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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.
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.
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...

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: September 7, 2016
This is version 87 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.