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Search results 301 to 400 out of 463 for Fes

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Type Details Score
Publication
11742080 | -
First Author: Schwartz CJ
Year: 2001
Journal: Proc Natl Acad Sci U S A
Title: IscR, an Fe-S cluster-containing transcription factor, represses expression of Escherichia coli genes encoding Fe-S cluster assembly proteins.
Volume: 98
Issue: 26
Pages: 14895-900
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Publication
12970486 | -
First Author: Maiwald D
Year: 2003
Journal: Plant Physiol
Title: Knock-out of the genes coding for the Rieske protein and the ATP-synthase delta-subunit of Arabidopsis. Effects on photosynthesis, thylakoid protein composition, and nuclear chloroplast gene expression.
Volume: 133
Issue: 1
Pages: 191-202
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Protein Domain
IPR023960 | Cyt_b6_f_Rieske
Type: Family
Description: The plant cytochrome b6f is located in the thylakoid membrane and functions in both linear and cyclic electron transport, providing ATP and NADPH for photosynthetic carbon fixation. The cytochrome b6f complex has eight different subunits, six being encoded in the chloroplast genome (PetA [cyt f], PetB [cyt b6], PetD, PetG, PetL, and PetN) and two in the nucleus (PetC [Rieske FeS]and PetM. The complex functions as a dimer []. In cyanobacteria, the cytochrome b6f complex contains four large subunits, including cytochrome f, cytochrome b6, the Rieske iron-sulfur protein (ISP), and subunit IV; as well as four small hydrophobic subunits, PetG, PetL, PetM, and PetN []. This entry represents the Rieske FeS protein (encoded by the PetC gene) of the cytochrome b6f complex from plants and cyanobacteria. The Rieske subunit acts by binding plastoquinol anion, transferring an electron to the 2Fe-2S cluster, then releasing the electron to thecytochrome f haem iron. The 2Fe-2S cluster is bound in the highly conserved C-terminal region of the Rieske subunit. In plants, Rieske FeS is required for the successful assembly of the b6f complex and is essential for photosynthesis [, ].
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Publication
9933933 | -
First Author: Westenberg DJ
Year: 1999
Journal: FEMS Microbiol Lett
Title: The F420H2-dehydrogenase from Methanolobus tindarius: cloning of the ffd operon and expression of the genes in Escherichia coli.
Volume: 170
Issue: 2
Pages: 389-98
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Protein Domain
IPR002744 | MIP18-like
Type: Domain
Description: This domain (previously known as DUF59) is found in proteins that are mostly defined as members of the MIP18 family. This includes iron-sulfur cluster carrier proteins, where the domain is found in the N terminus. This domain is also found in protein AE7 from Arabidopsis and its homologues. Protein AE7 is thought to be a central member of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) pathway, however protein AE7-like 1 and 2 (also containing this domain) are probably not involved in this pathway []. MIP18 family protein YHR122W (CIA2) from S. cerevisiae is a component of the CIA machinery, and acts at a late step of Fe-S cluster assembly []. The SufT protein from Staphylococcus aureus is composed of this domain solely and is involved in the maturation of FeS proteins [].
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Protein Domain
IPR018288 | F420H2-DH_FpoO
Type: Family
Description: This entry represents the FpoO subunit of membrane-bound multi-subunit F420H2 dehydrogenase, which oxidises the reduced coenzyme F420H2 to coenzyme F420 and feeds the electrons via an FeS cluster into an energy-conserving electron transport chain [, ]. This enzyme plays a role in the methanogenic pathway in methanogenic archaea. Reduced coenzyme F420H2 is the major cytoplasmic electron carrier of methanogens and a reversible hydride donor, much like NADH []. F420H2 + COB-S-S-CoM = F420 + CoM-SH + CoB-SHWhere CoB-S-S-CoM (the heterosulphide of 2-mercaptoethanesulphonate and 7-mercaptoheptanoylthreonine phosphate) is the terminal electron acceptor of the methanogenic pathway, and is reduced with the concomitant generation of a transmembrane proton potential and ATP synthesis. The FpoO subunit of F420H2 dehydrogenase probably participates in the reduction of methanophenazine, where it acts as a special mechanism for the reduction of the methanogenic cofactor [].
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Publication
10649999 | -
First Author: Dai S
Year: 2000
Journal: Science
Title: Redox signaling in chloroplasts: cleavage of disulfides by an iron-sulfur cluster.
Volume: 287
Issue: 5453
Pages: 655-8
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Publication
7628465 | -
First Author: Chow LP
Year: 1995
Journal: Eur J Biochem
Title: Amino acid sequence of spinach ferredoxin:thioredoxin reductase catalytic subunit and identification of thiol groups constituting a redox-active disulfide and a [4Fe-4S] cluster.
