Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Glutaredoxin-3

Gene

grxC

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 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

  • electron carrier activity Source: InterPro
  • glutathione binding Source: EcoCyc
  • protein disulfide oxidoreductase activity Source: EcoCyc

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Deoxyribonucleotide synthesis, Electron transport, Transport

Enzyme and pathway databases

BioCyciEcoCyc:GRXC-MONOMER.
ECOL316407:JW3585-MONOMER.
RETL1328306-WGS:GSTH-3840-MONOMER.
SABIO-RKP0AC62.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutaredoxin-3
Short name:
Grx3
Gene namesi
Name:grxC
Synonyms:yibM
Ordered Locus Names:b3610, JW3585
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG12294. grxC.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved2 Publications
Chaini2 – 8382Glutaredoxin-3PRO_0000141588Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi12 ↔ 15Redox-activeBy similarity

Keywords - PTMi

Disulfide bond

Proteomic databases

EPDiP0AC62.
PaxDbiP0AC62.
PRIDEiP0AC62.

Interactioni

Subunit structurei

Monomer.Curated

Protein-protein interaction databases

BioGridi4263295. 13 interactions.
IntActiP0AC62. 2 interactions.
STRINGi511145.b3610.

Structurei

Secondary structure

1
83
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 85Combined sources
Helixi13 – 2513Combined sources
Beta strandi30 – 334Combined sources
Helixi39 – 4810Combined sources
Beta strandi55 – 584Combined sources
Beta strandi61 – 655Combined sources
Helixi66 – 749Combined sources
Helixi79 – 824Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FOVNMR-A2-83[»]
1ILBmodel-A1-83[»]
1UQ8model-G2-83[»]
1UQ9model-G2-83[»]
1UQImodel-G2-83[»]
1UQJmodel-G2-83[»]
1UQKmodel-G2-83[»]
1UQLmodel-G2-83[»]
1UQMmodel-G2-83[»]
1UQOmodel-G2-83[»]
1UQPmodel-G2-83[»]
1UQQmodel-G2-83[»]
3GRXNMR-A2-83[»]
ProteinModelPortaliP0AC62.
SMRiP0AC62. Positions 2-83.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0AC62.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 8382GlutaredoxinPROSITE-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

eggNOGiENOG4105VW4. Bacteria.
COG0695. LUCA.
HOGENOMiHOG000095203.
InParanoidiP0AC62.
KOiK03676.
OMAiGYCTAAK.
OrthoDBiEOG6Z3KS6.
PhylomeDBiP0AC62.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR011767. GLR_AS.
IPR002109. Glutaredoxin.
IPR014025. Glutaredoxin_subgr.
IPR011900. GRX_bact.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF00462. Glutaredoxin. 1 hit.
[Graphical view]
PRINTSiPR00160. GLUTAREDOXIN.
SUPFAMiSSF52833. SSF52833. 1 hit.
TIGRFAMsiTIGR02181. GRX_bact. 1 hit.
PROSITEiPS00195. GLUTAREDOXIN_1. 1 hit.
PS51354. GLUTAREDOXIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0AC62-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MANVEIYTKE TCPYCHRAKA LLSSKGVSFQ ELPIDGNAAK REEMIKRSGR
60 70 80
TTVPQIFIDA QHIGGCDDLY ALDARGGLDP LLK
Length:83
Mass (Da):9,137
Last modified:January 23, 2007 - v2
Checksum:i5B19A85BB0C9FBEF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00039 Genomic DNA. Translation: AAB18587.1.
U00096 Genomic DNA. Translation: AAC76634.1.
AP009048 Genomic DNA. Translation: BAE77682.1.
PIRiS47831.
RefSeqiNP_418067.1. NC_000913.3.
WP_000024392.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76634; AAC76634; b3610.
BAE77682; BAE77682; BAE77682.
GeneIDi948132.
KEGGiecj:JW3585.
eco:b3610.
PATRICi32122705. VBIEscCol129921_3729.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00039 Genomic DNA. Translation: AAB18587.1.
U00096 Genomic DNA. Translation: AAC76634.1.
AP009048 Genomic DNA. Translation: BAE77682.1.
PIRiS47831.
RefSeqiNP_418067.1. NC_000913.3.
WP_000024392.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FOVNMR-A2-83[»]
1ILBmodel-A1-83[»]
1UQ8model-G2-83[»]
1UQ9model-G2-83[»]
1UQImodel-G2-83[»]
1UQJmodel-G2-83[»]
1UQKmodel-G2-83[»]
1UQLmodel-G2-83[»]
1UQMmodel-G2-83[»]
1UQOmodel-G2-83[»]
1UQPmodel-G2-83[»]
1UQQmodel-G2-83[»]
3GRXNMR-A2-83[»]
ProteinModelPortaliP0AC62.
SMRiP0AC62. Positions 2-83.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4263295. 13 interactions.
IntActiP0AC62. 2 interactions.
STRINGi511145.b3610.

