Skip Header

 
Contribute Send feedback
Read comments (1) or add your own

Reviewed, UniProtKB/Swiss-Prot P07071 (NRDD_BPT4)

Last modified June 16, 2009. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Hide | Top

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)
Taxonomic identifier10665 [NCBI]
Taxonomic lineageViruses › dsDNA viruses, no RNA stage › Caudovirales › Myoviridae › T4-like viruses
Virus hostEscherichia coli [TaxID: 562]

Hide | Top

Protein attributes

Sequence length605 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

Hide | Top

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.

Hide | Top

Ontologies

Keywords
   LigandMetal-binding
Zinc
   Molecular functionOxidoreductase
   PTMOrganic radical
   Technical term3D-structure
Gene Ontology (GO)
   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionribonucleoside-triphosphate reductase activity

Inferred from electronic annotation. Source: EC

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Hide | Top

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

1 ..................................................................................... 605
Helix Strand Turn

Details...

Hide | Top

Sequences

Sequence LengthMass (Da)Tools
P07071-1 [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

Hide | Top

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: 3575111] [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: 12626685] [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: 2974005] [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: 1938898] [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: 8421692] [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: 8051113] [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: 8702830] [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: 10066165] [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: 12655046] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS).
+Additional computationally mapped references.

Hide | Top

Cross-references

Sequence databases

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.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1H78X-ray2.50A1-605[»]
1H79X-ray2.90A1-605[»]
1H7AX-ray2.75A1-605[»]
1H7BX-ray2.45A1-605[»]
1HK8X-ray2.45A1-605[»]
ModBaseSearch...

Genome annotation databases

GeneID1258655.
GenomeReviewsGene locus T4p077 in contig AF158101_GR.

Enzyme and pathway databases

BRENDA1.17.4.2. 1108.

Family and domain databases

InterProIPR001150. Form_AcTrfase_GR.
IPR019777. Form_AcTrfase_GR_CS.
IPR012833. NrdD.
[Graphical view]
PfamPF01228. Gly_radical. 1 hit.
[Graphical view]
TIGRFAMsTIGR02487. NrdD. 1 hit.
PROSITEPS00850. GLY_RADICAL_1. 1 hit.
PS51149. GLY_RADICAL_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Hide | Top

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: June 16, 2009
This is version 81 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectVirus (Virus annotation project)

Hide | Top

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents