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Protein

Glutaredoxin-1

Gene

grxA

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

Functioni

The disulfide bond functions as an electron carrier in the glutathione-dependent synthesis of deoxyribonucleotides by the enzyme ribonucleotide reductase. In addition, it is also involved in reducing some disulfide bonds in a coupled system with glutathione reductase.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Deoxyribonucleotide synthesis, Electron transport, Transport

Enzyme and pathway databases

BioCyciEcoCyc:RED-GLUTAREDOXIN.
ECOL316407:JW0833-MONOMER.
MetaCyc:RED-GLUTAREDOXIN.
SABIO-RKP68688.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutaredoxin-1
Short name:
Grx1
Gene namesi
Name:grxA
Synonyms:grx
Ordered Locus Names:b0849, JW0833
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10417. grxA.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 8585Glutaredoxin-1PRO_0000141581Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi11 ↔ 14Redox-active

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiP68688.
PRIDEiP68688.

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

BioGridi4259990. 7 interactions.
IntActiP68688. 16 interactions.
STRINGi511145.b0849.

Structurei

Secondary structure

1
85
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 65Combined sources
Helixi13 – 2816Combined sources
Beta strandi32 – 365Combined sources
Helixi38 – 414Combined sources
Helixi46 – 516Combined sources
Beta strandi61 – 644Combined sources
Beta strandi67 – 726Combined sources
Helixi73 – 8412Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EGONMR-A1-85[»]
1EGRNMR-A1-85[»]
1GRXNMR-A1-85[»]
1QFNNMR-A1-85[»]
1UPYmodel-G1-85[»]
1UPZmodel-G1-85[»]
1UQ0model-G1-85[»]
1UQ1model-G1-85[»]
1UQ2model-G1-85[»]
1UQ3model-G1-85[»]
1UQ6model-G1-85[»]
1UQ7model-G1-85[»]
1UQHmodel-G1-85[»]
1UQNmodel-G1-85[»]
ProteinModelPortaliP68688.
SMRiP68688. Positions 1-85.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP68688.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 8585GlutaredoxinPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the glutaredoxin family.Curated
Contains 1 glutaredoxin domain.PROSITE-ProRule annotation

Keywords - Domaini

Redox-active center

Phylogenomic databases

eggNOGiENOG41090BQ. Bacteria.
COG0695. LUCA.
HOGENOMiHOG000095203.
InParanoidiP68688.
KOiK03674.
OMAiVGGCTEF.
OrthoDBiEOG6Z3KS6.
PhylomeDBiP68688.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR011767. GLR_AS.
IPR002109. Glutaredoxin.
IPR014025. Glutaredoxin_subgr.
IPR011902. GRXA.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF00462. Glutaredoxin. 1 hit.
[Graphical view]
PRINTSiPR00160. GLUTAREDOXIN.
SUPFAMiSSF52833. SSF52833. 1 hit.
TIGRFAMsiTIGR02183. GRXA. 1 hit.
PROSITEiPS00195. GLUTAREDOXIN_1. 1 hit.
PS51354. GLUTAREDOXIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P68688-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQTVIFGRSG CPYCVRAKDL AEKLSNERDD FQYQYVDIRA EGITKEDLQQ
60 70 80
KAGKPVETVP QIFVDQQHIG GYTDFAAWVK ENLDA
Length:85
Mass (Da):9,685
Last modified:July 21, 1986 - v1
Checksum:i33C185A47021EF42
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M13449 Genomic DNA. Translation: AAA23936.1.
U18655 Genomic DNA. Translation: AAC43449.1.
U00096 Genomic DNA. Translation: AAC73936.1.
AP009048 Genomic DNA. Translation: BAA35552.1.
PIRiA00283. GDEC.
RefSeqiNP_415370.1. NC_000913.3.
WP_001195240.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73936; AAC73936; b0849.
BAA35552; BAA35552; BAA35552.
GeneIDi945479.
KEGGiecj:JW0833.
eco:b0849.
PATRICi32116903. VBIEscCol129921_0877.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M13449 Genomic DNA. Translation: AAA23936.1.
U18655 Genomic DNA. Translation: AAC43449.1.
U00096 Genomic DNA. Translation: AAC73936.1.
AP009048 Genomic DNA. Translation: BAA35552.1.
PIRiA00283. GDEC.
RefSeqiNP_415370.1. NC_000913.3.
WP_001195240.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EGONMR-A1-85[»]
1EGRNMR-A1-85[»]
1GRXNMR-A1-85[»]
1QFNNMR-A1-85[»]
1UPYmodel-G1-85[»]
1UPZmodel-G1-85[»]
1UQ0model-G1-85[»]
1UQ1model-G1-85[»]
1UQ2model-G1-85[»]
1UQ3model-G1-85[»]
1UQ6model-G1-85[»]
1UQ7model-G1-85[»]
1UQHmodel-G1-85[»]
1UQNmodel-G1-85[»]
ProteinModelPortaliP68688.
SMRiP68688. Positions 1-85.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259990. 7 interactions.
IntActiP68688. 16 interactions.
STRINGi511145.b0849.

