Ribonucleoside-diphosphate reductase 2 subunit beta (P37146)

Identification
Name:Ribonucleoside-diphosphate reductase 2 subunit beta
Synonyms:
  • R2F protein
  • Ribonucleotide reductase 2
Gene Name:nrdF
Enzyme Class:
Biological Properties
General Function:Involved in oxidoreductase activity
Specific Function:Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. R2F contains the tyrosyl radical required for catalysis
Cellular Location:Not Available
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thioredoxin disulfide+1.0Thumb ↔ 1.0Thioredoxin+1.0Thumb
1.0dADP + 1.0Thioredoxin disulfide + 1.0Water ↔ 1.0Thioredoxin + 1.0ADP
ReactionCard
1.0dUDP+1.0Thioredoxin disulfide+1.0Thumb ↔ 1.0Thioredoxin+1.0Thumb
1.0dUDP + 1.0Thioredoxin disulfide + 1.0Water ↔ 1.0Thioredoxin + 1.0Uridine 5'-diphosphate
ReactionCard
1.0dGDP+1.0Thioredoxin disulfide+1.0Thumb ↔ 1.0Thumb+1.0Thioredoxin
1.0dGDP + 1.0Thioredoxin disulfide + 1.0Water ↔ 1.0Guanosine diphosphate + 1.0Thioredoxin
ReactionCard
1.0Thumb+1.0Thioredoxin disulfide+1.0Thumb ↔ 1.0Thioredoxin+1.0Thumb
1.0dCDP + 1.0Thioredoxin disulfide + 1.0Water ↔ 1.0Thioredoxin + 1.0CDP
ReactionCard
1.02'-Deoxyribonucleoside diphosphate+1.0Thioredoxin disulfide+1.0Thumb ↔ 1.0Ribonucleoside diphosphate+1.0Thumb
1.02'-Deoxyribonucleoside diphosphate + 1.0Thioredoxin disulfide + 1.0Water ↔ 1.0Ribonucleoside diphosphate + 1.0Thioredoxin
ReactionCard
SMPDB Reactions:
1.0Thumb+1.0a reduced NrdH glutaredoxin-like protein → 1.0Thumb+1.0an oxidized NrdH glutaredoxin-like protein+1.0dGDP+1.0Thumb
1.0Guanosine diphosphate + 1.0a reduced NrdH glutaredoxin-like protein → 1.0Water + 1.0an oxidized NrdH glutaredoxin-like protein + 1.0dGDP + 1.0dGDP
ReactionCard
1.0Adenosine diphosphate+1.0a reduced NrdH glutaredoxin-like protein+1.0Thumb → 1.0an oxidized NrdH glutaredoxin-like protein+1.0Thumb+1.0dADP+1.0Thumb
1.0Adenosine diphosphate + 1.0a reduced NrdH glutaredoxin-like protein + 1.0ADP → 1.0an oxidized NrdH glutaredoxin-like protein + 1.0Water + 1.0dADP + 1.0dADP
ReactionCard
1.0Thumb+1.0a reduced NrdH glutaredoxin-like protein → 1.0Thumb+1.0Thumb+1.0an oxidized NrdH glutaredoxin-like protein
1.0CDP + 1.0a reduced NrdH glutaredoxin-like protein → 1.0Water + 1.0dCDP + 1.0an oxidized NrdH glutaredoxin-like protein
ReactionCard
Complex Reactions:
1.0glutaredoxin+1.0Thumb → 1.0Thumb+1.0glutaredoxin+1.0Thumb
1.0glutaredoxin + 1.0Uridine 5'-diphosphate → 1.0dUDP + 1.0glutaredoxin + 1.0Water
ReactionCard
1.0Thumb+1.0glutaredoxin → 1.0Thumb+1.0glutaredoxin+1.0Thumb
1.0Guanosine diphosphate + 1.0glutaredoxin → 1.0dGDP + 1.0glutaredoxin + 1.0Water
ReactionCard
1.0Thumb+1.0glutaredoxin → 1.0Thumb+1.0glutaredoxin+1.0Thumb
1.0CDP + 1.0glutaredoxin → 1.0dCDP + 1.0glutaredoxin + 1.0Water
ReactionCard
1.0Thumb+1.0glutaredoxin → 1.0Thumb+1.0glutaredoxin+1.0Thumb
1.0ADP + 1.0glutaredoxin → 1.0dADP + 1.0glutaredoxin + 1.0Water
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB01341ADPMetaboCard
ECMDB01546CDPMetaboCard
ECMDB21326dADPMetaboCard
ECMDB01245dCDPMetaboCard
ECMDB00960dGDPMetaboCard
ECMDB01000dUDPMetaboCard
ECMDB01201Guanosine diphosphateMetaboCard
ECMDB23749ThioredoxinMetaboCard
ECMDB00295Uridine 5'-diphosphateMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Function
binding
catalytic activity
cation binding
ion binding
