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Protein

Glutaredoxin-2

Gene

grxB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Involved in reducing some disulfide bonds in a coupled system with glutathione reductase. Does not act as hydrogen donor for ribonucleotide reductase.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Electron transport, Transport

Enzyme and pathway databases

BioCyciEcoCyc:GRXB-MONOMER.
ECOL316407:JW1051-MONOMER.
MetaCyc:GRXB-MONOMER.
SABIO-RKP0AC59.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutaredoxin-2
Short name:
Grx2
Gene namesi
Name:grxB
Ordered Locus Names:b1064, JW1051
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG12688. grxB.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001415851 – 215Glutaredoxin-2Add BLAST215

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi9 ↔ 12Redox-activeBy similarity

Keywords - PTMi

Disulfide bond

Proteomic databases

EPDiP0AC59.
PaxDbiP0AC59.
PRIDEiP0AC59.

Interactioni

Protein-protein interaction databases

BioGridi4260069. 15 interactors.
DIPiDIP-48247N.
IntActiP0AC59. 1 interactor.
STRINGi511145.b1064.

Structurei

Secondary structure

1215
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 5Combined sources4
Helixi10 – 21Combined sources12
Beta strandi27 – 30Combined sources4
Helixi37 – 43Combined sources7
Beta strandi44 – 46Combined sources3
Beta strandi50 – 52Combined sources3
Turni54 – 56Combined sources3
Beta strandi58 – 60Combined sources3
Helixi62 – 71Combined sources10
Helixi84 – 94Combined sources11
Turni95 – 97Combined sources3
Helixi98 – 105Combined sources8
Helixi111 – 113Combined sources3
Helixi116 – 130Combined sources15
Helixi133 – 138Combined sources6
Helixi140 – 155Combined sources16
Beta strandi159 – 162Combined sources4
Helixi170 – 182Combined sources13
Helixi192 – 205Combined sources14
Helixi211 – 213Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1G7ONMR-A1-215[»]
4KSMX-ray2.40A1-215[»]
4KX4X-ray1.60A1-215[»]
ProteinModelPortaliP0AC59.
SMRiP0AC59.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0AC59.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 77GST N-terminalAdd BLAST77

Sequence similaritiesi

Belongs to the glutaredoxin family.Curated
Contains 1 GST N-terminal domain.Curated

Keywords - Domaini

Redox-active center

Phylogenomic databases

eggNOGiENOG4105E9S. Bacteria.
COG2999. LUCA.
HOGENOMiHOG000064700.
InParanoidiP0AC59.
KOiK03675.
OMAiLRNLTCV.

Family and domain databases

CDDicd03199. GST_C_GRX2. 1 hit.
Gene3Di1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProiIPR011767. GLR_AS.
IPR007494. Glutaredoxin2_C.
IPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR011901. Grx2.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF04399. Glutaredoxin2_C. 1 hit.
PF13417. GST_N_3. 1 hit.
[Graphical view]
SUPFAMiSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
TIGRFAMsiTIGR02182. GRXB. 1 hit.
PROSITEiPS00195. GLUTAREDOXIN_1. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0AC59-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKLYIYDHCP YCLKARMIFG LKNIPVELHV LLNDDAETPT RMVGQKQVPI
60 70 80 90 100
LQKDDSRYMP ESMDIVHYVD KLDGKPLLTG KRSPAIEEWL RKVNGYANKL
110 120 130 140 150
LLPRFAKSAF DEFSTPAARK YFVDKKEASA GNFADLLAHS DGLIKNISDD
160 170 180 190 200
LRALDKLIVK PNAVNGELSE DDIQLFPLLR NLTLVAGINW PSRVADYRDN
210
MAKQTQINLL SSMAI
Length:215
Mass (Da):24,350
Last modified:November 8, 2005 - v1
Checksum:iA8AAAB2548D824FE
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti13L → I AA sequence (PubMed:7937896).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X92076 Genomic DNA. Translation: CAA63058.1.
U00096 Genomic DNA. Translation: AAC74148.1.
AP009048 Genomic DNA. Translation: BAA35872.1.
PIRiE64849.
RefSeqiNP_415582.1. NC_000913.3.
WP_000780912.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC74148; AAC74148; b1064.
BAA35872; BAA35872; BAA35872.
GeneIDi946926.
KEGGiecj:JW1051.
eco:b1064.
PATRICi32117367. VBIEscCol129921_1106.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X92076 Genomic DNA. Translation: CAA63058.1.
U00096 Genomic DNA. Translation: AAC74148.1.
AP009048 Genomic DNA. Translation: BAA35872.1.
PIRiE64849.
RefSeqiNP_415582.1. NC_000913.3.
WP_000780912.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1G7ONMR-A1-215[»]
4KSMX-ray2.40A1-215[»]
4KX4X-ray1.60A1-215[»]
ProteinModelPortaliP0AC59.
SMRiP0AC59.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260069. 15 interactors.
DIPiDIP-48247N.
IntActiP0AC59. 1 interactor.
STRINGi511145.b1064.

Proteomic databases

EPDiP0AC59.
PaxDbiP0AC59.
PRIDEiP0AC59.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74148; AAC74148; b1064.
BAA35872; BAA35872; BAA35872.
GeneIDi946926.
KEGGiecj:JW1051.
eco:b1064.
PATRICi32117367. VBIEscCol129921_1106.

Organism-specific databases

EchoBASEiEB2551.
EcoGeneiEG12688. grxB.

Phylogenomic databases

eggNOGiENOG4105E9S. Bacteria.
COG2999. LUCA.
HOGENOMiHOG000064700.
InParanoidiP0AC59.
KOiK03675.
OMAiLRNLTCV.

Enzyme and pathway databases

BioCyciEcoCyc:GRXB-MONOMER.
ECOL316407:JW1051-MONOMER.
MetaCyc:GRXB-MONOMER.
SABIO-RKP0AC59.

Miscellaneous databases

EvolutionaryTraceiP0AC59.
PROiP0AC59.

Family and domain databases

CDDicd03199. GST_C_GRX2. 1 hit.
Gene3Di1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProiIPR011767. GLR_AS.
IPR007494. Glutaredoxin2_C.
IPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR011901. Grx2.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF04399. Glutaredoxin2_C. 1 hit.
PF13417. GST_N_3. 1 hit.
[Graphical view]
SUPFAMiSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
TIGRFAMsiTIGR02182. GRXB. 1 hit.
PROSITEiPS00195. GLUTAREDOXIN_1. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiGLRX2_ECOLI
AccessioniPrimary (citable) accession number: P0AC59
Secondary accession number(s): P39811, P75928, P77043
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: November 8, 2005
Last modified: November 30, 2016
This is version 90 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.