Volume: 231
Issue: 1
Pages: 149-56
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Publication
16603772 | -
First Author: Layer G
Year: 2006
Journal: J Biol Chem
Title: Iron-sulfur cluster biosynthesis: characterization of Escherichia coli CYaY as an iron donor for the assembly of [2Fe-2S] clusters in the scaffold IscU.
Volume: 281
Issue: 24
Pages: 16256-63
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Publication
16428423 | -
First Author: Vivas E
Year: 2006
Journal: J Bacteriol
Title: Salmonella enterica strains lacking the frataxin homolog CyaY show defects in Fe-S cluster metabolism in vivo.
Volume: 188
Issue: 3
Pages: 1175-9
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Protein
E9Q2P9
Organism: Mus musculus/domesticus
Length: 145  
Fragment?: false
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Protein
O09111
Organism: Mus musculus/domesticus
Length: 151  
Fragment?: false
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Protein
Q9CQ68
Organism: Mus musculus/domesticus
Length: 150  
Fragment?: false
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Protein
A0A3Q4EC31
Organism: Mus musculus/domesticus
Length: 58  
Fragment?: false
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Protein
A0A3Q4L320
Organism: Mus musculus/domesticus
Length: 46  
Fragment?: false
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Protein
Q9R295
Organism: Mus musculus/domesticus
Length: 84  
Fragment?: true
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Protein
Q9D9S8
Organism: Mus musculus/domesticus
Length: 150  
Fragment?: false
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Protein
A0A3Q4EGA7
Organism: Mus musculus/domesticus
Length: 50  
Fragment?: false
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Protein
Q4VBC9
Organism: Mus musculus/domesticus
Length: 151  
Fragment?: true
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Publication
22976985 | -
First Author: Andersson CS
Year: 2012
Journal: Chem Biodivers
Title: A dynamic C-terminal segment in the Mycobacterium tuberculosis Mn/Fe R2lox protein can adopt a helical structure with possible functional consequences.
Volume: 9
Issue: 9
Pages: 1981-8
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Publication
23104832 | -
First Author: Luo D
Year: 2012
Journal: Plant Cell
Title: The DUF59 family gene AE7 acts in the cytosolic iron-sulfur cluster assembly pathway to maintain nuclear genome integrity in Arabidopsis.
Volume: 24
Issue: 10
Pages: 4135-48
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Publication
11526118 | -
First Author: Andersson J
Year: 2001
Journal: J Biol Chem
Title: Two active site asparagines are essential for the reaction mechanism of the class III anaerobic ribonucleotide reductase from bacteriophage T4.
Volume: 276
Issue: 44
Pages: 40457-63
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Publication
10066165 | -
First Author: Logan DT
Year: 1999
Journal: Science
Title: A glycyl radical site in the crystal structure of a class III ribonucleotide reductase.
Volume: 283
Issue: 5407
Pages: 1499-504
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Publication
12655046 | -
First Author: Logan DT
Year: 2003
Journal: Proc Natl Acad Sci U S A
Title: A metal-binding site in the catalytic subunit of anaerobic ribonucleotide reductase.
Volume: 100
Issue: 7
Pages: 3826-31
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Publication
12381726 | -
First Author: Carroll J
Year: 2002
Journal: J Biol Chem
Title: Definition of the nuclear encoded protein composition of bovine heart mitochondrial complex I. Identification of two new subunits.
Volume: 277
Issue: 52
Pages: 50311-7
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Publication
18563446 | -
First Author: Remacle C
Year: 2008
Journal: Mol Genet Genomics
Title: Eukaryotic complex I: functional diversity and experimental systems to unravel the assembly process.
Volume: 280
Issue: 2
Pages: 93-110
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Publication
17854760 | -
First Author: Vogel RO
Year: 2007
Journal: Biochim Biophys Acta
Title: Human mitochondrial complex I assembly: a dynamic and versatile process.
Volume: 1767
Issue: 10
Pages: 1215-27
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Protein Domain
IPR002908 | Frataxin/CyaY
Type: Family
Description: The eukaryotic proteins in this entry include frataxin, the protein that is mutated in Friedreich's ataxia [], and related sequences. Friedreich's ataxia is a progressive neurodegenerative disorder caused by loss of function mutations in the gene encoding frataxin (FRDA). Frataxin mRNA is predominantly expressed in tissues with a high metabolic rate (including liver, kidney, brown fat and heart). Mouse and yeast frataxin homologues contain a potential N-terminal mitochondrial targeting sequence, and human frataxin has been observed to co-localise with a mitochondrial protein. Furthermore, disruption of the yeast gene has been shown to result in mitochondrial dysfunction. Friedreich's ataxia is thus believed to be a mitochondrial disease caused by a mutation in the nuclear genome (specifically, expansion of an intronic GAA triplet repeat) [, , ].The bacterial proteins in this entry are iron-sulphur cluster (FeS) metabolism CyaY proteins homologous to eukaryotic frataxin. Partial Phylogenetic Profiling []suggests that CyaY most likely functions as part of the ISC system for FeS cluster biosynthesis, and is supported by expermimental data in some species [, ].
