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UniProtKB/Swiss-Prot entry P07071


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name NRDD_BPT4
Primary accession number P07071
Secondary accession numbers P07073 Q38428 Q9T0V5
Integrated into Swiss-Prot on April 1, 1988
Sequence was last modified on January 23, 2002 (Sequence version 4)
Annotations were last modified on    November 4, 2008 (Entry version 77)
Name and origin of the protein
Protein name Anaerobic ribonucleoside-triphosphate reductase
Synonym EC 1.17.4.2
Gene name
Name: NRDD
Synonyms: 49.1, 55.11/55.13, SUNY
From
Enterobacteria phage T4 (Bacteriophage T4) [TaxID: 10665] 
Taxonomy Viruses; dsDNA viruses, no RNA stage; Caudovirales; Myoviridae; T4-like viruses.
Virus host Escherichia coli [TaxID: 562]
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=C;
DOI=10.1093/nar/15.8.3632; PubMed=3575111 [NCBI, ExPASy, EBI, Israel, Japan]
Tomaschewski J., Rueger W.;
"Nucleotide sequence and primary structures of gene products coded for by the T4 genome between map positions 48.266 kb and 39.166 kb.";
Nucleic Acids Res. 15:3632-3633(1987).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1128/MMBR.67.1.86-156.2003; PubMed=12626685 [NCBI, ExPASy, EBI, Israel, Japan]
Miller E.S., Kutter E., Mosig G., Arisaka F., Kunisawa T., Ruger W.;
"Bacteriophage T4 genome.";
Microbiol. Mol. Biol. Rev. 67:86-156(2003).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-181.
PubMed=2974005 [NCBI, ExPASy, EBI, Israel, Japan]
Barth K.A., Powell D., Trupin M., Mosig G.;
"Regulation of two nested proteins from gene 49 (recombination endonuclease VII) and of a lambda RexA-like protein of bacteriophage T4.";
Genetics 120:329-343(1988).
[4]
IDENTIFICATION.
PubMed=1938898 [NCBI, ExPASy, EBI, Israel, Japan]
Zeh A., Shub D.A.;
"The product of the split sunY gene of bacteriophage T4 is a processed protein.";
J. Bacteriol. 173:6980-6985(1991).
[5]
POSSIBLE FUNCTION.
PubMed=8421692 [NCBI, ExPASy, EBI, Israel, Japan]
Sun X., Harder J., Krook M., Joernvall H., Sjoeberg B.-M., Reichard P.;
"A possible glycine radical in anaerobic ribonucleotide reductase from Escherichia coli: nucleotide sequence of the cloned nrdD gene.";
Proc. Natl. Acad. Sci. U.S.A. 90:577-581(1993).
[6]
CHARACTERIZATION.
PubMed=8051113 [NCBI, ExPASy, EBI, Israel, Japan]
Young P., Oehman M., Xu M.Q., Shub D.A., Sjoeberg B.-M.;
"Intron-containing T4 bacteriophage gene sunY encodes an anaerobic ribonucleotide reductase.";
J. Biol. Chem. 269:20229-20232(1994).
[7]
CHARACTERIZATION.
DOI=10.1074/jbc.271.34.20770; PubMed=8702830 [NCBI, ExPASy, EBI, Israel, Japan]
Young P., Andersson J., Sahlin M., Sjoeberg B.-M.;
"Bacteriophage T4 anaerobic ribonucleotide reductase contains a stable glycyl radical at position 580.";
J. Biol. Chem. 271:20770-20775(1996).
[8]
X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS).
DOI=10.1126/science.283.5407.1499; PubMed=10066165 [NCBI, ExPASy, EBI, Israel, Japan]
Logan D.T., Andersson J., Sjoeberg B.-M., Nordlund P.;
"A glycyl radical site in the crystal structure of a class III ribonucleotide reductase.";
Science 283:1499-1504(1999).
[9]
X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS).
