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Protein

Peptide methionine sulfoxide reductase MsrA/MsrB

Gene

msrAB

Organism
Neisseria meningitidis serogroup A / serotype 4A (strain Z2491)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Has an important function as a repair enzyme for proteins that have been inactivated by oxidation (By similarity). Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine.By similarity

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei207 – 2071By similarity
Active sitei495 – 4951NucleophilePROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Electron transport, Transport

Enzyme and pathway databases

BioCyciNMEN122587:GI3Q-281-MONOMER.
BRENDAi1.8.4.11. 3593.
1.8.4.12. 3593.
SABIO-RKQ9JWM8.

Names & Taxonomyi

Protein namesi
Recommended name:
Peptide methionine sulfoxide reductase MsrA/MsrB
Including the following 3 domains:
Thioredoxin
Peptide methionine sulfoxide reductase MsrA (EC:1.8.4.11)
Short name:
Protein-methionine-S-oxide reductase
Alternative name(s):
Peptide-methionine (S)-S-oxide reductase
Short name:
Peptide Met(O) reductase
Peptide methionine sulfoxide reductase MsrB (EC:1.8.4.12)
Alternative name(s):
Peptide-methionine (R)-S-oxide reductase
Gene namesi
Name:msrAB
Synonyms:pilB
Ordered Locus Names:NMA0290
OrganismiNeisseria meningitidis serogroup A / serotype 4A (strain Z2491)
Taxonomic identifieri122587 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeNeisseria
Proteomesi
  • UP000000626 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 522522Peptide methionine sulfoxide reductase MsrA/MsrBPRO_0000138509Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi68 ↔ 71Redox-activeBy similarity
Disulfide bondi440 ↔ 495Curated

Keywords - PTMi

Disulfide bond

Structurei

Secondary structure

1
522
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi35 – 395Combined sources
Beta strandi46 – 483Combined sources
Helixi49 – 524Combined sources
Beta strandi59 – 646Combined sources
Helixi69 – 724Combined sources
Helixi75 – 839Combined sources
Helixi85 – 873Combined sources
Beta strandi90 – 967Combined sources
Beta strandi100 – 1023Combined sources
Helixi108 – 1136Combined sources
Beta strandi123 – 1253Combined sources
Helixi130 – 1345Combined sources
Beta strandi139 – 1468Combined sources
Beta strandi152 – 1587Combined sources
Helixi162 – 1709Combined sources
Beta strandi198 – 2069Combined sources
Helixi208 – 2169Combined sources
Beta strandi221 – 23010Combined sources
Beta strandi232 – 2354Combined sources
Helixi238 – 2436Combined sources
Beta strandi249 – 2579Combined sources
Turni258 – 2603Combined sources
Helixi263 – 27311Combined sources
Helixi278 – 2803Combined sources
Beta strandi281 – 2833Combined sources
Beta strandi285 – 2873Combined sources
Helixi288 – 2903Combined sources
Beta strandi292 – 2987Combined sources
Helixi299 – 31315Combined sources
Beta strandi323 – 3264Combined sources
Beta strandi330 – 3323Combined sources
Helixi335 – 3373Combined sources
Helixi340 – 3434Combined sources
Turni355 – 3573Combined sources
Helixi383 – 3897Combined sources
Helixi392 – 4009Combined sources
Helixi410 – 4134Combined sources
Beta strandi417 – 4226Combined sources
Turni423 – 4253Combined sources
Beta strandi428 – 4314Combined sources
Helixi432 – 4343Combined sources
Beta strandi439 – 4424Combined sources
Beta strandi444 – 4474Combined sources
Helixi451 – 4533Combined sources
Beta strandi454 – 4618Combined sources
Beta strandi464 – 4718Combined sources
Turni472 – 4743Combined sources
Beta strandi477 – 4837Combined sources
Helixi487 – 4893Combined sources
Beta strandi493 – 4964Combined sources
Helixi498 – 5003Combined sources
Beta strandi501 – 5055Combined sources
Helixi506 – 5083Combined sources
Helixi509 – 5124Combined sources
Helixi515 – 5206Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2FY6X-ray1.90A34-176[»]
2JZRNMR-A34-176[»]
2JZSNMR-A34-176[»]
2K9FNMR-A34-176[»]
3BQEX-ray2.00A196-389[»]
3BQFX-ray2.24A196-389[»]
3BQGX-ray2.00A196-389[»]
3BQHX-ray1.95A197-389[»]
3HCGX-ray1.82A/B/C/D377-522[»]
3HCHX-ray2.10A/B377-522[»]
ProteinModelPortaliQ9JWM8.
SMRiQ9JWM8. Positions 34-176, 196-364, 375-521.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9JWM8.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini17 – 174158ThioredoxinAdd
BLAST
Domaini383 – 506124MsrBPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni199 – 354156Peptide methionine sulfoxide reductase AAdd
BLAST