Proteomic databases

EPDiP0AC62.
PaxDbiP0AC62.
PRIDEiP0AC62.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76634; AAC76634; b3610.
BAE77682; BAE77682; BAE77682.
GeneIDi948132.
KEGGiecj:JW3585.
eco:b3610.
PATRICi32122705. VBIEscCol129921_3729.

Organism-specific databases

EchoBASEiEB2202.
EcoGeneiEG12294. grxC.

Phylogenomic databases

eggNOGiENOG4105VW4. Bacteria.
COG0695. LUCA.
HOGENOMiHOG000095203.
InParanoidiP0AC62.
KOiK03676.
OMAiGYCTAAK.
OrthoDBiEOG6Z3KS6.
PhylomeDBiP0AC62.

Enzyme and pathway databases

BioCyciEcoCyc:GRXC-MONOMER.
ECOL316407:JW3585-MONOMER.
RETL1328306-WGS:GSTH-3840-MONOMER.
SABIO-RKP0AC62.

Miscellaneous databases

EvolutionaryTraceiP0AC62.
PROiP0AC62.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR011767. GLR_AS.
IPR002109. Glutaredoxin.
IPR014025. Glutaredoxin_subgr.
IPR011900. GRX_bact.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF00462. Glutaredoxin. 1 hit.
[Graphical view]
PRINTSiPR00160. GLUTAREDOXIN.
SUPFAMiSSF52833. SSF52833. 1 hit.
TIGRFAMsiTIGR02181. GRX_bact. 1 hit.
PROSITEiPS00195. GLUTAREDOXIN_1. 1 hit.
PS51354. GLUTAREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Analysis of the Escherichia coli genome. V. DNA sequence of the region from 76.0 to 81.5 minutes."
    Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R.
    Nucleic Acids Res. 22:2576-2586(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. "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.
  4. "Glutaredoxin-3 from Escherichia coli. Amino acid sequence, 1H AND 15N NMR assignments, and structural analysis."
    Aaslund F., Nordstrand K., Berndt K.D., Nikkola M., Bergman T., Ponsting H., Joernvall H., Otting G., Holmgren A.
    J. Biol. Chem. 271:6736-6745(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-83.
  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 2-21, CHARACTERIZATION.
  6. "NMR structure of Escherichia coli glutaredoxin 3-glutathione mixed disulfide complex: implications for the enzymatic mechanism."
    Nordstrand K., Aaslund F., Holmgren A., Otting G., Berndt K.D.
    J. Mol. Biol. 286:541-552(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.
  7. "NMR structure of oxidized glutaredoxin 3 from Escherichia coli."
    Nordstrand K., Sandstroem A., Aaslund F., Holmgren A., Otting G., Berndt K.D.
    J. Mol. Biol. 303:423-432(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.

Entry informationi

Entry nameiGLRX3_ECOLI
AccessioniPrimary (citable) accession number: P0AC62
Secondary accession number(s): P37687, Q2M7S4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: January 23, 2007
Last modified: March 16, 2016
This is version 86 of the entry and version 2 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.