Ribonucleoside-diphosphate reductase 1 subunit beta

NameRibonucleoside-diphosphate reductase 1 subunit beta
Synonyms
  • 1.17.4.1
  • ftsB
  • Protein B2
  • Protein R2
  • Ribonucleotide reductase 1
Gene NamenrdB
OrganismEscherichia coli (strain K12)
Amino acid sequence
>lcl|BSEQ0012236|Ribonucleoside-diphosphate reductase 1 subunit beta
MAYTTFSQTKNDQLKEPMFFGQPVNVARYDQQKYDIFEKLIEKQLSFFWRPEEVDVSRDR
IDYQALPEHEKHIFISNLKYQTLLDSIQGRSPNVALLPLISIPELETWVETWAFSETIHS
RSYTHIIRNIVNDPSVVFDDIVTNEQIQKRAEGISSYYDELIEMTSYWHLLGEGTHTVNG
KTVTVSLRELKKKLYLCLMSVNALEAIRFYVSFACSFAFAERELMEGNAKIIRLIARDEA
LHLTGTQHMLNLLRSGADDPEMAEIAEECKQECYDLFVQAAQQEKDWADYLFRDGSMIGL
NKDILCQYVEYITNIRMQAVGLDLPFQTRSNPIPWINTWLVSDNVQVAPQEVEVSSYLVG
QIDSEVDTDDLSNFQL
Number of residuesNone
Molecular Weight43516.885
Theoretical pI4.43
GO Classification
Functions
  • iron ion binding
  • identical protein binding
  • ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor
Processes
  • DNA replication
  • deoxyribonucleotide biosynthetic process
  • nucleobase-containing small molecule interconversion
  • deoxyribonucleoside diphosphate metabolic process
Components
  • cytoplasm
  • ribonucleoside-diphosphate reductase complex
  • cytosol
General FunctionRibonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor
Specific FunctionProvides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. R2 contains the tyrosyl radical required for catalysis.
Transmembrane Regions
GenBank Protein ID
UniProtKB IDP69924
UniProtKB Entry Name
Cellular LocationNone
Gene sequence
>lcl|BSEQ0012237|Ribonucleoside-diphosphate reductase 1 subunit beta (nrdB)
ATGGCATATACCACCTTTTCACAGACGAAAAATGATCAGCTCAAAGAACCGATGTTCTTT
GGTCAGCCGGTCAACGTGGCTCGCTACGATCAGCAAAAATATGACATCTTCGAAAAGCTG
ATCGAAAAGCAGCTCTCTTTCTTCTGGCGTCCGGAAGAAGTTGACGTCTCCCGCGACCGT
ATAGATTACCAGGCGCTGCCGGAGCACGAAAAACACATCTTTATCAGCAACCTGAAATAT
CAGACGCTGCTGGATTCCATTCAGGGTCGTAGCCCGAACGTGGCGCTATTGCCGCTTATT
TCTATTCCGGAACTGGAAACCTGGGTCGAAACCTGGGCGTTCTCAGAAACGATTCATTCC
CGTTCCTATACTCATATCATTCGTAATATCGTTAACGATCCGTCTGTTGTGTTTGACGAT
ATCGTCACCAACGAGCAGATCCAGAAACGTGCGGAAGGGATCTCCAGCTATTACGATGAG
CTGATCGAAATGACCAGCTACTGGCATCTGCTGGGCGAAGGTACCCACACCGTTAACGGT
AAAACTGTGACCGTTAGCCTGCGCGAGCTGAAGAAAAAACTGTATCTCTGCCTGATGAGC
GTTAACGCGCTGGAAGCGATTCGTTTCTACGTCAGCTTTGCTTGTTCCTTCGCATTTGCA
GAACGCGAATTGATGGAAGGCAACGCCAAAATTATTCGCCTGATTGCCCGCGACGAAGCC
CTGCACCTGACCGGCACCCAGCATATGCTGAATCTGCTGCGCAGCGGCGCGGACGATCCT
GAGATGGCGGAAATTGCCGAAGAGTGTAAGCAGGAGTGCTATGACCTGTTTGTTCAGGCA
GCTCAACAGGAGAAAGACTGGGCGGATTATCTGTTCCGCGACGGTTCGATGATTGGTCTG
AATAAAGACATTCTCTGCCAGTACGTTGAATACATCACCAATATCCGTATGCAGGCAGTC
GGTTTGGATCTGCCGTTCCAGACGCGCTCCAACCCGATCCCGTGGATCAACACTTGGCTG
GTGTCTGATAACGTGCAGGTTGCTCCGCAGGAAGTGGAAGTCAGTTCTTATCTGGTCGGG
CAGATTGACTCGGAAGTGGACACCGACGATTTGAGTAACTTCCAGCTCTGA
GenBank Gene ID
GeneCard IDNone
GenAtlas ID
HGNC ID
Chromosome LocationNone
LocusNone
References
