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Protein

Peptide methionine sulfoxide reductase MsrB

Gene

msrB

Organism
Burkholderia ambifaria (strain ATCC BAA-244 / AMMD) (Burkholderia cepacia (strain AMMD))
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

Catalytic activityi

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

Cofactori

Zn2+UniRule annotationNote: Binds 1 zinc ion per subunit. The zinc ion is important for the structural integrity of the protein.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi55 – 551ZincPROSITE-ProRule annotation
Metal bindingi58 – 581ZincPROSITE-ProRule annotation
Metal bindingi104 – 1041ZincPROSITE-ProRule annotation
Metal bindingi107 – 1071ZincPROSITE-ProRule annotation
Active sitei128 – 1281NucleophilePROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciBAMB339670:GH48-1942-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Peptide methionine sulfoxide reductase MsrBUniRule annotation (EC:1.8.4.12UniRule annotation)
Alternative name(s):
Peptide-methionine (R)-S-oxide reductaseUniRule annotation
Gene namesi
Name:msrBUniRule annotation
Ordered Locus Names:Bamb_1897
OrganismiBurkholderia ambifaria (strain ATCC BAA-244 / AMMD) (Burkholderia cepacia (strain AMMD))
Taxonomic identifieri339670 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiaBurkholderia cepacia complex
Proteomesi
  • UP000000662 Componenti: Chromosome 1

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 143143Peptide methionine sulfoxide reductase MsrBPRO_1000145355Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi339670.Bamb_1897.

Structurei

3D structure databases

ProteinModelPortaliQ0BEH0.
SMRiQ0BEH0. Positions 10-140.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini16 – 139124MsrBPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the MsrB Met sulfoxide reductase family.UniRule annotation
Contains 1 MsrB (methionine-R-sulfoxide reductase) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG4105E0X. Bacteria.
COG0229. LUCA.
HOGENOMiHOG000243425.
KOiK07305.
OMAiKFIPYEQ.
OrthoDBiPOG091H064P.

Family and domain databases

Gene3Di2.170.150.20. 1 hit.
HAMAPiMF_01400. MsrB. 1 hit.
InterProiIPR028427. Met_Sox_Rdtase.
IPR002579. Met_Sox_Rdtase_MsrB.
IPR011057. Mss4-like.
[Graphical view]
PANTHERiPTHR10173. PTHR10173. 1 hit.
PfamiPF01641. SelR. 1 hit.
[Graphical view]
SUPFAMiSSF51316. SSF51316. 1 hit.
TIGRFAMsiTIGR00357. TIGR00357. 1 hit.
PROSITEiPS51790. MSRB. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q0BEH0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSHDTDDKTY PYQKDDAELR RRLTPMQYEV TQHAATERAF TGEYTDTEDA
60 70 80 90 100
GIYKCVVCST PLFESGAKFH SGCGWPSYFK PLNGEVIDEK IDRTHGMVRV
110 120 130 140
EVRCNHCGAH LGHVFEDGPR DKTGLRYCIN SAALNFESRP ENE
Length:143
Mass (Da):16,267
Last modified:October 17, 2006 - v1
Checksum:i048B947F5A546643
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000440 Genomic DNA. Translation: ABI87453.1.
RefSeqiWP_011657150.1. NZ_CP009798.1.

Genome annotation databases

EnsemblBacteriaiABI87453; ABI87453; Bamb_1897.
KEGGibam:Bamb_1897.
PATRICi19019410. VBIBurAmb61564_1992.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000440 Genomic DNA. Translation: ABI87453.1.
RefSeqiWP_011657150.1. NZ_CP009798.1.

3D structure databases

ProteinModelPortaliQ0BEH0.
SMRiQ0BEH0. Positions 10-140.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi339670.Bamb_1897.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABI87453; ABI87453; Bamb_1897.
KEGGibam:Bamb_1897.
PATRICi19019410. VBIBurAmb61564_1992.

Phylogenomic databases

eggNOGiENOG4105E0X. Bacteria.
COG0229. LUCA.
HOGENOMiHOG000243425.
KOiK07305.
OMAiKFIPYEQ.
OrthoDBiPOG091H064P.

Enzyme and pathway databases

BioCyciBAMB339670:GH48-1942-MONOMER.

Family and domain databases

Gene3Di2.170.150.20. 1 hit.
HAMAPiMF_01400. MsrB. 1 hit.
InterProiIPR028427. Met_Sox_Rdtase.
IPR002579. Met_Sox_Rdtase_MsrB.
IPR011057. Mss4-like.
[Graphical view]
PANTHERiPTHR10173. PTHR10173. 1 hit.
PfamiPF01641. SelR. 1 hit.
[Graphical view]
SUPFAMiSSF51316. SSF51316. 1 hit.
TIGRFAMsiTIGR00357. TIGR00357. 1 hit.
PROSITEiPS51790. MSRB. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiMSRB_BURCM
AccessioniPrimary (citable) accession number: Q0BEH0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: October 17, 2006
Last modified: September 7, 2016
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. 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.