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Protein Domain
IPR000358 | RNR_small_fam
Type: Family
Description: Ribonucleotide reductase (RNR), also known as ribonucleoside diphosphate reductase, () [, ]catalyses the reductive synthesisof deoxyribonucleotides from their corresponding ribonucleotides:2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O = ribonucleoside diphosphate + reduced thioredoxinRNR provides the precursors necessary for DNA synthesis. RNRs divide into three classes on the basis of their metallocofactor usage. Class I RNRs, found in eukaryotes, bacteria, bacteriophage and viruses, use adiiron-tyrosyl radical, Class II RNRs, found in bacteria,bacteriophage, algae and archaea, use coenzyme B12(adenosylcobalamin, AdoCbl). Class III RNRs, found inanaerobic bacteria and bacteriophage, use an FeS cluster andS-adenosylmethionine to generate a glycyl radical. Manyorganisms have more than one class of RNR present in theirgenomes. Class I ribonucleotide reductase is an oligomeric enzyme composed of a large subunit (700 to 1000 residues) and a small subunit (300 to 400 residues) - class II RNRs are less complex, using the small molecule B12 in place of the small chain []. The small chain binds two iron atoms [](three Glu, one Asp, and two His areinvolved in metal binding) and contains an active site tyrosine radical. Theregions of the sequence that contain the metal-binding residues and the activesite tyrosine are conserved in ribonucleotide reductase small chain fromprokaryotes, eukaryotes and viruses.This family consist of the small subunit of class I ribonucleotide reductases. It also includes R2-like ligand-binding oxidase, which is homologous to the ribonucleotide reductase small subunit (R2), but whose function is still unknown [, ].
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Protein Domain
IPR036524 | Frataxin/CyaY_sf
Type: Homologous_superfamily
Description: The eukaryotic proteins in this entry include frataxin, the protein that is mutated in Friedreich's ataxia [], and related sequences. Friedreich's ataxia is a progressive neurodegenerative disorder caused by loss of function mutations in the gene encoding frataxin (FRDA). Frataxin mRNA is predominantly expressed in tissues with a high metabolic rate (including liver, kidney, brown fat and heart). Mouse and yeast frataxin homologues contain a potential N-terminal mitochondrial targeting sequence, and human frataxin has been observed to co-localise with a mitochondrial protein. Furthermore, disruption of the yeast gene has been shown to result in mitochondrial dysfunction. Friedreich's ataxia is thus believed to be a mitochondrial disease caused by a mutation in the nuclear genome (specifically, expansion of an intronic GAA triplet repeat) [, , ].The bacterial proteins in this entry are iron-sulphur cluster (FeS) metabolism CyaY proteins homologous to eukaryotic frataxin. Partial Phylogenetic Profiling []suggests that CyaY most likely functions as part of the ISC system for FeS cluster biosynthesis, and is supported by expermimental data in some species [, ]. The structure of Frataxin/CyaY has an α-β(5)-alpha fold arranged in two layers (alpha/beta) with meander antiparallel sheet.
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Protein Domain
IPR012833 | NrdD
Type: Family
Description: This entry represents anaerobic, class III ribonucleotide reductase. The mechanism of the enzyme involves a glycine-centred radical[], a C-terminal zinc binding site [], and a set of conserved active site cysteines and asparagines []. This enzyme requires an activating component, NrdG, a radical-SAM domain containing enzyme (). Together the two form an alpha-2/beta-2 heterodimer.Ribonucleotide reductase (RNR) catalyzes the reductive synthesis of deoxyribonucleotides from their corresponding ribonucleotides. It provides the precursors necessary for DNA synthesis. RNRs are separated into three classes based on their metallocofactor usage. Class I RNRs, found in eukaryotes, bacteria, and bacteriophage, use a diiron-tyrosyl radical. Class II RNRs, found in bacteria, bacteriophage, algae and archaea, use coenzyme B12 (adenosylcobalamin, AdoCbl). Class III RNRs, found in strict or facultative anaerobic bacteria, bacteriophage, and archaea, use an FeS cluster and S-adenosylmethionine to generate a glycyl radical []. Many organisms have more than one class of RNR present in their genomes. All three RNRs have a ten-stranded α-β barrel domain that is structurally similar to the domain of PFL (pyruvate formate lyase) []. The class III enzyme from phage T4 consists of two subunits, this model covers the larger subunit which contains the active and allosteric sites.
