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Protein
Submitted name:

NRDH-redoxin

Gene

BC_3987

Organism
Bacillus cereus (strain ATCC 14579 / DSM 31)
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

  1. electron carrier activity Source: InterPro
  2. protein disulfide oxidoreductase activity Source: InterPro

GO - Biological processi

  1. cell redox homeostasis Source: InterPro
Complete GO annotation...

Enzyme and pathway databases

BioCyciBCER226900:GJEU-3983-MONOMER.

Names & Taxonomyi

Protein namesi
Submitted name:
NRDH-redoxinImported
Gene namesi
Ordered Locus Names:BC_3987Imported
OrganismiBacillus cereus (strain ATCC 14579 / DSM 31)Imported
Taxonomic identifieri226900 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group
ProteomesiUP000001417 Componenti: Chromosome

PTM / Processingi

Proteomic databases

PRIDEiQ819J1.

Interactioni

Protein-protein interaction databases

STRINGi226900.BC3987.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3ZIJX-ray1.40A/B1-78[»]
3ZITX-ray1.18A/B1-78[»]
ProteinModelPortaliQ819J1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Phylogenomic databases

eggNOGiCOG0695.
OMAiINHAFNI.
OrthoDBiEOG64FKJQ.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR011911. GlrX_YruB.
IPR002109. Glutaredoxin.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF00462. Glutaredoxin. 1 hit.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 1 hit.
TIGRFAMsiTIGR02196. GlrX_YruB. 1 hit.
PROSITEiPS51354. GLUTAREDOXIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q819J1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKIEVYTQP DCPPCVIVKE FLKHNNVAYE EFDVKKDAAA RNRLLYDYDS
60 70
YSTPTVVIDG EVVAGFQIEK LQQLLNIE
Length:78
Mass (Da):8,995
Last modified:June 1, 2003 - v1
Checksum:i0EDA3E97229BB2AC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016877 Genomic DNA. Translation: AAP10907.1.
RefSeqiNP_833706.1. NC_004722.1.

Genome annotation databases

EnsemblBacteriaiAAP10907; AAP10907; BC_3987.
GeneIDi1206332.
KEGGibce:BC3987.
PATRICi32604022. VBIBacCer54481_4114.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016877 Genomic DNA. Translation: AAP10907.1.
RefSeqiNP_833706.1. NC_004722.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3ZIJX-ray1.40A/B1-78[»]
3ZITX-ray1.18A/B1-78[»]
ProteinModelPortaliQ819J1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi226900.BC3987.

Proteomic databases

PRIDEiQ819J1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAP10907; AAP10907; BC_3987.
GeneIDi1206332.
KEGGibce:BC3987.
PATRICi32604022. VBIBacCer54481_4114.

Phylogenomic databases

eggNOGiCOG0695.
OMAiINHAFNI.
OrthoDBiEOG64FKJQ.

Enzyme and pathway databases

BioCyciBCER226900:GJEU-3983-MONOMER.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR011911. GlrX_YruB.
IPR002109. Glutaredoxin.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF00462. Glutaredoxin. 1 hit.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 1 hit.
TIGRFAMsiTIGR02196. GlrX_YruB. 1 hit.
PROSITEiPS51354. GLUTAREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 14579 / DSM 31Imported.
  2. "Tuning of thioredoxin redox properties by intramolecular hydrogen bonds."
    Rohr A.K., Hammerstad M., Andersson K.K.
    PLoS ONE 8:e69411-e69411(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.18 ANGSTROMS), ACTIVE SITE.

Entry informationi

Entry nameiQ819J1_BACCR
AccessioniPrimary (citable) accession number: Q819J1
Entry historyi
Integrated into UniProtKB/TrEMBL: June 1, 2003
Last sequence update: June 1, 2003
Last modified: January 7, 2015
This is version 69 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources, Complete proteome, Reference proteomeImported

External Data

Dasty 3

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 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.