Proteomic databases

PaxDbiP68688.
PRIDEiP68688.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73936; AAC73936; b0849.
BAA35552; BAA35552; BAA35552.
GeneIDi945479.
KEGGiecj:JW0833.
eco:b0849.
PATRICi32116903. VBIEscCol129921_0877.

Organism-specific databases

EchoBASEiEB0412.
EcoGeneiEG10417. grxA.

Phylogenomic databases

eggNOGiENOG41090BQ. Bacteria.
COG0695. LUCA.
HOGENOMiHOG000095203.
InParanoidiP68688.
KOiK03674.
OMAiVGGCTEF.
OrthoDBiEOG6Z3KS6.
PhylomeDBiP68688.

Enzyme and pathway databases

BioCyciEcoCyc:RED-GLUTAREDOXIN.
ECOL316407:JW0833-MONOMER.
MetaCyc:RED-GLUTAREDOXIN.
SABIO-RKP68688.

Miscellaneous databases

EvolutionaryTraceiP68688.
PROiP68688.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR011767. GLR_AS.
IPR002109. Glutaredoxin.
IPR014025. Glutaredoxin_subgr.
IPR011902. GRXA.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF00462. Glutaredoxin. 1 hit.
[Graphical view]
PRINTSiPR00160. GLUTAREDOXIN.
SUPFAMiSSF52833. SSF52833. 1 hit.
TIGRFAMsiTIGR02183. GRXA. 1 hit.
PROSITEiPS00195. GLUTAREDOXIN_1. 1 hit.
PS51354. GLUTAREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The primary structure of Escherichia coli glutaredoxin. Distant homology with thioredoxins in a superfamily of small proteins with a redox-active cystine disulfide/cysteine dithiol."
    Hoeoeg J.-O., Joernvall H., Holmgren A., Carlquist M., Persson M.
    Eur. J. Biochem. 136:223-232(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE.
    Strain: K12.
  2. "Cloning and expression of the glutaredoxin (grx) gene of Escherichia coli."
    Hoeoeg J.-O., von Bahr-Lindstroem H., Joernvall H., Holmgren A.
    Gene 43:13-21(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. Chatterjee P.K., Sternberg N.L.
    Submitted (DEC-1994) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  6. "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.
  7. "Escherichia coli proteome analysis using the gene-protein database."
    VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
    Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY 2D-GEL.
  8. "Nuclear magnetic resonance studies of recombinant Escherichia coli glutaredoxin. Sequence-specific assignments and secondary structure determination of the oxidized form."
    Sodano P., Chary K.V.R., Bjoernberg O., Holmgren A., Kren B., Fuchs J.A., Wuethrich K.
    Eur. J. Biochem. 200:369-377(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.
  9. "Sequence-specific 1H NMR assignments and determination of the three-dimensional structure of reduced Escherichia coli glutaredoxin."
    Sodano P., Xia T.-H., Bushweller J.H., Bjoernberg O., Holmgren A., Billeter M., Wuethrich K.
    J. Mol. Biol. 221:1311-1324(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.
  10. "NMR structure of oxidized Escherichia coli glutaredoxin: comparison with reduced E. coli glutaredoxin and functionally related proteins."
    Xia T.-H., Bushweller J.H., Sodano P., Billeter M., Bjoernberg O., Holmgren A., Wuethrich K.
    Protein Sci. 1:310-321(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.
  11. "Comparison of backbone dynamics of reduced and oxidized Escherichia coli glutaredoxin-1 using 15N NMR relaxation measurements."
    Kelley J.J. III, Caputo M., Eaton S.F., Laue T.M., Bushweller J.H.
    Biochemistry 36:5029-5044(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.

Entry informationi

Entry nameiGLRX1_ECOLI
AccessioniPrimary (citable) accession number: P68688
Secondary accession number(s): P00277
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: January 20, 2016
This is version 97 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.