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PEC Original Annotations
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Essentiality
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Class
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essential
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References (PMID)
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J Bacteriol. 1987;169(1):14-8.
Characterization of the ftsB gene as an allele of the nrdB gene in Escherichia coli.
Kren B, Fuchs JA.
(
3025167
)
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Deletion
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OCL68,69-10 (BK9-6 / AK7-6)
(D)
,
OCL68,69-9 (BK9-6 / AK6-6)
(D)
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Related gene (W3110 PEC)
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Gene Search
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Search MG1655 PEC by gene name:
nrdB
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Related strains
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Strains Search
|
Search strains by gene name:
nrdB
Search strains by all related name:
nrdB b2235 ECK2227 ftsB JW2229
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General information (Go to Linear View: )
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Gene Name
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nrdB
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Alternative name
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b2235,ECK2227,ftsB,JW2229
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Location, Length
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2,345,406 - 2,346,536
(
+
)
;
50.55
min
;
1131
(bp) ,
376
(aa)
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Product
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ribonucleoside-diphosphate reductase 1, beta subunit, ferritin-like protein
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Operon Name
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nrdAB
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Note
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ribonucleoside-diphosphate reductase 1, beta subunit, B2; GO_process: GO:0015949 - nucleobase, nucleoside and nucleotide interconversion
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Function
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enzyme; 2'-Deoxyribonucleotide metabolism
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Gene Ontology
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GO:0004748
;
ribonucleoside-diphosphate reductase activity ( nrdB )
GO:0005506
;
iron ion binding ( nrdB )
GO:0005515
;
protein binding ( nrdB )
GO:0005886
;
plasma membrane ( ftsB )
GO:0006260
;
DNA replication ( nrdB )
GO:0007049
;
cell cycle ( ftsB )
GO:0009186
;
deoxyribonucleoside diphosphate metabolic process ( nrdB )
GO:0016020
;
membrane ( ftsB )
GO:0016021
;
integral to membrane ( ftsB )
GO:0016491
;
oxidoreductase activity ( nrdB )
GO:0046872
;
metal ion binding ( nrdB )
GO:0046914
;
transition metal ion binding ( nrdB )
GO:0051301
;
cell division ( ftsB )
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PID
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1788567
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EC number
(KEGG Pathway)
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1.17.4.1
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Verified Protein Starts
(data
compiled from literature and appropriate citations are available from EcoGene)
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EcoGene
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nrdB
(
EG10661
)
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Number of removed
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1 aa cleaved
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SWISS-PROT
(
Show details
[
1
more]
)
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Entry name(Acc.no)
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RIR2_ECOLI
(
P00453
)
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- Protein name
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Ribonucleoside-diphosphate reductase 1 beta chain
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- Synonyms
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EC 1.17.4.1, Ribonucleotide reductase 1, B2 protein, R2 protein
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- Gene name
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Name=nrdB; Synonyms=ftsB; OrderedLocusNames=b2235, z3491, ECs3118;
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MMBR References
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J Bacteriol. 1978;135(2):429-35.
Regulation of the synthesis of ribonucleoside diphosphate reductase in Escherichia coli: specific activity of the enzyme in relationship to perturbations of DNA replication.
Filpula D, Fuchs JA.
(
355225
)
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J Bacteriol. 1977;130(1):107-13.
Regulation of ribonucleoside diphosphate reductase synthesis in Escherichia coli: increased enzyme synthesis as a result of inhibition of deoxyribonucleic acid synthesis.
Filpula D, Fuchs JA.
(
67110
)
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J Bacteriol. 1976;128(3):810-4.
Mapping of nrdA and nrdB in Escherichia coli K-12.
Fuchs JA, Karlstrom HO.
(
791934
)
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J Bacteriol. 1990;172(5):2336-42.
Identification of a second promoter for the metY-nusA-infB operon of Escherichia coli.
Granston AE, Thompson DL, Friedman DI.
(
1692017
)
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J Bacteriol. 1983;154(3):1040-5.
Regulation of ribonucleoside diphosphate reductase mRNA synthesis in Escherichia coli.
Hanke PD, Fuchs JA.
(
6189817
)
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J Bacteriol. 1987;169(1):14-8.
Characterization of the ftsB gene as an allele of the nrdB gene in Escherichia coli.
Kren B, Fuchs JA.
(
3025167
)
|
J Bacteriol. 1980;143(2):561-8.
Construction and characterization of hybrid plasmids containing the Escherichia coli nrd region.
Platz A, Sjoberg BM.
(
7009552
)
|
J Bacteriol. 1986;165(2):363-6.
Cloning, overproduction, and purification of the B2 subunit of ribonucleoside-diphosphate reductase.
Salowe SP, Stubbe J.