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Protein Domain
IPR019329 | NADH_UbQ_OxRdtase_ESSS_su
Type: Family
Description: NADH:ubiquinone oxidoreductase (complex I) () is a respiratory-chain enzyme that catalyses the transfer of two electrons from NADH to ubiquinone in a reaction that is associated with proton translocation across the membrane (NADH + ubiquinone = NAD+ + ubiquinol) []. Complex I is a major source of reactive oxygen species (ROS) that are predominantly formed by electron transfer from FMNH(2). Complex I is found in bacteria, cyanobacteria (as a NADH-plastoquinone oxidoreductase), archaea [], mitochondria, and in the hydrogenosome, a mitochondria-derived organelle. In general, the bacterial complex consists of 14 different subunits, while the mitochondrial complex contains homologues to these subunits in addition to approximately 31 additional proteins [].Mitochondrial complex I, which is located inthe inner mitochondrial membrane, is the largest multimeric respiratory enzyme in the mitochondria, consisting of more than 45 subunits, one FMN co-factor and eight FeS clusters []. The assembly of mitochondrial complex I is an intricate process that requires the cooperation of the nuclear and mitochondrial genomes [, ].This entry represents the ESSS subunit from mitochondrial NADH:ubiquinone oxidoreductase (complex I). It carries mitochondrial import sequences [].
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Protein Domain
IPR020895 | Frataxin_CS
Type: Conserved_site
Description: The eukaryotic proteins in this entry include frataxin, the protein that is mutated in Friedreich's ataxia [], and related sequences. Friedreich's ataxia is a progressive neurodegenerative disorder caused by loss of function mutations in the gene encoding frataxin (FRDA). Frataxin mRNA is predominantly expressed in tissues with a high metabolic rate (including liver, kidney, brown fat and heart). Mouse and yeast frataxin homologues contain a potential N-terminal mitochondrial targeting sequence, and human frataxin has been observed to co-localise with a mitochondrial protein. Furthermore, disruption of the yeast gene has been shown to result in mitochondrial dysfunction. Friedreich's ataxia is thus believed to be a mitochondrial disease caused by a mutation in the nuclear genome (specifically, expansion of an intronic GAA triplet repeat) [, , ].The bacterial proteins in this entry are iron-sulphur cluster (FeS) metabolism CyaY proteins homologous to eukaryotic frataxin. Partial Phylogenetic Profiling []suggests that CyaY most likely functions as part of the ISC system for FeS cluster biosynthesis, and is supported by expermimental data in some species [, ]. This conserved site covers a conserved region in the central section of these proteins.
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Protein
A0A1B0GSB1
Organism: Mus musculus/domesticus
Length: 65  
Fragment?: true
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Publication
28754840 | -
First Author: Simkin AJ
Year: 2017
Journal: Plant Physiol
Title: Overexpression of the RieskeFeS Protein Increases Electron Transport Rates and Biomass Yield.
Volume: 175
Issue: 1
Pages: 134-145
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Publication
19321420 | -
First Author: Andersson CS
Year: 2009
Journal: Proc Natl Acad Sci U S A
Title: A Mycobacterium tuberculosis ligand-binding Mn/Fe protein reveals a new cofactor in a remodeled R2-protein scaffold.
Volume: 106
Issue: 14
Pages: 5633-8
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Publication
23600726 | -
First Author: Kazmierczak BI
Year: 2013
Journal: Mol Microbiol
Title: Spatial and numerical regulation of flagellar biosynthesis in polarly flagellated bacteria.
Volume: 88
Issue: 4
Pages: 655-63
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Protein Domain
IPR039718 | Rrm1
Type: Family
Description: Ribonucleotide reductase (RNR, ) [, ]catalyzes the reductivesynthesis of deoxyribonucleotides from their corresponding ribonucleotides. It provides the precursors necessary for DNA synthesis. RNRs divide into three classes on the basis of their metallocofactor usage. Class I RNRs, found in eukaryotes, bacteria, bacteriophage and viruses, use a diiron-tyrosyl radical, Class II RNRs, found in bacteria, bacteriophage, algae and archaea, use coenzyme B12 (adenosylcobalamin, AdoCbl). Class III RNRs, found in anaerobic bacteria and bacteriophage, use an FeS cluster and S-adenosylmethionine to generate a glycyl radical. Many organisms have more than one class of RNR present in their genomes. Ribonucleotide reductase is an oligomeric enzyme composed of a large subunit (700 to 1000 residues) and a small subunit (300 to 400 residues) - class II RNRs are less complex, using the small molecule B12 in place of the small chain []. The reduction of ribonucleotides to deoxyribonucleotides involves the transfer of free radicals, the function of each metallocofactor is to generate an active site thiyl radical. This thiyl radical then initiates the nucleotide reduction process by hydrogen atom abstraction from the ribonucleotide []. The radical-based reaction involves five cysteines: two of these are located at adjacent anti-parallel strands in a new type of ten-stranded alpha/β-barrel; two others reside at the carboxyl end in a flexible arm; and the fifth, in a loop in the centre of the barrel, is positioned to initiate the radical reaction []. There are several regions of similarity in the sequence of the large chain of prokaryotes, eukaryotes and viruses spread across 3 domains: an N-terminal domain common to the mammalian and bacterial enzymes; a C-terminal domain common to the mammalian and viral ribonucleotide reductases; and a central domain common to all three [].
