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
	OrderedLocusNames:	jhp_0210

From

Helicobacter pylori J99 (Campylobacter pylori J99)

[TaxID: 85963]

[HAMAP proteome]

Taxonomy

Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; Helicobacteraceae; Helicobacter.

Protein existence

3: Inferred from homology;

References

[1]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/16495; PubMed=9923682 [NCBI, ExPASy, EBI, Israel, Japan]
Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C., Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., Tummino P.J., Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., Gibson R., Merberg D., Mills S.D., Jiang Q., Taylor D.E., Vovis G.F., Trust T.J.;
"Genomic sequence comparison of two unrelated isolates of the human gastric pathogen Helicobacter pylori.";
Nature 397:176-180(1999).

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

AE001439; AAD05793.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

E71960; E71960.

RefSeq

NP_222931.1; -.

3D structure databases

HSSP

P14930; 1L1D. [HSSP ENTRY / PDB]

ModBase

Q9ZMK8.

Enzyme and pathway databases

BioCyc

HPYL85963:JHP0210-MON; -.

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

Q9ZMK8.

Genome annotation databases

GeneID

889429; -.

GenomeReviews

AE001439_GR; jhp_0210.

KEGG

hpj:jhp0210; -.

NMPDR

fig|85963.1.peg.209; -.

Phylogenomic databases

HOGENOM

Q9ZMK8; -.

Genome annotation databases

CMR

Q9ZMK8; jhp_0210.

Other

ProtoNet

Q9ZMK8.

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`	`1 359`	`359`	`Peptide methionine sulfoxide reductase msrA/msrB.`	`PRO_0000138514`
`REGION`	`36 189`	`154`	`Peptide methionine sulfoxide reductase A.`
`REGION`	`206 329`	`124`	`Peptide methionine sulfoxide reductase B.`
`ACT_SITE`	`44 44`		`By similarity.`
`ACT_SITE`	`318 318`		`By similarity.`

Sequence information

Length: 359 AA [This is the length of the unprocessed precursor]

Molecular weight: 41249 Da [This is the MW of the unprocessed precursor]

CRC64: 6786490ABA0F2386 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKILSYLKKF YLFLLIGAIM QANESMGAKL PKTDERVIYL AGGCFWGLEA YMERIYGVID 

        70         80         90        100        110        120 
ASSGYANGKT SSTNYEKLHE SDHAESVKVI YDPKKISLDK LLRYYFKVID PVSVNKQGND 

       130        140        150        160        170        180 
VGRQYRTGIY YVNSADKEVI DNALKALQKE VKGKIAIEVE PLKNYVRAEE YHQDYLKKHP 

       190        200        210        220        230        240 
GGYCHIDLKK ADEVIVDDDK YTKPSDEVLK KKLTKLQYEV TQNKHTEKPF ENEYYNKEEE 

       250        260        270        280        290        300 
GIYVDITTGE PLFSSADKYD SGCGWPSFSK PINKDVVKYE DDESLNRKRI EVLSRIGKAH 

       310        320        330        340        350 
LGHVFNDGPK ELGGLRYCIN SAALRFIPLK DMEKEGYGEF IPYIKKGELK KYIQDKKSH

Q9ZMK8 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
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