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Information on EC 1.17.4.1 - ribonucleoside-diphosphate reductase and Organism(s) Arabidopsis thaliana and UniProt Accession Q9LSD0

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EC Tree
IUBMB Comments
This enzyme is responsible for the de novo conversion of ribonucleoside diphosphates into deoxyribonucleoside diphosphates, which are essential for DNA synthesis and repair. There are three types of this enzyme differing in their cofactors. Class Ia enzymes contain a diiron(III)-tyrosyl radical, class Ib enzymes contain a dimanganese-tyrosyl radical, and class II enzymes contain adenosylcobalamin. In all cases the cofactors are involved in generation of a transient thiyl (sulfanyl) radical on a cysteine residue, which attacks the substrate, forming a ribonucleotide 3'-radical, followed by water loss to form a ketyl (alpha-oxoalkyl) radical. The ketyl radical is reduced to 3'-keto-deoxynucleotide concomitant with formation of a disulfide anion radical between two cysteine residues. A proton-coupled electron-transfer from the disulfide radical to the substrate generates a 3'-deoxynucleotide radical, and the final product is formed when the hydrogen atom that was initially removed from the 3'-position of the nucleotide by the thiyl radical is returned to the same position. The disulfide bridge is reduced by the action of thioredoxin. cf. EC 1.1.98.6, ribonucleoside-triphosphate reductase (formate) and EC 1.17.4.2, ribonucleoside-triphosphate reductase (thioredoxin).
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Arabidopsis thaliana
UNIPROT: Q9LSD0
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Word Map
The taxonomic range for the selected organisms is: Arabidopsis thaliana
The enzyme appears in selected viruses and cellular organisms
Synonyms
ribonucleoside diphosphate reductase, cdp reductase, class i rnr, class i ribonucleotide reductase, class ia rnr, ribonucleoside-diphosphate reductase, class ia ribonucleotide reductase, adp reductase, p53-inducible ribonucleotide reductase, class ic ribonucleotide reductase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ribonucleotide reductase
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2'-deoxyribonucleoside-diphosphate:oxidized-thioredoxin 2'-oxidoreductase
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ADP reductase
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CDP reductase
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nucleoside diphosphate reductase
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reductase, ribonucleoside diphosphate
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ribonucleoside 5'-diphosphate reductase
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ribonucleoside diphosphate reductase
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ribonucleotide diphosphate reductase
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ribonucleotide reductase
UDP reductase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
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oxidation
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reduction
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SYSTEMATIC NAME
IUBMB Comments
2'-deoxyribonucleoside-5'-diphosphate:thioredoxin-disulfide 2'-oxidoreductase
This enzyme is responsible for the de novo conversion of ribonucleoside diphosphates into deoxyribonucleoside diphosphates, which are essential for DNA synthesis and repair. There are three types of this enzyme differing in their cofactors. Class Ia enzymes contain a diiron(III)-tyrosyl radical, class Ib enzymes contain a dimanganese-tyrosyl radical, and class II enzymes contain adenosylcobalamin. In all cases the cofactors are involved in generation of a transient thiyl (sulfanyl) radical on a cysteine residue, which attacks the substrate, forming a ribonucleotide 3'-radical, followed by water loss to form a ketyl (alpha-oxoalkyl) radical. The ketyl radical is reduced to 3'-keto-deoxynucleotide concomitant with formation of a disulfide anion radical between two cysteine residues. A proton-coupled electron-transfer from the disulfide radical to the substrate generates a 3'-deoxynucleotide radical, and the final product is formed when the hydrogen atom that was initially removed from the 3'-position of the nucleotide by the thiyl radical is returned to the same position. The disulfide bridge is reduced by the action of thioredoxin. cf. EC 1.1.98.6, ribonucleoside-triphosphate reductase (formate) and EC 1.17.4.2, ribonucleoside-triphosphate reductase (thioredoxin).
CAS REGISTRY NUMBER
COMMENTARY hide
9047-64-7
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
additional information
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
small subunit C, TSO2; var. Columbia, ecotype Columbia-0, three AtRNR2-like catalytic subunit genes AtTSO2, AtRNR2A, and AtRNR2B
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
RNR is an essential enzyme that provides dNTPs for DNA replication and repair, TSO2 and E2Fa are likely required for the DNA damage response. Individual RNR2-like catalytic subunit genes participate in unique aspects of the cellular response to DNA damage in Arabidopsis thaliana
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
RIR2C_ARATH
332
0
38034
Swiss-Prot
other Location (Reliability: 2)
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
morme
AtRNR2B induction is abolished in the rad9-rad17 double mutant, transgenic plant phenotypes, overview
additional information
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression analysis of the AtRNR2-like catalytic subunit gene TSO2, phylogenetic analysis. Transcriptional changes of 17-days-old Arabidopsis plants, enriched in S-phase cells over younger seedlings, in response to the replication-blocking agent hydroxyurea and to the DNA double-strand break inducer bleomycin
expression analysis of AtRNR2-like catalytic subunit gene AtRNR2A, phylogenetic analysis. Transcriptional changes of 17-days-old Arabidopsis plants, enriched in S-phase cells over younger seedlings, in response to the replication-blocking agent hydroxyurea and to the DNA double-strand break inducer bleomycin
expression analysis of AtRNR2-like catalytic subunit gene AtRNR2B, phylogenetic analysis. Transcriptional changes of 17-days-old Arabidopsis plants, enriched in S-phase cells over younger seedlings, in response to the replication-blocking agent hydroxyurea and to the DNA double-strand break inducer bleomycin
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Roa, H.; Lang, J.; Culligan, K.M.; Keller, M.; Holec, S.; Cognat, V.; Montane, M.H.; Houlne, G.; Chaboute, M.E.
Ribonucleotide reductase regulation in response to genotoxic stress in Arabidopsis
Plant Physiol.
151
461-471
2009
Arabidopsis thaliana (P0DKH2), Arabidopsis thaliana (P50651), Arabidopsis thaliana (Q9LSD0)
Manually annotated by BRENDA team