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Protein

Glutaredoxin

Gene

NRDC

Organism
Enterobacteria phage T4 (Bacteriophage T4)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Serves as a reducing agent for the phage-induced ribonucleotide reductase, but not for the bacterial ones. This specificity may be the result of sequence differences around the redox-active disulfide bond. The oxidized form accepts electrons from bacterial glutathione and will, in turn, reduce other small disulfides. Can also be reduced by NADPH and by bacterial thioredoxin reductase.1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Deoxyribonucleotide synthesis, Electron transport, Transport

Keywords - Ligandi

NADP

Names & Taxonomyi

Protein namesi
Recommended name:
Glutaredoxin
Alternative name(s):
Thioredoxin
Gene namesi
Name:NRDC
OrganismiEnterobacteria phage T4 (Bacteriophage T4)
Taxonomic identifieri10665 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stageCaudoviralesMyoviridaeTevenvirinaeT4likevirus
Virus hostiEscherichia coli [TaxID: 562]
Proteomesi
  • UP000009087 Componenti: Genome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi12H → S: 70% loss of ability to be reduced by thioredoxin reductase. 1 Publication1
Mutagenesisi13K → S: 85% loss of ability to be reduced by thioredoxin reductase. 1 Publication1
Mutagenesisi15V → G: Almost no effect. 1 Publication1
Mutagenesisi15V → P: Almost no effect. 55% loss of ability to be reduced by thioredoxin reductase; when associated with P-16. 1 Publication1
Mutagenesisi16Y → A: 20% loss of ability to be reduced by thioredoxin reductase. 1 Publication1
Mutagenesisi21K → Q: Complete loss of ability to be reduced by thioredoxin reductase. 1 Publication1
Mutagenesisi66P → A: 30% loss of ability to be reduced by thioredoxin reductase. 1 Publication1
Mutagenesisi80D → S: Increased ability to be reduced by thioredoxin reductase. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001416491 – 87GlutaredoxinAdd BLAST87

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi14 ↔ 17Redox-active1 Publication

Keywords - PTMi

Disulfide bond

Structurei

Secondary structure

187
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 6Combined sources5
Turni9 – 11Combined sources3
Helixi15 – 26Combined sources12
Beta strandi31 – 36Combined sources6
Beta strandi38 – 42Combined sources5
Helixi45 – 55Combined sources11
Beta strandi67 – 69Combined sources3
Turni71 – 73Combined sources3
Beta strandi75 – 78Combined sources4
Helixi79 – 85Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AAZX-ray2.00A/B1-87[»]
1ABAX-ray1.45A1-87[»]
1DE1NMR-A1-87[»]
1DE2NMR-A1-87[»]
ProteinModelPortaliP00276.
SMRiP00276.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00276.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 87GlutaredoxinPROSITE-ProRule annotationAdd BLAST87

Sequence similaritiesi

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

Keywords - Domaini

Redox-active center

Phylogenomic databases

KOiK03676.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR011767. GLR_AS.
IPR002109. Glutaredoxin.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF00462. Glutaredoxin. 1 hit.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 1 hit.
PROSITEiPS00195. GLUTAREDOXIN_1. 1 hit.
PS51354. GLUTAREDOXIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P00276-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFKVYGYDSN IHKCVYCDNA KRLLTVKKQP FEFINIMPEK GVFDDEKIAE
60 70 80
LLTKLGRDTQ IGLTMPQVFA PDGSHIGGFD QLREYFK
Length:87
Mass (Da):10,050
Last modified:July 21, 1986 - v1
Checksum:i7CBB775323D1B4CE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M13894 Genomic DNA. Translation: AAA32529.1.
Y00122 Genomic DNA. No translation available.
AF158101 Genomic DNA. Translation: AAD42626.1.
PIRiA00282. TXBPT4.
RefSeqiNP_049698.1. NC_000866.4.

Genome annotation databases

GeneIDi1258540.
KEGGivg:1258540.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M13894 Genomic DNA. Translation: AAA32529.1.
Y00122 Genomic DNA. No translation available.
AF158101 Genomic DNA. Translation: AAD42626.1.
PIRiA00282. TXBPT4.
RefSeqiNP_049698.1. NC_000866.4.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AAZX-ray2.00A/B1-87[»]
1ABAX-ray1.45A1-87[»]
1DE1NMR-A1-87[»]
1DE2NMR-A1-87[»]
ProteinModelPortaliP00276.
SMRiP00276.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi1258540.
KEGGivg:1258540.

Phylogenomic databases

KOiK03676.

Miscellaneous databases

EvolutionaryTraceiP00276.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR011767. GLR_AS.
IPR002109. Glutaredoxin.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF00462. Glutaredoxin. 1 hit.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 1 hit.
PROSITEiPS00195. GLUTAREDOXIN_1. 1 hit.
PS51354. GLUTAREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiGLRX_BPT4
AccessioniPrimary (citable) accession number: P00276
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: November 30, 2016
This is version 111 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Miscellaneous

The disulfide bond functions as an electron carrier in the synthesis of deoxyribonucleotides from the corresponding ribonucleotide.

Caution

As it can also be reduced by thioredoxin reductase, it is also known as thioredoxin.Curated

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.