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Protein Domain
IPR000788 | RNR_lg_C
Type: Domain
Description: Ribonucleotide reductase (RNR, ) [, ]catalyzes the reductivesynthesis of deoxyribonucleotides from their corresponding ribonucleotides. It provides the precursors necessary for DNA synthesis. RNRs divide into three classes on the basis of their metallocofactor usage. Class I RNRs, found in eukaryotes, bacteria, bacteriophage and viruses, use a diiron-tyrosyl radical, Class II RNRs, found in bacteria, bacteriophage, algae and archaea, use coenzyme B12 (adenosylcobalamin, AdoCbl). Class III RNRs, found in anaerobic bacteria and bacteriophage, use an FeS cluster and S-adenosylmethionine to generate a glycyl radical. Many organisms have more than one class of RNR present in their genomes. Ribonucleotide reductase is an oligomeric enzyme composed of a large subunit (700 to 1000 residues) and a small subunit (300 to 400 residues) - class II RNRs are less complex, using the small molecule B12 in place of the small chain []. The reduction of ribonucleotides to deoxyribonucleotides involves the transfer of free radicals, the function of each metallocofactor is to generate an active site thiyl radical. This thiyl radical then initiates the nucleotide reduction process by hydrogen atom abstraction from the ribonucleotide []. The radical-based reaction involves five cysteines: two of these are located at adjacent anti-parallel strands in a new type of ten-stranded alpha/β-barrel; two others reside at the carboxyl end in a flexible arm; and the fifth, in a loop in the centre of the barrel, is positioned to initiate the radical reaction []. There are several regions of similarity in the sequence of the large chain of prokaryotes, eukaryotes and viruses spread across 3 domains: an N-terminal domain common to the mammalian and bacterial enzymes; a C-terminal domain common to the mammalian and viral ribonucleotide reductases; and a central domain common to all three [].
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Protein Domain
IPR034085 | TOG
Type: Domain
Description: XMAP215/Dis1 proteins, such as Alp14 and XMAP215, increase microtubules dynamic polymerization rates by recruiting soluble alpha/beta-tubulin via their conserved TOG domains to polymerizing microtubule plus ends [, ]. A TOG domain contains HEAT repeats.This entry represents a structural domain with an armadillo (ARM)-like fold, consisting of a multi-helical fold comprised of two curved layers of α- helices arranged in a regular right-handed superhelix, where the repeats that make up this structure are arranged about a common axis []. These superhelical structures present an extensive solvent-accessible surface that is well suited to binding large substrates such as proteins and nucleic acids. Domains and repeats with an ARM-like fold have been found in a number of proteins, including:ARM repeat domain, found in beta-catenins, importins, karyopherin and exportins.HEAT repeat domain, found in protein phosphatase 2a and initiation factor eIF4G.PHAT domain, found in the RNA-binding protein Smaug.Leucine-rich repeat variant, which contain an FeS cluster.Pumilio repeat domain, found in Pumilio protein.Regulatory subunit H of V-type ATPases.PBS lyase HEAT-like repeat.Mo25 protein.MIF4G domain-like, found in eukaryotic initiation factor eIF4G, translation initiation factor eIF-2b epsilon and nuclear cap-binding protein CBP80.The N-terminal domain of eukaryotic translation initiation factor 3 subunit 12.The C-terminal domain of leukotriene A4 hydrolase.The helical domain of phosphoinositide 3-kinase.The N-terminal fragment of adaptin alpha-C and beta subunits.The proximal leg segment and the linker domain of the clathrin heavy chain.The sequence similarity among these different repeats or domains is low, however they exhibit considerable structural similarity. Furthermore, the number of repeats present in the superhelical structure can vary between orthologues, indicating that rapid loss/gain of repeats has occurred frequently in evolution. A common phylogenetic origin has been proposed for the armadillo and HEAT repeats [].
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Protein Domain
IPR034716 | HSV_RIR1_betahv
Type: Family
Description: Ribonucleotide reductase (RNR, ) [, ]catalyzes the reductivesynthesis of deoxyribonucleotides from their corresponding ribonucleotides. It provides the precursors necessary for DNA synthesis. RNRs divide into three classes on the basis of their metallocofactor usage. Class I RNRs, found in eukaryotes, bacteria, bacteriophage and viruses, use a diiron-tyrosyl radical, Class II RNRs, found in bacteria, bacteriophage, algae and archaea, use coenzyme B12 (adenosylcobalamin, AdoCbl). Class III RNRs, found in anaerobic bacteria and bacteriophage, use an FeS cluster and S-adenosylmethionine to generate a glycyl radical. Many organisms have more than one class of RNR present in their genomes. Ribonucleotide reductase is an oligomeric enzyme composed of a large subunit (700 to 1000 residues) and a small subunit (300 to 400 residues) - class II RNRs are less complex, using the small molecule B12 in place of the small chain []. The reduction of ribonucleotides to deoxyribonucleotides involves the transfer of free radicals, the function of each metallocofactor is to generate an active site thiyl radical. This thiyl radical then initiates the nucleotide reduction process by hydrogen atom abstraction from the ribonucleotide []. The radical-based reaction involves five cysteines: two of these are located at adjacent anti-parallel strands in a new type of ten-stranded alpha/β-barrel; two others reside at the carboxyl end in a flexible arm; and the fifth, in a loop in the centre of the barrel, is positioned to initiate the radical reaction []. There are several regions of similarity in the sequence of the large chain of prokaryotes, eukaryotes and viruses spread across 3 domains: an N-terminal domain common to the mammalian and bacterial enzymes; a C-terminal domain common to the mammalian and viral ribonucleotide reductases; and a central domain common to all three [].This entry represents the ribonucleotide reductase large subunit from Betaherpesviruses.