metal ion binding
oxidoreductase activity
oxidoreductase activity, acting on CH or CH2 groups
oxidoreductase activity, acting on CH or CH2 groups, disulfide as acceptor
ribonucleoside-diphosphate reductase activity
transition metal ion binding
Process
cellular nitrogen compound metabolic process
deoxyribonucleoside diphosphate metabolic process
metabolic process
nitrogen compound metabolic process
nucleobase, nucleoside and nucleotide metabolic process
nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
nucleoside diphosphate metabolic process
nucleoside phosphate metabolic process
nucleotide metabolic process
oxidation reduction
Gene Properties
Blattner:b2676
Gene OrientationClockwise
Centisome Percentage:60.38
Left Sequence End2801524
Right Sequence End2802483
Gene Sequence:
>960 bp
ATGAGTCTGAATTTCCTTGATTTTGAACAGCCGATTGCAGAGCTGGAAGCGAAAATCGAT
TCTCTGACTGCGGTTAGCCGTCAGGATGAGAAACTGGATATTAACATCGATGAAGAAGTG
CATCGTCTGCGTGAAAAAAGCGTAGAACTGACACGTAAAATCTTCGCCGATCTCGGTGCA
TGGCAGATTGCGCAACTGGCACGCCATCCACAGCGTCCTTATACCCTGGATTACGTTCGC
CTGGCATTTGATGAATTTGACGAACTGGCTGGCGACCGCGCGTATGCAGACGATAAAGCT
ATCGTCGGTGGTATCGCCCGTCTCGATGGTCGTCCGGTGATGATCATTGGTCATCAAAAA
GGTCGTGAAACCAAAGAAAAAATTCGCCGTAACTTTGGTATGCCAGCGCCAGAAGGTTAC
CGCAAAGCACTGCGTCTGATGCAAATGGCTGAACGCTTTAAGATGCCTATCATCACCTTT
ATCGACACCCCGGGGGCTTATCCTGGCGTGGGCGCAGAAGAGCGTGGTCAGTCTGAAGCC
ATTGCACGCAACCTGCGTGAAATGTCTCGCCTCGGCGTACCGGTAGTTTGTACGGTTATC
GGTGAAGGTGGTTCTGGCGGTGCGCTGGCGATTGGCGTGGGCGATAAAGTGAATATGCTG
CAATACAGCACCTATTCCGTTATCTCGCCGGAAGGTTGTGCGTCCATTCTGTGGAAGAGC
GCCGACAAAGCGCCGCTGGCGGCTGAAGCGATGGGTATCATTGCTCCGCGTCTGAAAGAA
CTGAAACTGATCGACTCCATCATCCCGGAACCACTGGGTGGTGCTCACCGTAACCCGGAA
GCGATGGCGGCATCGTTGAAAGCGCAACTGCTGGCGGATCTGGCCGATCTCGACGTGTTA
AGCACTGAAGATTTAAAAAATCGTCGTTATCAGCGCCTGATGAGCTACGGTTACGCGTAA
Protein Properties
Pfam Domain Function:
Protein Residues:319
Protein Molecular Weight:36443
Protein Theoretical pI:4
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Ribonucleoside-diphosphate reductase 2 subunit beta
MKLSRISAINWNKISDDKDLEVWNRLTSNFWLPEKVPLSNDIPAWQTLTVVEQQLTMRVF
TGLTLLDTLQNVIGAPSLMPDALTPHEEAVLSNISFMEAVHARSYSSIFSTLCQTKDVDA
AYAWSEENAPLQRKAQIIQQHYRGDDPLKKKIASVFLESFLFYSGFWLPMYFSSRGKLTN
TADLIRLIIRDEAVHGYYIGYKYQKNMEKISLGQREELKSFAFDLLLELYDNELQYTDEL
YAETPWADDVKAFLCYNANKALMNLGYEPLFPAEMAEVNPAILAALSPNADENHDFFSGS
GSSYVMGKAVETEDEDWNF
References
External Links:
ResourceLink
Uniprot ID:P37146
Uniprot Name:RIR4_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674373
Ecogene ID:EG12381
Ecocyc:EG12381
ColiBase:b2676
Kegg Gene:b2676
EchoBASE ID:EB2283
CCDB:RIR4_ECOLI
BacMap:16130590
General Reference:
  • Blattner, F. R., Plunkett, G. 3rd, 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. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Gowrishankar, J. (1989). "Nucleotide sequence of the osmoregulatory proU operon of Escherichia coli." J Bacteriol 171:1923-1931. Pubmed: 2649479
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Jordan, A., Gibert, I., Barbe, J. (1994). "Cloning and sequencing of the genes from Salmonella typhimurium encoding a new bacterial ribonucleotide reductase." J Bacteriol 176:3420-3427. Pubmed: 8195103
  • 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, a. l. .. (1997). "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 4:91-113. Pubmed: 9205837