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P07071 (NRDD_BPT4) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Anaerobic ribonucleoside-triphosphate reductase

EC=1.17.4.2
Gene names
Name:NRDD
Synonyms:49.1, 55.11/55.13, SUNY
OrganismEnterobacteria phage T4 (Bacteriophage T4) [Reference proteome]
Taxonomic identifier10665 [NCBI]
Taxonomic lineageVirusesdsDNA viruses, no RNA stageCaudoviralesMyoviridaeTevenvirinaeT4likevirus
Virus hostEscherichia coli [TaxID: 562]

Protein attributes

Sequence length605 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

2'-deoxyribonucleoside triphosphate + thioredoxin disulfide + H2O = ribonucleoside triphosphate + thioredoxin.

Subunit structure

Tetramer consisting of 2 alpha (NrdD) and 2 beta (NrdG) subunits.

Induction

Probably by activating enzyme under anaerobic conditions by generation of an organic free radical. Exposure of this activated protein to oxygen may result in cleavage at the glycine residue harboring its organic radical with loss of the 25 C-terminal AA.

Sequence similarities

Belongs to the anaerobic ribonucleoside-triphosphate reductase family.

Contains 1 glycine radical domain.

Ontologies

Keywords
   LigandMetal-binding
Zinc
   Molecular functionOxidoreductase
   PTMOrganic radical
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA replication

Inferred from electronic annotation. Source: InterPro

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

ribonucleoside-triphosphate reductase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 605605Anaerobic ribonucleoside-triphosphate reductase
PRO_0000166686

Regions

Domain482 – 605124Glycine radical

Sites

Metal binding5431Zinc
Metal binding5461Zinc
Metal binding5611Zinc
Metal binding5641Zinc

Amino acid modifications

Modified residue5801Glycine radical

Secondary structure

............................................................................................... 605
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P07071 [UniParc].

Last modified January 23, 2002. Version 4.
Checksum: C5F29CE03126800B

FASTA60567,957
        10         20         30         40         50         60 
MTIEKEIEGL IHKTNKDLLN ENANKDSRVF PTQRDLMAGI VSKHIAKNMV PSFIMKAHES 

        70         80         90        100        110        120 
GIIHVHDIDY SPALPFTNCC LVDLKGMLEN GFKLGNAQIE TPKSIGVATA IMAQITAQVA 

       130        140        150        160        170        180 
SHQYGGTTFA NVDKVLSPYV KRTYAKHIED AEKWQIADAL NYAQSKTEKD VYDAFQAYEY 

       190        200        210        220        230        240 
EVNTLFSSNG QTPFVTITFG TGTDWTERMI QKAILKNRIK GLGRDGITPI FPKLVMFVEE 

       250        260        270        280        290        300 
GVNLYKDDPN YDIKQLALEC ASKRMYPDII SAKNNKAITG SSVPVSPMGC RSFLSVWKDS 

       310        320        330        340        350        360 
TGNEILDGRN NLGVVTLNLP RIALDSYIGT QFNEQKFVEL FNERMDLCFE ALMCRISSLK 

       370        380        390        400        410        420 
GVKATVAPIL YQEGAFGVRL KPDDDIIELF KNGRSSVSLG YIGIHELNIL VGRDIGREIL 

       430        440        450        460        470        480 
TKMNAHLKQW TERTGFAFSL YSTPAENLCY RFCKLDTEKY GSVKDVTDKG WYTNSFHVSV 

       490        500        510        520        530        540 
EENITPFEKI SREAPYHFIA TGGHISYVEL PDMKNNLKGL EAVWDYAAQH LDYFGVNMPV 

       550        560        570        580        590        600 
DKCFTCGSTH EMTPTENGFV CSICGETDPK KMNTIRRTCG YLGNPNERGF NLGKNKEIMH 


RVKHQ 

« Hide

References

« Hide 'large scale' references
[1]"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].
Strain: C.
[2]"Bacteriophage T4 genome."
Miller E.S., Kutter E., Mosig G., Arisaka F., Kunisawa T., Ruger W.
Microbiol. Mol. Biol. Rev. 67:86-156(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"Regulation of two nested proteins from gene 49 (recombination endonuclease VII) and of a lambda RexA-like protein of bacteriophage T4."
Barth K.A., Powell D., Trupin M., Mosig G.
Genetics 120:329-343(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-181.
[4]"The product of the split sunY gene of bacteriophage T4 is a processed protein."
Zeh A., Shub D.A.
J. Bacteriol. 173:6980-6985(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION.
[5]"A possible glycine radical in anaerobic ribonucleotide reductase from Escherichia coli: nucleotide sequence of the cloned nrdD gene."
Sun X., Harder J., Krook M., Joernvall H., Sjoeberg B.-M., Reichard P.
Proc. Natl. Acad. Sci. U.S.A. 90:577-581(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: POSSIBLE FUNCTION.
[6]"Intron-containing T4 bacteriophage gene sunY encodes an anaerobic ribonucleotide reductase."
Young P., Oehman M., Xu M.Q., Shub D.A., Sjoeberg B.-M.
J. Biol. Chem. 269:20229-20232(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[7]"Bacteriophage T4 anaerobic ribonucleotide reductase contains a stable glycyl radical at position 580."
Young P., Andersson J., Sahlin M., Sjoeberg B.-M.
J. Biol. Chem. 271:20770-20775(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[8]"A glycyl radical site in the crystal structure of a class III ribonucleotide reductase."
Logan D.T., Andersson J., Sjoeberg B.-M., Nordlund P.
Science 283:1499-1504(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS).
[9]"A metal-binding site in the catalytic subunit of anaerobic ribonucleotide reductase."
Logan D.T., Mulliez E., Larsson K.-M., Bodevin S., Atta M., Garnaud P.E., Sjoeberg B.-M., Fontecave M.
Proc. Natl. Acad. Sci. U.S.A. 100:3826-3831(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y00122 Genomic DNA. Translation: CAA68308.1.
Y00122 Genomic DNA. Translation: CAA68310.1. Sequence problems.
AF158101 Genomic DNA. Translation: AAD42633.1.
X12629 Genomic DNA. Translation: CAA31150.1.
PIRZ6BPT9. E29284.
Z4BPT9. S01907.
RefSeqNP_049690.1. NC_000866.4.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1H78X-ray2.50A1-605[»]
1H79X-ray2.90A1-605[»]
1H7AX-ray2.75A1-605[»]
1H7BX-ray2.45A1-605[»]
1HK8X-ray2.45A1-605[»]
ProteinModelPortalP07071.
SMRP07071. Positions 27-589.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1258655.

Family and domain databases

InterProIPR019777. Form_AcTrfase_GR_CS.
IPR001150. Gly_radical.
IPR012833. NrdD.
[Graphical view]
TIGRFAMsTIGR02487. NrdD. 1 hit.
PROSITEPS00850. GLY_RADICAL_1. 1 hit.
PS51149. GLY_RADICAL_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP07071.

Entry information

Entry nameNRDD_BPT4
AccessionPrimary (citable) accession number: P07071
Secondary accession number(s): P07073, Q38428, Q9T0V5
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: January 23, 2002
Last modified: May 14, 2014
This is version 103 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references