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Protein Domain
IPR034717 | HSV_RIR1
Type: Family
Description: Ribonucleotide reductase (RNR, ) [, ]catalyzes the reductivesynthesis of deoxyribonucleotides from their corresponding ribonucleotides. It provides the precursors necessary for DNA synthesis. RNRs divide into three classes on the basis of their metallocofactor usage. Class I RNRs, found in eukaryotes, bacteria, bacteriophage and viruses, use a diiron-tyrosyl radical, Class II RNRs, found in bacteria, bacteriophage, algae and archaea, use coenzyme B12 (adenosylcobalamin, AdoCbl). Class III RNRs, found in anaerobic bacteria and bacteriophage, use an FeS cluster and S-adenosylmethionine to generate a glycyl radical. Many organisms have more than one class of RNR present in their genomes. Ribonucleotide reductase is an oligomeric enzyme composed of a large subunit (700 to 1000 residues) and a small subunit (300 to 400 residues) - class II RNRs are less complex, using the small molecule B12 in place of the small chain []. The reduction of ribonucleotides to deoxyribonucleotides involves the transfer of free radicals, the function of each metallocofactor is to generate an active site thiyl radical. This thiyl radical then initiates the nucleotide reduction process by hydrogen atom abstraction from the ribonucleotide []. The radical-based reaction involves five cysteines: two of these are located at adjacent anti-parallel strands in a new type of ten-stranded alpha/β-barrel; two others reside at thecarboxyl end in a flexible arm; and the fifth, in a loop in the centre of the barrel, is positioned to initiate the radical reaction []. There are several regions of similarity in the sequence of the large chain of prokaryotes, eukaryotes and viruses spread across 3 domains: an N-terminal domain common to the mammalian and bacterial enzymes; a C-terminal domain common to the mammalian and viral ribonucleotide reductases; and a central domain common to all three [].This entry represents the ribonucleotide reductase large subunit from Alphaherpesviruses.
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Protein Domain
IPR013509 | RNR_lsu_N
Type: Domain
Description: Ribonucleotide reductase (RNR, ) [, ]catalyzes the reductivesynthesis of deoxyribonucleotides from their corresponding ribonucleotides. It provides the precursors necessary for DNA synthesis. RNRs divide into three classes on the basis of their metallocofactor usage. Class I RNRs, found in eukaryotes, bacteria, bacteriophage and viruses, use a diiron-tyrosyl radical, Class II RNRs, found in bacteria, bacteriophage, algae and archaea, use coenzyme B12 (adenosylcobalamin, AdoCbl). Class III RNRs, found in anaerobic bacteria and bacteriophage, use an FeS cluster and S-adenosylmethionine to generate a glycyl radical. Many organisms have more than one class of RNR present in their genomes. Ribonucleotide reductase is an oligomeric enzyme composed of a large subunit (700 to 1000 residues) and a small subunit (300 to 400 residues) - class II RNRs are less complex, using the small molecule B12 in place of the small chain []. The reduction of ribonucleotides to deoxyribonucleotides involves the transfer of free radicals, the function of each metallocofactor is to generate an active site thiyl radical. This thiyl radical then initiates the nucleotide reduction process by hydrogen atom abstraction from the ribonucleotide []. The radical-based reaction involves five cysteines: two of these are located at adjacent anti-parallel strands in a new type of ten-stranded alpha/β-barrel; two others reside at the carboxyl end in a flexible arm; and the fifth, in a loop in the centre of the barrel, is positioned to initiate the radical reaction []. There are several regions of similarity in the sequence of the large chain of prokaryotes, eukaryotes and viruses spread across 3 domains: an N-terminal domain common to the mammalian and bacterial enzymes; a C-terminal domain common to the mammalian and viral ribonucleotide reductases; and a central domain common to all three [].
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•
•
Publication
9241270 | J:42050
First Author: Koutnikova H
Year: 1997
Journal: Nat Genet
Title: Studies of human, mouse and yeast homologues indicate a mitochondrial function for frataxin.
