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Protein

Glutaredoxin

Gene

NRDC

Organism
Enterobacteria phage T4 (Bacteriophage T4)
Status
Reviewed-Annotation score: -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

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

GO - Molecular functioni

GO - Biological processi

Keywordsi

Biological processDeoxyribonucleotide synthesis, Electron transport, Transport
LigandNADP

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 stageCaudoviralesMyoviridaeTevenvirinaeT4virus
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

Keywords - Domaini

Redox-active center

Phylogenomic databases

OrthoDBiVOG090001HH

Family and domain databases

InterProiView protein in InterPro
IPR011767 GLR_AS
IPR002109 Glutaredoxin
IPR036249 Thioredoxin-like_sf
PfamiView protein in Pfam
PF00462 Glutaredoxin, 1 hit
SUPFAMiSSF52833 SSF52833, 1 hit
PROSITEiView protein in PROSITE
PS00195 GLUTAREDOXIN_1, 1 hit
PS51354 GLUTAREDOXIN_2, 1 hit

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

Similar proteinsi

Entry informationi

Entry nameiGLRX_BPT4
AccessioniPrimary (citable) accession number: P00276
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: April 25, 2018
This is version 120 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

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

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