  1. Carlson J, Fuchs JA, Messing J: Primary structure of the Escherichia coli ribonucleoside diphosphate reductase operon. Proc Natl Acad Sci U S A. 1984 Jul;81(14):4294-7. [6087316 ]
  2. Yamamoto Y, Aiba H, Baba T, Hayashi K, Inada T, Isono K, Itoh T, Kimura S, Kitagawa M, Makino K, Miki T, Mitsuhashi N, Mizobuchi K, Mori H, Nakade S, Nakamura Y, Nashimoto H, Oshima T, Oyama S, Saito N, Sampei G, Satoh Y, Sivasundaram S, Tagami H, Horiuchi T, et al.: Construction of a contiguous 874-kb sequence of the Escherichia coli -K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features. DNA Res. 1997 Apr 28;4(2):91-113. [9205837 ]
  3. Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. [9278503 ]
  4. Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [16738553 ]
  5. Salowe SP, Stubbe J: Cloning, overproduction, and purification of the B2 subunit of ribonucleoside-diphosphate reductase. J Bacteriol. 1986 Feb;165(2):363-6. [3511029 ]
  6. Davies BW, Kohanski MA, Simmons LA, Winkler JA, Collins JJ, Walker GC: Hydroxyurea induces hydroxyl radical-mediated cell death in Escherichia coli. Mol Cell. 2009 Dec 11;36(5):845-60. doi: 10.1016/j.molcel.2009.11.024. [20005847 ]
  7. Nordlund P, Sjoberg BM, Eklund H: Three-dimensional structure of the free radical protein of ribonucleotide reductase. Nature. 1990 Jun 14;345(6276):593-8. [2190093 ]
  8. Nordlund P, Eklund H: Structure and function of the Escherichia coli ribonucleotide reductase protein R2. J Mol Biol. 1993 Jul 5;232(1):123-64. [8331655 ]
  9. Logan DT, Su XD, Aberg A, Regnstrom K, Hajdu J, Eklund H, Nordlund P: Crystal structure of reduced protein R2 of ribonucleotide reductase: the structural basis for oxygen activation at a dinuclear iron site. Structure. 1996 Sep 15;4(9):1053-64. [8805591 ]
  10. Eriksson M, Uhlin U, Ramaswamy S, Ekberg M, Regnstrom K, Sjoberg BM, Eklund H: Binding of allosteric effectors to ribonucleotide reductase protein R1: reduction of active-site cysteines promotes substrate binding. Structure. 1997 Aug 15;5(8):1077-92. [9309223 ]
  11. Tong W, Burdi D, Riggs-Gelasco P, Chen S, Edmondson D, Huynh BH, Stubbe J, Han S, Arvai A, Tainer J: Characterization of Y122F R2 of Escherichia coli ribonucleotide reductase by time-resolved physical biochemical methods and X-ray crystallography. Biochemistry. 1998 Apr 28;37(17):5840-8. [9558317 ]
  12. Logan DT, deMare F, Persson BO, Slaby A, Sjoberg BM, Nordlund P: Crystal structures of two self-hydroxylating ribonucleotide reductase protein R2 mutants: structural basis for the oxygen-insertion step of hydroxylation reactions catalyzed by diiron proteins. Biochemistry. 1998 Jul 28;37(30):10798-807. [9692970 ]
  13. Hogbom M, Andersson ME, Nordlund P: Crystal structures of oxidized dinuclear manganese centres in Mn-substituted class I ribonucleotide reductase from Escherichia coli: carboxylate shifts with implications for O2 activation and radical generation. J Biol Inorg Chem. 2001 Mar;6(3):315-23. [11315567 ]

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