Volume: 16
Issue: 4
Pages: 345-51
•
•
•
•
•
Protein
O35943
Organism: Mus musculus/domesticus
Length: 207  
Fragment?: false
•
•
•
•
•
Protein
Q3UG34
Organism: Mus musculus/domesticus
Length: 207  
Fragment?: false
•
•
•
•
•
Protein
Q3TV21
Organism: Mus musculus/domesticus
Length: 207  
Fragment?: false
•
•
•
•
•
Protein
Q6PDS4
Organism: Mus musculus/domesticus
Length: 101  
Fragment?: false
•
•
•
•
•
Publication
8815938 | -
First Author: Dürr A
Year: 1996
Journal: N Engl J Med
Title: Clinical and genetic abnormalities in patients with Friedreich's ataxia.
Volume: 335
Issue: 16
Pages: 1169-75
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•
•
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•
Publication
8596916 | -
First Author: Campuzano V
Year: 1996
Journal: Science
Title: Friedreich's ataxia: autosomal recessive disease caused by an intronic GAA triplet repeat expansion.
Volume: 271
Issue: 5254
Pages: 1423-7
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•
•
•
•
Publication
8931268 | -
First Author: Gibson TJ
Year: 1996
Journal: Trends Neurosci
Title: Friedreich's ataxia protein: phylogenetic evidence for mitochondrial dysfunction.
Volume: 19
Issue: 11
Pages: 465-8
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•
•
•
•
Publication
9309223 | -
First Author: Eriksson M
Year: 1997
Journal: Structure
Title: Binding of allosteric effectors to ribonucleotide reductase protein R1: reduction of active-site cysteines promotes substrate binding.
Volume: 5
Issue: 8
Pages: 1077-92
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•
•
•
•
Publication
3286319 | -
First Author: Nilsson O
Year: 1988
Journal: Biochem Soc Trans
Title: Structure-function studies of the large subunit of ribonucleotide reductase from Escherichia coli.
Volume: 16
Issue: 2
Pages: 91-4
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•
•
•
•
Publication
8511586 | -
First Author: Reichard P
Year: 1993
Journal: Science
Title: From RNA to DNA, why so many ribonucleotide reductases?
Volume: 260
Issue: 5115
Pages: 1773-7
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•
•
•
•
Publication
11875520 | -
First Author: Sintchak MD
Year: 2002
Journal: Nat Struct Biol
Title: The crystal structure of class II ribonucleotide reductase reveals how an allosterically regulated monomer mimics a dimer.
Volume: 9
Issue: 4
Pages: 293-300
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•
•
•
•
Protein
P07742
Organism: Mus musculus/domesticus
Length: 792  
Fragment?: false
•
•
•
•
•
Protein
Q6NZB3
Organism: Mus musculus/domesticus
Length: 792  
Fragment?: false
•
•
•
•
•
Protein
Q05DU8
Organism: Mus musculus/domesticus
Length: 762  
Fragment?: true
•
•
•
•
•
Protein
Q9R0P3
Organism: Mus musculus/domesticus
Length: 282  
Fragment?: false
•
•
•
•
•
Protein
H3BKH6
Organism: Mus musculus/domesticus
Length: 295  
Fragment?: false
•
•
•
•
•
Protein
H3BL99
Organism: Mus musculus/domesticus
Length: 105  
Fragment?: true
•
•
•
•
•
Protein
H3BJL6
Organism: Mus musculus/domesticus
Length: 265  
Fragment?: false
•
•
•
•
•
Protein
H3BJP2
Organism: Mus musculus/domesticus
Length: 247  
Fragment?: true
•
•
•
•
•
Protein
A0A3Q4EGB1
Organism: Mus musculus/domesticus
Length: 189  
Fragment?: true
•
•
•
•
•
Protein
A0A3Q4EIH1
Organism: Mus musculus/domesticus
Length: 133  
Fragment?: false
•
•
•
•
•
Protein
F7D3P0
Organism: Mus musculus/domesticus
Length: 138  
Fragment?: true
•
•
•
•
•
Protein
A0A3Q4L2S1
Organism: Mus musculus/domesticus
Length: 251  
Fragment?: false
•
•
•
•
•
Protein
Q8BNI3
Organism: Mus musculus/domesticus
Length: 140  
Fragment?: false
•
•
•
•
•
Protein
A0A3Q4EGU9
Organism: Mus musculus/domesticus
Length: 245  
Fragment?: false
•
•
•
•
•
Protein
H3BK43
Organism: Mus musculus/domesticus
Length: 249  
Fragment?: false
•
•
•
•
•
Protein
A0A3Q4EGS2
Organism: Mus musculus/domesticus
Length: 64  
Fragment?: false
•
•
•
•
•
Protein
H3BLJ9
Organism: Mus musculus/domesticus
Length: 259  
Fragment?: false
•
•
•
•
•
Protein
H3BJC6
Organism: Mus musculus/domesticus
Length: 135  
Fragment?: true
•
•
•
•
•
Protein
A0A2R8W6X5
Organism: Mus musculus/domesticus
Length: 121  
Fragment?: false
•
•
•
•
•
Protein
A0A3Q4EH93
Organism: Mus musculus/domesticus
Length: 211  
Fragment?: false
•
•
•
•
•
Publication
2190093 | -
First Author: Nordlund P
Year: 1990
Journal: Nature
Title: Three-dimensional structure of the free radical protein of ribonucleotide reductase.
