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:	HI1455

From

Haemophilus influenzae

[TaxID: 727]

[HAMAP proteome]

Taxonomy

Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; Pasteurellaceae; Haemophilus.

Protein existence

1: Evidence at protein level;

References

[1]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
PubMed=7542800 [NCBI, ExPASy, EBI, Israel, Japan]
Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
"Whole-genome random sequencing and assembly of Haemophilus influenzae Rd.";
Science 269:496-512(1995).

[2]

IDENTIFICATION BY MASS SPECTROMETRY.
DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.3.CO;2-W; PubMed=10675023 [NCBI, ExPASy, EBI, Israel, Japan]
Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., Gray C., Fountoulakis M.;
"Two-dimensional map of the proteome of Haemophilus influenzae.";
Electrophoresis 21:411-429(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

L42023; AAC23103.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

E64124; E64124.

RefSeq

NP_439606.1; -.

3D structure databases

HSSP

P14930; 1L1D. [HSSP ENTRY / PDB]

ModBase

P45213.

Enzyme and pathway databases

BioCyc

HINF71421:HI_1455-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

P45213.

Genome annotation databases

950358; -.

L42023_GR; HI1455.

hin:HI1455; -.

fig|71421.1.peg.1388; -.

TIGR

HI1455; -.

Phylogenomic databases

HOGENOM

P45213; -.

Other

ProtoNet

P45213.

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`	`1 353`	`353`	`Peptide methionine sulfoxide reductase msrA/msrB.`	`PRO_0000138513`
`REGION`	`43 196`	`154`	`Peptide methionine sulfoxide reductase A.`
`REGION`	`213 336`	`124`	`Peptide methionine sulfoxide reductase B.`
`ACT_SITE`	`51 51`		`By similarity.`
`ACT_SITE`	`325 325`		`By similarity.`

Sequence information

Length: 353 AA [This is the length of the unprocessed precursor]

Molecular weight: 39864 Da [This is the MW of the unprocessed precursor]

CRC64: ADBCDDB4D90A8B1E [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKLSKTFLFI TALCCATPTL AIQNSTSSSG EQKMAMENTQ NIREIYLAGG CFWGMEAYME 

        70         80         90        100        110        120 
RIHGVKDAIS GYANGNTEKT SYQMIGLTDH AETVKVTYDA NQISLDKLLK YYFKVIDPTS 

       130        140        150        160        170        180 
VNKQGNDRGR QYRTGIYYQD GADKAVIGQA LAQLQTKYKK PVQIEVQPLK NYIVAEEYHQ 

       190        200        210        220        230        240 
DYLKKNPNGY CHIDITKADE PVIDEKDYPK PSDAELKAKL TPLQYSVTQN KHTERSFSNE 

       250        260        270        280        290        300 
YWDNFQPGIY VDITTGEPVF SSNDKFESGC GWPSFTKPII KDVVHYETDN SFNMQRTEVL 

       310        320        330        340        350 
SRAGNAHLGH VFDDGPKDKG GLRYCINSAS IKFIPLAEME KAGYGYLIQS IKK

P45213 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