

CRC64: 2E1F1374F4028ADF [This is a checksum on the sequence]

        10         20         30         40         50         60 
MIYLAGGCFW GVEEYFSQVD GVLDAVSGYA NGRGDTTNYQ LIHQTGHAET VEVAYDTNRI 

        70         80         90        100        110        120 
SLKELLLHFF RIIDPTSLNK QGNDRGSQYR TGIYYTDKAD LAIIDEVFKE KAKDYKKKIV 

       130        140        150        160        170        180 
VEKAPLKHFI KAEDYHQDYL KKNPNGYCHI DINQATYPVI DESKYPKPSA TEIKEKLSAD 

       190        200        210        220        230        240 
EYRVTQKNET EKAFSNRYWD SFDAGIYVDV VTGEPLFSSK DKFESGCGWP SFSRPISPDV 

       250        260        270        280        290        300 
VRYKEDKSFN MTRTEVRSRS GNSHLGHVFT DGPKDQGGLR YCINSLSITF IPKADMEAKG 


YGYLLSSVE

Q8P046 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