(
3511029
)
|
Mol Biol Cell 1992;3:1095-1105
Escherichia coli ribonucleotide reductase expression in cell cycle regulated.
Sun, L., and J. A. Fuchs.
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J Bacteriol. 1987;169(1):19-25.
Genetic and morphological characterization of ftsB and nrdB mutants of Escherichia coli.
Taschner PE, Verest JG, Woldringh CL.
(
3098730
)
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J Bacteriol. 1990;172(4):1711-8.
Regulation of the operon encoding ribonucleotide reductase: role of the negative sites in nrd repression.
Tuggle CK, Fuchs JA.
(
2180902
)
|
Gene. 1982;18(3):309-18.
Physical map of the nrdA-nrdB-ftsB-glpT region of the chromosomal DNA of Escherichia coli.
Yamada M, Takeda Y, Okamoto K, Hirota Y.
(
6290334
)
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Proc Natl Acad Sci U S A. 1984;81:4294-4297
Primary structure of the Escherichia coli ribonucleoside diphosphate reductase operon.
Carlson, J., J. A. Fuchs, and J. Messing.
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| Sequences |
Amino acid
FASTA format
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0001 MAYTTFSQTK NDQLKEPMFF GQPVNVARYD QQKYDIFEKL IEKQLSFFWR PEEVDVSRDR IDYQALPEHE
0071 KHIFISNLKY QTLLDSIQGR SPNVALLPLI SIPELETWVE TWAFSETIHS RSYTHIIRNI VNDPSVVFDD
0141 IVTNEQIQKR AEGISSYYDE LIEMTSYWHL LGEGTHTVNG KTVTVSLREL KKKLYLCLMS VNALEAIRFY
0211 VSFACSFAFA ERELMEGNAK IIRLIARDEA LHLTGTQHML NLLRSGADDP EMAEIAEECK QECYDLFVQA
0281 AQQEKDWADY LFRDGSMIGL NKDILCQYVE YITNIRMQAV GLDLPFQTRS NPIPWINTWL VSDNVQVAPQ
0351 EVEVSSYLVG QIDSEVDTDD LSNFQL
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Nucleotide
FASTA format
View sequence out neighbor 100bp
|
-100 TCGGATTTGT AGGCCTGATA AGACGCGCCA
-070 GCGTCGCATC AGGCACAGGA TGCGGCGTAA AATGCCTTAT CCGGCATTAA ACTCCCAACA GGACACACTC
0001 atggcatata ccaccttttc acagacgaaa aatgatcagc tcaaagaacc gatgttcttt ggtcagccgg
0071 tcaacgtggc tcgctacgat cagcaaaaat atgacatctt cgaaaagctg atcgaaaagc agctctcttt
0141 cttctggcgt ccggaagaag ttgacgtctc ccgcgaccgt atagattacc aggcgctgcc ggagcacgaa
0211 aaacacatct ttatcagcaa cctgaaatat cagacgctgc tggattccat tcagggtcgt agcccgaacg
0281 tggcgctatt gccgcttatt tctattccgg aactggaaac ctgggtcgaa acctgggcgt tctcagaaac
0351 gattcattcc cgttcctata ctcatatcat tcgtaatatc gttaacgatc cgtctgttgt gtttgacgat
0421 atcgtcacca acgagcagat ccagaaacgt gcggaaggga tctccagcta ttacgatgag ctgatcgaaa
0491 tgaccagcta ctggcatctg ctgggcgaag gtacccacac cgttaacggt aaaactgtga ccgttagcct
0561 gcgcgagctg aagaaaaaac tgtatctctg cctgatgagc gttaacgcgc tggaagcgat tcgtttctac
0631 gtcagctttg cttgttcctt cgcatttgca gaacgcgaat tgatggaagg caacgccaaa attattcgcc
0701 tgattgcccg cgacgaagcc ctgcacctga ccggcaccca gcatatgctg aatctgctgc gcagcggcgc
0771 ggacgatcct gagatggcgg aaattgccga agagtgtaag caggagtgct atgacctgtt tgttcaggca
0841 gctcaacagg agaaagactg ggcggattat ctgttccgcg acggttcgat gattggtctg aataaagaca
0911 ttctctgcca gtacgttgaa tacatcacca atatccgtat gcaggcagtc ggtttggatc tgccgttcca
0981 gacgcgctcc aacccgatcc cgtggatcaa cacttggctg gtgtctgata acgtgcaggt tgctccgcag
1051 gaagtggaag tcagttctta tctggtcggg cagattgact cggaagtgga caccgacgat ttgagtaact
1121 tccagctctg aTGGCCCGCG TTACCCTGCG CATCACTGGC ACACAACTGC TGTGCCAGGA TGAACACCCT
1191 TCCCTTCTGG CGGCGCTGGA ATCCCACAAT GTGGCGGTTG A
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