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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.
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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 215215Glutaredoxin-2PRO_0000141585Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi9 ↔ 12Redox-activeBy similarity

Keywords - PTMi

Disulfide bond

Proteomic databases

EPDiP0AC59.
PaxDbiP0AC59.
PRIDEiP0AC59.

Interactioni

Protein-protein interaction databases

BioGridi4260069. 15 interactions.
DIPiDIP-48247N.
IntActiP0AC59. 1 interaction.
STRINGi511145.b1064.

Structurei

Secondary structure

1
215
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 54Combined sources
Helixi10 – 2112Combined sources
Beta strandi27 – 304Combined sources
Helixi37 – 437Combined sources
Beta strandi44 – 463Combined sources
Beta strandi50 – 523Combined sources
Turni54 – 563Combined sources
Beta strandi58 – 603Combined sources
Helixi62 – 7110Combined sources
Helixi84 – 9411Combined sources
Turni95 – 973Combined sources
Helixi98 – 1058Combined sources
Helixi111 – 1133Combined sources
Helixi116 – 13015Combined sources
Helixi133 – 1386Combined sources
Helixi140 – 15516Combined sources
Beta strandi159 – 1624Combined sources
Helixi170 – 18213Combined sources
Helixi192 – 20514Combined sources
Helixi211 – 2133Combined sources

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP0AC59.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 7777GST N-terminalAdd
BLAST

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.
OrthoDBiEOG64BQ52.

Family and domain databases

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. GRXB.
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti13 – 131L → I AA sequence (PubMed:7937896).Curated

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
EntryMethodResolution (Å)ChainPositionsPDBsum
1G7ONMR-A1-215[»]
4KSMX-ray2.40A1-215[»]
4KX4X-ray1.60A1-215[»]
ProteinModelPortaliP0AC59.
SMRiP0AC59. Positions 1-215.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260069. 15 interactions.
DIPiDIP-48247N.
IntActiP0AC59. 1 interaction.
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.
OrthoDBiEOG64BQ52.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiP0AC59.
PROiP0AC59.

Family and domain databases

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. GRXB.
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...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning, overexpression, and characterization of glutaredoxin 2, an atypical glutaredoxin from Escherichia coli."
    Vlamis-Gardikas A., Aaslund F., Spyrou G., Bergman T., Holmgren A.
    J. Biol. Chem. 272:11236-11243(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION.
    Strain: K12.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. "Two additional glutaredoxins exist in Escherichia coli: glutaredoxin 3 is a hydrogen donor for ribonucleotide reductase in a thioredoxin/glutaredoxin 1 double mutant."
    Aaslund F., Ehn B., Miranda-Vizuete A., Pueyo C., Holmgren A.
    Proc. Natl. Acad. Sci. U.S.A. 91:9813-9817(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-18, CHARACTERIZATION.

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: March 16, 2016
This is version 86 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.