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Q9K1N8 (MSRAB_NEIMB) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Peptide methionine sulfoxide reductase MsrA/MsrB

Including the following 3 domains:

  1. Thioredoxin
  2. Peptide methionine sulfoxide reductase MsrA
    Short name=Protein-methionine-S-oxide reductase
    EC=1.8.4.11
    Alternative name(s):
    Peptide-methionine (S)-S-oxide reductase
    Short name=Peptide Met(O) reductase
  3. Peptide methionine sulfoxide reductase MsrB
    EC=1.8.4.12
    Alternative name(s):
    Peptide-methionine (R)-S-oxide reductase
Gene names
Name:msrAB
Synonyms:pilB
Ordered Locus Names:NMB0044
OrganismNeisseria meningitidis serogroup B
Taxonomic identifier491 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Neisseriales › Neisseriaceae › Neisseria

Protein attributes

Sequence length522 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (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. HAMAP MF_01400

Catalytic activity

Peptide-L-methionine + thioredoxin disulfide + H2O = peptide-L-methionine (S)-S-oxide + thioredoxin. HAMAP MF_01400

L-methionine + thioredoxin disulfide + H2O = L-methionine (S)-S-oxide + thioredoxin. HAMAP MF_01400

Peptide-L-methionine + thioredoxin disulfide + H2O = peptide-L-methionine (R)-S-oxide + thioredoxin.

Domain

Possesses 2 methionine sulfoxide reductase domains (A/MsrA and B/MsrB) and 1 N-terminal thioredoxin domain. The domain B exhibits a thioredoxin dependent methionine sulfoxide reductase activity; the Cys-495 is probably involved in the reduction of MetSO and in formation of the sulfenic acid derivative. The regeneration of Cys-495 is probably done via formation of a disulfide bond with Cys-440 followed by its reduction by thioredoxin. HAMAP MF_01400

Sequence similarities

In the N-terminal section; belongs to the thioredoxin family.

In the central section; belongs to the MsrA Met sulfoxide reductase family.

In the C-terminal section; belongs to the MsrB Met sulfoxide reductase family.

Contains 1 thioredoxin domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 522522Peptide methionine sulfoxide reductase MsrA/MsrB HAMAP MF_01400
PRO_0000138510

Regions

Domain17 – 174158Thioredoxin
Region199 – 354156Peptide methionine sulfoxide reductase A HAMAP MF_01400
Region383 – 506124Peptide methionine sulfoxide reductase B HAMAP MF_01400

Sites

Active site2071 By similarity

Amino acid modifications

Disulfide bond68 ↔ 71Redox-active By similarity
Disulfide bond440 ↔ 495 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9K1N8 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 535A823EDB76BFD1

FASTA52258,015
        10         20         30         40         50         60 
MKHRTFFSLC AKFGCLLALG ACSPKIVDAG AATVPHTLST LKTADNRPAS VYLKKDKPTL 

        70         80         90        100        110        120 
IKFWASWCPL CLSELGQTEK WAQDAKFSSA NLITVASPGF LHEKKDGDFQ KWYAGLNYPK 

       130        140        150        160        170        180 
LPVVTDNGGT IAQSLNISVY PSWALIGKDS DVQRIVKGSI NEAQALALIR DPNADLGSLK 

       190        200        210        220        230        240 
HSFYKPDTQK KDSKIMNTRT IYLAGGCFWG LEAYFQRIDG VVDAVSGYAN GNTKNPSYED 

       250        260        270        280        290        300 
VSYRHTGHAE TVKVTYDADK LSLDDILQYF FRVVDPTSLN KQGNDTGTQY RSGVYYTDPA 

       310        320        330        340        350        360 
EKAVIAAALK REQQKYQLPL VVENEPLKNF YDAEEYHQDY LIKNPNGYCH IDIRKADEPL 

       370        380        390        400        410        420 
PGKTKTAPQG KGFDAATYKK PSDAELKRTL TEEQYQVTQN SATEYAFSHE YDHLFKPGIY 

       430        440        450        460        470        480 
VDVVSGEPLF SSADKYDSGC GWPSFTRPID AKSVTEHDDF SYNMRRTEVR SHAADSHLGH 

       490        500        510        520 
VFPDGPRDKG GLRYCINGAS LKFIPLEQMD AAGYGALKGK VK

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE002098 Genomic DNA. Translation: AAF40515.1.
PIRG81243.
RefSeqNP_273110.1. NC_003112.2.

3D structure databases

ProteinModelPortalQ9K1N8.
SMRQ9K1N8. Positions 32-182, 196-364, 375-521.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBNEIT00000010923; EBNEIP00000010543; EBNEIG00000010923.
GeneID902147.
GenomeReviewsGene locus NMB0044 in contig AE002098_GR.
KEGGnme:NMB0044.
NMPDRfig|122586.1.peg.44.
PATRIC20355045. VBINeiMen85645_0059.
TIGRNMB0044.

Phylogenomic databases

GeneTreeEBGT00050000021048.
HOGENOMHBG715255.
OMAYYFRVVD.
ProtClustDBPRK14018.

Enzyme and pathway databases

BioCycNMEN122586:NMB_0044-MONOMER.

Family and domain databases

HAMAPMF_01400. MsrB. Fused.
[Tree]
MF_01401. MsrA. Fused.
[Tree]
InterProIPR002579. Methionine_sulphoxide_MsrB.
IPR011057. Mss4-like.
IPR002569. Peptide_Met_Sox_Rdtase_MsrA.
IPR013740. Redoxin.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
Gene3DG3DSA:3.30.1060.10. MsrA. 1 hit.
G3DSA:2.170.150.20. MsrB. 1 hit.
G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.
KOK12267.
PfamPF01625. PMSR. 1 hit.
PF08534. Redoxin. 1 hit.
PF01641. SelR. 1 hit.
[Graphical view]
SUPFAMSSF55068. MsrA. 1 hit.
SSF51316. Mss4_like. 1 hit.
SSF52833. Thiordxn-like_fd. 1 hit.
TIGRFAMsTIGR00401. MsrA. 1 hit.
TIGR00357. TIGR00357. 1 hit.
PROSITEPS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMSRAB_NEIMB
AccessionPrimary (citable) accession number: Q9K1N8
Entry history
Integrated into UniProtKB/Swiss-Prot: May 2, 2002
Last sequence update: October 1, 2000
Last modified: January 25, 2012
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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