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UniProtKB/Swiss-Prot entry P28903


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

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Entry information
Entry name NRDD_ECOLI
Primary accession number P28903
Secondary accession number Q2M669
Integrated into Swiss-Prot on December 1, 1992
Sequence was last modified on August 29, 2003 (Sequence version 2)
Annotations were last modified on    September 2, 2008 (Entry version 74)
Name and origin of the protein
Protein name Anaerobic ribonucleoside-triphosphate reductase
Synonym EC 1.17.4.2
Gene name
Name: nrdD
OrderedLocusNames: b4238, JW4197
From
Escherichia coli (strain K12) [TaxID: 83333] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
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).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
DOI=10.1093/nar/23.12.2105; PubMed=7610040 [NCBI, ExPASy, EBI, Israel, Japan]
Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.;
"Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes.";
Nucleic Acids Res. 23:2105-2119(1995).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
DOI=10.1126/science.277.5331.1453; PubMed=9278503 [NCBI, ExPASy, EBI, Israel, Japan]
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1474(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan]
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-229.
STRAIN=K12;
PubMed=8083158 [NCBI, ExPASy, EBI, Israel, Japan]
Rimmele M., Boos W.;
"Trehalose-6-phosphate hydrolase of Escherichia coli.";
J. Bacteriol. 176:5654-5664(1994).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 703-712.
STRAIN=K12;
DOI=10.1074/jbc.270.6.2443; PubMed=7852304 [NCBI, ExPASy, EBI, Israel, Japan]
Sun X., Eliasson R., Pontis E., Andersson J., Buist G., Sjoeberg B.-M., Reichard P.;
"Generation of the glycyl radical of the anaerobic Escherichia coli ribonucleotide reductase requires a specific activating enzyme.";
J. Biol. Chem. 270:2443-2446(1995).
[7]
MUTAGENESIS OF CYSTEINE RESIDUES, AND ENZYME ACTIVITY.
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
L06097; AAA24226.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U14003; AAA97135.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC77195.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAE78237.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U06195; AAC43383.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z46865; CAA86938.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A47331; A47331.
RefSeq AP_004736.1; -.
NP_418659.1; -.
3D structure databases
HSSP P07071; 1H78. [HSSP ENTRY / PDB]
ModBase P28903.
Protein-protein interaction databases
IntAct P28903; -.
Enzyme and pathway databases
BioCyc EcoCyc:RIBONUCLEOSIDE-TRIP-REDUCT-MON; -.
MetaCyc:RIBONUCLEOSIDE-TRIP-REDUCT-MON; -.
Organism-specific databases
EchoBASE EB1388; -.
EcoGene EG11417; nrdD.
Ontologies
GO
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
QuickGo view.
Family and domain databases
InterPro IPR005144; ATP-cone.
IPR001150; Form_AcTrfase_GR.
IPR012833; NrdD.
Graphical view of domain structure.
Pfam PF03477; ATP-cone; 1.
PF01228; Gly_radical; 1.
Pfam graphical view of domain structure.
TIGRFAMs TIGR02487; NrdD; 1.
PROSITE PS51161; ATP_CONE; 1.
PS00850; GLY_RADICAL_1; 1.
PS51149; GLY_RADICAL_2; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P28903.
Genome annotation databases
GeneID 948755; -.
GenomeReviews U00096_GR; b4238.
AP009048_GR; JW4197.
KEGG ecj:JW4197; -.
eco:b4238; -.
Phylogenomic databases
HOGENOM P28903; -.
Genome annotation databases
CMR P28903; b4238.
Other
ProtoNet P28903.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
ATP-binding; Complete proteome; Direct protein sequencing; Metal-binding; Nucleotide-binding; Organic radical; Oxidoreductase; Zinc.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   712  712     Anaerobic ribonucleoside-triphosphate reductase. PRO_0000166683
DOMAIN   3    92  90     ATP-cone. 
DOMAIN   583   708  126     Glycine radical. 
METAL   644   644        Zinc. 
METAL   647   647        Zinc. 
METAL   662   662        Zinc. 
METAL   665   665        Zinc. 
MOD_RES   681   681        Glycine radical (By similarity). 
CONFLICT   257   257        G -> R (in Ref. 1; AAA24226). 
CONFLICT   420   420        A -> P (in Ref. 1; AAA24226). 
Sequence information
Length: 712 AA [This is the length of the unprocessed precursor] Molecular weight: 80023 Da [This is the MW of the unprocessed precursor] CRC64: 943589D653EB0C38 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MTPHVMKRDG CKVPFKSERI KEAILRAAKA AEVDDADYCA TVAAVVSEQM QGRNQVDINE 

        70         80         90        100        110        120 
IQTAVENQLM SGPYKQLARA YIEYRHDRDI EREKRGRLNQ EIRGLVEQTN ASLLNENANK 

       130        140        150        160        170        180 
DSKVIPTQRD LLAGIVAKHY ARQHLLPRDV VQAHERGDIH YHDLDYSPFF PMFNCMLIDL 

       190        200        210        220        230        240 
KGMLTQGFKM GNAEIEPPKS ISTATAVTAQ IIAQVASHIY GGTTINRIDE VLAPFVTASY 

       250        260        270        280        290        300 
NKHRKTAEEW NIPDAEGYAN SRTIKECYDA FQSLEYEVNT LHTANGQTPF VTFGFGLGTS 

       310        320        330        340        350        360 
WESRLIQESI LRNRIAGLGK NRKTAVFPKL VFAIRDGLNH KKGDPNYDIK QLALECASKR 

       370        380        390        400        410        420 
MYPDILNYDQ VVKVTGSFKT PMGCRSFLGV WENENGEQIH DGRNNLGVIS LNLPRIALEA 

       430        440        450        460        470        480 
KGDEATFWKL LDERLVLARK ALMTRIARLE GVKARVAPIL YMEGACGVRL NADDDVSEIF 

       490        500        510        520        530        540 
KNGRASISLG YIGIHETINA LFGGEHVYDN EQLRAKGIAI VERLRQAVDQ WKEETGYGFS 

       550        560        570        580        590        600 
LYSTPSENLC DRFCRLDTAE FGVVPGVTDK GYYTNSFHLD VEKKVNPYDK IDFEAPYPPL 

       610        620        630        640        650        660 
ANGGFICYGE YPNIQHNLKA LEDVWDYSYQ HVPYYGTNTP IDECYECGFT GEFECTSKGF 

       670        680        690        700        710 
TCPKCGNHDA SRVSVTRRVC GYLGSPDARP FNAGKQEEVK RRVKHLGNGQ IG 

P28903 in FASTA format

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View entry in raw text format (no links)
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