DOI=10.1073/pnas.0736456100; PubMed=12655046 [NCBI, ExPASy, EBI, Israel, Japan]
Logan D.T., Mulliez E., Larsson K.-M., Bodevin S., Atta M., Garnaud P.E., Sjoeberg B.-M., Fontecave M.;
"A metal-binding site in the catalytic subunit of anaerobic ribonucleotide reductase.";
Proc. Natl. Acad. Sci. U.S.A. 100:3826-3831(2003).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
Y00122; CAA68308.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Y00122; CAA68310.1; ALT_SEQ; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF158101; AAD42633.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X12629; CAA31150.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR E29284; Z6BPT9.
S01907; Z4BPT9.
RefSeq NP_049690.1; -.
3D structure databases
PDB
1H78; X-ray; 2.50 A; A=1-605.[ExPASy / RCSB / EBI]
1H79; X-ray; 2.90 A; A=1-605.[ExPASy / RCSB / EBI]
1H7A; X-ray; 2.75 A; A=1-605.[ExPASy / RCSB / EBI]
1H7B; X-ray; 2.45 A; A=1-605.[ExPASy / RCSB / EBI]
1HK8; X-ray; 2.45 A; A=1-605.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1H78; -.
1H79; -.
1H7A; -.
1H7B; -.
1HK8; -.
ModBase P07071.
Ontologies
GO
GO:0008270; Molecular function: zinc ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR001150; Form_AcTrfase_GR.
IPR012833; NrdD.
Graphical view of domain structure.
Pfam PF01228; Gly_radical; 1.
Pfam graphical view of domain structure.
TIGRFAMs TIGR02487; NrdD; 1.
PROSITE PS00850; GLY_RADICAL_1; 1.
PS51149; GLY_RADICAL_2; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P07071.
ProtoNet P07071.
Genome annotation databases
GeneID 1258655; -.
GenomeReviews AF158101_GR; T4p077.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Metal-binding; Organic radical; Oxidoreductase; Zinc.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   605  605     Anaerobic ribonucleoside-triphosphate reductase. PRO_0000166686
DOMAIN   482   605  124     Glycine radical. 
METAL   543   543        Zinc. 
METAL   546   546        Zinc. 
METAL   561   561        Zinc. 
METAL   564   564        Zinc. 
MOD_RES   580   580        Glycine radical. 
HELIX   30    49  20      
HELIX   52    59  8      
STRAND   62    65  4      
TURN   66    73  8      
HELIX   84    89  6      
STRAND   92    94  3      
STRAND   97    99  3      
HELIX   105   120  16      
STRAND   123   125  3      
STRAND   127   129  3      
HELIX   132   153  22      
HELIX   159   184  26      
STRAND   195   199  5      
HELIX   205   220  16      
TURN   223   226  4      
STRAND   232   238  7      
TURN   240   243  4      
HELIX   251   264  14      
STRAND   268   271  4      
HELIX   272   279  8      
TURN   289   291  3      
STRAND   310   318  9      
HELIX   319   324  6      
HELIX   334   358  25      
TURN   359   361  3      
HELIX   364   366  3      
HELIX   368   371  4      
HELIX   387   390  4      
TURN   391   394  4      
STRAND   395   402  8      
HELIX   404   411  8      
HELIX   416   434  19      
STRAND   437   442  6      
HELIX   448   460  13      
TURN   464   469  6      
HELIX   486   497  12      
STRAND   506   509  4      
HELIX   517   530  14      
STRAND   532   537  6      
STRAND   540   543  4      
TURN   544   546  3      
STRAND   556   560  5      
STRAND   562   564  3      
HELIX   569   571  3      
STRAND   572   576  5      
STRAND   578   581  4      
Sequence information
Length: 605 AA [This is the length of the unprocessed precursor] Molecular weight: 67957 Da [This is the MW of the unprocessed precursor] CRC64: C5F29CE03126800B [This is a checksum on the sequence]
        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 

P07071 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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