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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)DescriptionActionsGraphical viewLength
Active sitei207By similarity1
Active sitei495NucleophilePROSITE-ProRule annotation1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Electron transport, Transport

Enzyme and pathway databases

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

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001385091 – 522Peptide methionine sulfoxide reductase MsrA/MsrBAdd BLAST522

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi68 ↔ 71Redox-activeBy similarity
Disulfide bondi440 ↔ 495Curated

Keywords - PTMi

Disulfide bond

Structurei

Secondary structure

1522
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi35 – 39Combined sources5
Beta strandi46 – 48Combined sources3
Helixi49 – 52Combined sources4
Beta strandi59 – 64Combined sources6
Helixi69 – 72Combined sources4
Helixi75 – 83Combined sources9
Helixi85 – 87Combined sources3
Beta strandi90 – 96Combined sources7
Beta strandi100 – 102Combined sources3
Helixi108 – 113Combined sources6
Beta strandi123 – 125Combined sources3
Helixi130 – 134Combined sources5
Beta strandi139 – 146Combined sources8
Beta strandi152 – 158Combined sources7
Helixi162 – 170Combined sources9
Beta strandi198 – 206Combined sources9
Helixi208 – 216Combined sources9
Beta strandi221 – 230Combined sources10
Beta strandi232 – 235Combined sources4
Helixi238 – 243Combined sources6
Beta strandi249 – 257Combined sources9
Turni258 – 260Combined sources3
Helixi263 – 273Combined sources11
Helixi278 – 280Combined sources3
Beta strandi281 – 283Combined sources3
Beta strandi285 – 287Combined sources3
Helixi288 – 290Combined sources3
Beta strandi292 – 298Combined sources7
Helixi299 – 313Combined sources15
Beta strandi323 – 326Combined sources4
Beta strandi330 – 332Combined sources3
Helixi335 – 337Combined sources3
Helixi340 – 343Combined sources4
Turni355 – 357Combined sources3
Helixi383 – 389Combined sources7
Helixi392 – 400Combined sources9
Helixi410 – 413Combined sources4
Beta strandi417 – 422Combined sources6
Turni423 – 425Combined sources3
Beta strandi428 – 431Combined sources4
Helixi432 – 434Combined sources3
Beta strandi439 – 442Combined sources4
Beta strandi444 – 447Combined sources4
Helixi451 – 453Combined sources3
Beta strandi454 – 461Combined sources8
Beta strandi464 – 471Combined sources8
Turni472 – 474Combined sources3
Beta strandi477 – 483Combined sources7
Helixi487 – 489Combined sources3
Beta strandi493 – 496Combined sources4
Helixi498 – 500Combined sources3
Beta strandi501 – 505Combined sources5
Helixi506 – 508Combined sources3
Helixi509 – 512Combined sources4
Helixi515 – 520Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9JWM8.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini17 – 174ThioredoxinAdd BLAST158
Domaini383 – 506MsrBPROSITE-ProRule annotationAdd BLAST124

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni199 – 354Peptide methionine sulfoxide reductase AAdd BLAST156

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.

Family and domain databases

Gene3Di2.170.150.20. 1 hit.
3.30.1060.10. 1 hit.
3.40.30.10. 1 hit.
HAMAPiMF_01401. MsrA. 1 hit.
MF_01400. MsrB. 1 hit.
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
PDB 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.
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.

Enzyme and pathway databases

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_01401. MsrA. 1 hit.
MF_01400. MsrB. 1 hit.
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...

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: November 2, 2016
This is version 120 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.