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:	VC_A0615

From

Vibrio cholerae

[TaxID: 666]

[HAMAP proteome]

Taxonomy

Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae; Vibrio.

Protein existence

3: Inferred from homology;

References

[1]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 39315 / El Tor Inaba N16961 / Serotype O1;
DOI=10.1038/35020000; PubMed=10952301 [NCBI, ExPASy, EBI, Israel, Japan]
Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L., Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R., Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D., Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A., Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L., Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
"DNA sequence of both chromosomes of the cholera pathogen Vibrio cholerae.";
Nature 406:477-483(2000).

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

AE003853; AAF96516.1; ALT_INIT; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

C82439; C82439.

RefSeq

NP_233004.1; -.

3D structure databases

HSSP

P14930; 1L1D. [HSSP ENTRY / PDB]

ModBase

Q9KLX6.

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.

BLOCKS

Q9KLX6.

Genome annotation databases

GeneID

2612594; -.

GenomeReviews

AE003853_GR; VC_A0615.

KEGG

vch:VCA0615; -.

TIGR

VC_A0615; -.

Phylogenomic databases

HOGENOM

Q9KLX6; -.

Other

ProtoNet

Q9KLX6.

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`	`1 378`	`378`	`Peptide methionine sulfoxide reductase msrA/msrB.`	`PRO_0000138526`
`REGION`	`40 197`	`158`	`Peptide methionine sulfoxide reductase A.`
`REGION`	`240 362`	`123`	`Peptide methionine sulfoxide reductase B.`
`ACT_SITE`	`48 48`		`By similarity.`
`ACT_SITE`	`351 351`		`By similarity.`

Sequence information

Length: 378 AA [This is the length of the unprocessed precursor]

Molecular weight: 43477 Da [This is the MW of the unprocessed precursor]

CRC64: BEE0F1A614562B10 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKRLFAWGAP LFALVALTLS LFSQADTKPS TIDSTSANYQ QATLAGGCFW CTESDMEKLP 

        70         80         90        100        110        120 
GVVDVISGYA GGDVDNPTYK QVSSGKTGHI EVIQVTFDPK IVTYEQVLDN FFRHIDPTDD 

       130        140        150        160        170        180 
QGSFVDRGEQ YRPAIFYHNA EQLEVAKRFM MEIDQLGIFK KPLKTELIEF KKFWPAEDYH 

       190        200        210        220        230        240 
QDYYKKNKVR YNYYRYASGR DQYLDEIFGA DRNTHPKTLR QWIDEKNGQA NVKAYVRPSD 

       250        260        270        280        290        300 
EQIRAKLTSL QYKVTQRDGT ERPFDNEYWD NKEEGIYVDI VSGEPLFSST DKYDSKTGWP 

       310        320        330        340        350        360 
SFTQPLNSSY IVTKDDNSLF YTRTEVRSRF ADSHLGHVFN DGPAPTGLRY CMNSAAMRFI 

       370 
PKQEMAAQGY GEYLALFK

Q9KLX6 in FASTA format

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View entry in raw text format (no links)
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	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