Domaini

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.

Sequence similaritiesi

In the N-terminal section; belongs to the thioredoxin family.Curated
In the central section; belongs to the MsrA Met sulfoxide reductase family.Curated
In the C-terminal section; belongs to the MsrB Met sulfoxide reductase family.Curated
Contains 1 MsrB (methionine-R-sulfoxide reductase) domain.PROSITE-ProRule annotation
Contains 1 thioredoxin domain.Curated

Keywords - Domaini

Redox-active center

Phylogenomic databases

HOGENOMiHOG000243423.
KOiK12267.
OMAiWIDEKNG.
OrthoDBiEOG6091JX.

Family and domain databases

Gene3Di2.170.150.20. 1 hit.
3.30.1060.10. 1 hit.
3.40.30.10. 1 hit.
HAMAPiMF_01400. MsrB.
MF_01401. MsrA.
InterProiIPR028427. Met_Sox_Rdtase.
IPR002569. Met_Sox_Rdtase_MsrA.
IPR002579. Met_Sox_Rdtase_MsrB.
IPR011057. Mss4-like.
IPR013740. Redoxin.
IPR012336. Thioredoxin-like_fold.
IPR013766. Thioredoxin_domain.
[Graphical view]
PANTHERiPTHR10173. PTHR10173. 2 hits.
PfamiPF01625. PMSR. 1 hit.
PF08534. Redoxin. 1 hit.
PF01641. SelR. 1 hit.
[Graphical view]
SUPFAMiSSF51316. SSF51316. 1 hit.
SSF52833. SSF52833. 1 hit.
SSF55068. SSF55068. 1 hit.
TIGRFAMsiTIGR00401. msrA. 1 hit.
TIGR00357. TIGR00357. 1 hit.
PROSITEiPS51790. MSRB. 1 hit.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9JWM8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKHRTFFSLC AKFGCLLALG ACSPKIVDAG AATVPHTLST LKTADNRPAS
60 70 80 90 100
VYLKKDKPTL IKFWASWCPL CLSELGQTEK WAQDAKFSSA NLITVASPGF
110 120 130 140 150
LHEKKDGDFQ KWYAGLNYPK LPVVTDNGGT IAQSLNISVY PSWALIGKDG
160 170 180 190 200
DVQRIVKGSI NEAQALALIR DPNADLGSLK HSFYKPDTQK KDSKIMNTRT
210 220 230 240 250
IYLAGGCFWG LEAYFQRIDG VVDAVSGYAN GNTKNPSYED VSYRHTGHAE
260 270 280 290 300
TVKVTYDADK LSLDDILQYF FRVVDPTSLN KQGNDTGTQY RSGVYYTDPA
310 320 330 340 350
EKAVIAAALK REQQKYQLPL VVENEPLKNF YDAEEYHQDY LIKNPNGYCH
360 370 380 390 400
IDIRKADEPL PGKTKTAPQG KGFDAATYKK PSDAELKRTL TEEQYQVTQN
410 420 430 440 450
SATEYAFSHE YDHLFKPGIY VDVVSGEPLF SSADKYDSGC GWPSFTRPID
460 470 480 490 500
AKSVTEHDDF SYNMRRTEVR SHAADSHLGH VFPDGPRDKG GLRYCINGAS
510 520
LKFIPLEQMD AAGYGALKSK VK
Length:522
Mass (Da):58,015
Last modified:October 1, 2000 - v1
Checksum:iF61E8EA7189F0667
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL157959 Genomic DNA. Translation: CAM07595.1.
PIRiE82024.
RefSeqiWP_002216163.1. NC_003116.1.

