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

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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi12 – 121H → S: 70% loss of ability to be reduced by thioredoxin reductase. 1 Publication
Mutagenesisi13 – 131K → S: 85% loss of ability to be reduced by thioredoxin reductase. 1 Publication
Mutagenesisi15 – 151V → G: Almost no effect. 1 Publication
Mutagenesisi15 – 151V → P: Almost no effect. 55% loss of ability to be reduced by thioredoxin reductase; when associated with P-16. 1 Publication
Mutagenesisi16 – 161Y → A: 20% loss of ability to be reduced by thioredoxin reductase. 1 Publication
Mutagenesisi21 – 211K → Q: Complete loss of ability to be reduced by thioredoxin reductase. 1 Publication
Mutagenesisi66 – 661P → A: 30% loss of ability to be reduced by thioredoxin reductase. 1 Publication
Mutagenesisi80 – 801D → S: Increased ability to be reduced by thioredoxin reductase. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 8787GlutaredoxinPRO_0000141649Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi14 ↔ 17Redox-active1 Publication

Keywords - PTMi

Disulfide bond

Structurei

Secondary structure

1
87
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 65Combined sources
Turni9 – 113Combined sources
Helixi15 – 2612Combined sources
Beta strandi31 – 366Combined sources
Beta strandi38 – 425Combined sources
Helixi45 – 5511Combined sources
Beta strandi67 – 693Combined sources
Turni71 – 733Combined sources
Beta strandi75 – 784Combined sources
Helixi79 – 857Combined sources

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP00276.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 8787GlutaredoxinPROSITE-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

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
EntryMethodResolution (Å)ChainPositionsPDBsum
1AAZX-ray2.00A/B1-87[»]
1ABAX-ray1.45A1-87[»]
1DE1NMR-A1-87[»]
1DE2NMR-A1-87[»]
ProteinModelPortaliP00276.
SMRiP00276. Positions 1-87.
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...

Publicationsi

« Hide 'large scale' publications
  1. "Studies on the structure of T4 thioredoxin. II. Amino acid sequence of the protein and comparison with thioredoxin from Escherichia coli."
    Sjoeberg B.-M., Holmgren A.
    J. Biol. Chem. 247:8063-8068(1972) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE.
  2. "Nucleotide sequence and protein overproduction of bacteriophage T4 thioredoxin."
    Lemaster D.M.
    J. Virol. 59:759-760(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Nucleotide sequence and primary structures of gene products coded for by the T4 genome between map positions 48.266 kb and 39.166 kb."
    Tomaschewski J., Rueger W.
    Nucleic Acids Res. 15:3632-3633(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "Reduction of mutant phage T4 glutaredoxins by Escherichia coli thioredoxin reductase."
    Nikkola M., Gleason F.K., Eklund H.
    J. Biol. Chem. 268:3845-3849(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF HIS-12; LYS-13; VAL-15; TYR-16; LYS-21; PRO-66 AND ASP-80, FUNCTION.
  6. "Three-dimensional structure of thioredoxin induced by bacteriophage T4."
    Soederberg B.-O., Sjoeberg B.-M., Sonnerstam U., Braenden C.-I.
    Proc. Natl. Acad. Sci. U.S.A. 75:5827-5830(1978) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
  7. "Solution structures of reduced and oxidized bacteriophage T4 glutaredoxin."
    Wang Y., Amegbey G., Wishart D.S.
    J. Biomol. NMR 29:85-90(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.

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: June 8, 2016
This is version 108 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.