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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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
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)DescriptionActionsGraphical viewLength
ChainiPRO_00001415811 – 85Glutaredoxin-1Add BLAST85

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi11 ↔ 14Redox-active

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiP68688.
PRIDEiP68688.

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

BioGridi4259990. 7 interactors.
IntActiP68688. 16 interactors.
STRINGi511145.b0849.

Structurei

Secondary structure

185
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 6Combined sources5
Helixi13 – 28Combined sources16
Beta strandi32 – 36Combined sources5
Helixi38 – 41Combined sources4
Helixi46 – 51Combined sources6
Beta strandi61 – 64Combined sources4
Beta strandi67 – 72Combined sources6
Helixi73 – 84Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP68688.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 85GlutaredoxinPROSITE-ProRule annotationAdd BLAST85

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.
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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259990. 7 interactors.
IntActiP68688. 16 interactors.
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.
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...

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: November 2, 2016
This is version 99 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.