Genome annotation databases

EnsemblBacteriaiCAM07595; CAM07595; NMA0290.
KEGGinma:NMA0290.
PATRICi20361222. VBINeiMen132687_0336.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL157959 Genomic DNA. Translation: CAM07595.1.
PIRiE82024.
RefSeqiWP_002216163.1. NC_003116.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2FY6X-ray1.90A34-176[»]
2JZRNMR-A34-176[»]
2JZSNMR-A34-176[»]
2K9FNMR-A34-176[»]
3BQEX-ray2.00A196-389[»]
3BQFX-ray2.24A196-389[»]
3BQGX-ray2.00A196-389[»]
3BQHX-ray1.95A197-389[»]
3HCGX-ray1.82A/B/C/D377-522[»]
3HCHX-ray2.10A/B377-522[»]
ProteinModelPortaliQ9JWM8.
SMRiQ9JWM8. Positions 34-176, 196-364, 375-521.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAM07595; CAM07595; NMA0290.
KEGGinma:NMA0290.
PATRICi20361222. VBINeiMen132687_0336.

Phylogenomic databases

HOGENOMiHOG000243423.
KOiK12267.
OMAiWIDEKNG.
OrthoDBiEOG6091JX.

Enzyme and pathway databases

BioCyciNMEN122587:GI3Q-281-MONOMER.
BRENDAi1.8.4.11. 3593.
1.8.4.12. 3593.
SABIO-RKQ9JWM8.

Miscellaneous databases

EvolutionaryTraceiQ9JWM8.

Family and domain databases

Gene3Di2.170.150.20. 1 hit.
3.30.1060.10. 1 hit.
3.40.30.10. 1 hit.
HAMAPiMF_01400. MsrB.
MF_01401. MsrA.
InterProiIPR028427. Met_Sox_Rdtase.
IPR002569. Met_Sox_Rdtase_MsrA.
IPR002579. Met_Sox_Rdtase_MsrB.
IPR011057. Mss4-like.
IPR013740. Redoxin.
IPR012336. Thioredoxin-like_fold.
IPR013766. Thioredoxin_domain.
[Graphical view]
PANTHERiPTHR10173. PTHR10173. 2 hits.
PfamiPF01625. PMSR. 1 hit.
PF08534. Redoxin. 1 hit.
PF01641. SelR. 1 hit.
[Graphical view]
SUPFAMiSSF51316. SSF51316. 1 hit.
SSF52833. SSF52833. 1 hit.
SSF55068. SSF55068. 1 hit.
TIGRFAMsiTIGR00401. msrA. 1 hit.
TIGR00357. TIGR00357. 1 hit.
PROSITEiPS51790. MSRB. 1 hit.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Z2491.
  2. "Characterization of the methionine sulfoxide reductase activities of PILB, a probable virulence factor from Neisseria meningitidis."
    Olry A., Boschi-Muller S., Marraud M., Sanglier-Cianferani S., van Dorsselaer A., Branlant G.
    J. Biol. Chem. 277:12016-12022(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION OF THE METHIONINE SULFOXIDE REDUCTASE ACTIVITIES (MSRA AND MSRB).
    Strain: Z2491.

Entry informationi

Entry nameiMSRAB_NEIMA
AccessioniPrimary (citable) accession number: Q9JWM8
Secondary accession number(s): A1IPD1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 2, 2002
Last sequence update: October 1, 2000
Last modified: July 6, 2016
This is version 117 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

The domain MsrB is stereospecific for the R isomer of the sulfoxide of MetSO whereas the domain MsrA is stereospecific for the S isomer.

Keywords - Technical termi

3D-structure, Complete proteome, Multifunctional enzyme

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.