Volume: 345
Issue: 6276
Pages: 593-8
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•
Publication
15168610 | -
First Author: Deppenmeier U
Year: 2004
Journal: J Bioenerg Biomembr
Title: The membrane-bound electron transport system of Methanosarcina species.
Volume: 36
Issue: 1
Pages: 55-64
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•
Publication
10629180 | -
First Author: Dasgupta N
Year: 2000
Journal: J Bacteriol
Title: fleN, a gene that regulates flagellar number in Pseudomonas aeruginosa.
Volume: 182
Issue: 2
Pages: 357-64
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•
Publication
21782439 | -
First Author: Al-Bassam J
Year: 2011
Journal: Trends Cell Biol
Title: Regulation of microtubule dynamics by TOG-domain proteins XMAP215/Dis1 and CLASP.
Volume: 21
Issue: 10
Pages: 604-14
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•
Publication
24630105 | -
 
First Author: Al-Bassam J
Year: 2014
Journal: Methods Enzymol
Title: Reconstituting dynamic microtubule polymerization regulation by TOG domain proteins.
Volume: 540
Pages: 131-48
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•
Publication
14526088 | -
First Author: Kurisu G
Year: 2003
Journal: Science
Title: Structure of the cytochrome b6f complex of oxygenic photosynthesis: tuning the cavity.
Volume: 302
Issue: 5647
Pages: 1009-14
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•
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•
•
Publication
8052308 | -
First Author: Uhlin U
Year: 1994
Journal: Nature
Title: Structure of ribonucleotide reductase protein R1.
Volume: 370
Issue: 6490
Pages: 533-9
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•
•
•
•
Protein
Q9R061
Organism: Mus musculus/domesticus
Length: 275  
Fragment?: false
•
•
•
•
•
Protein
Q9CWD8
Organism: Mus musculus/domesticus
Length: 319  
Fragment?: false
•
•
•
•
•
Protein
B9EJR8
Organism: Mus musculus/domesticus
Length: 853  
Fragment?: false
•
•
•
•
•
Protein
Q8BRT1
Organism: Mus musculus/domesticus
Length: 1286  
Fragment?: false
•
•
•
•
•
Protein
Q6A070
Organism: Mus musculus/domesticus
Length: 1776  
Fragment?: false
•
•
•
•
•
Protein
Q3TYG6
Organism: Mus musculus/domesticus
Length: 1002  
Fragment?: false
•
•
•
•
•
Protein
Q3URR8
Organism: Mus musculus/domesticus
Length: 319  
Fragment?: false
•
•
•
•
•
Protein
Q08EB6
Organism: Mus musculus/domesticus
Length: 1287  
Fragment?: false
•
•
•
•
•
Protein
B2RXS2
Organism: Mus musculus/domesticus
Length: 1776  
Fragment?: false
•
•
•
•
•
Protein
B2RXW9
Organism: Mus musculus/domesticus
Length: 1826  
Fragment?: false
•
•
•
•
•
Protein
Q3UF57
Organism: Mus musculus/domesticus
Length: 306  
Fragment?: true
•
•
•
•
•
Protein
A2RRR3
Organism: Mus musculus/domesticus
Length: 1089  
Fragment?: false
•
•
•
•
•
Protein
A0A1Y7VLN0
Organism: Mus musculus/domesticus
Length: 677  
Fragment?: true
•
•
•
•
•
Protein
D3YXX2
Organism: Mus musculus/domesticus
Length: 139  
Fragment?: false
•
•
•
•
•
Protein
B9EJA4
Organism: Mus musculus/domesticus
Length: 1308  
Fragment?: false
•
•
•
•
•
Protein
B7ZWL4
Organism: Mus musculus/domesticus
Length: 1776  
Fragment?: false
•
•
•
•
•
Protein
F7DCH5
Organism: Mus musculus/domesticus
Length: 1307  
Fragment?: false
•
•
•
•
•
Protein
Q6P6P2
Organism: Mus musculus/domesticus
Length: 441  
Fragment?: false
•
•
•
•
•




MouseMine is a collaboration between MGI at The Jackson Laboratory and the InterMine project at the Cambridge Systems Biology Centre. MouseMine is funded through a grant from the NIH/NHGRI.The Jackson Laboratory makes no representation about the suitability or accuracy of this software or data for any purpose, and makes no warranties, either express or implied, including merchantability and fitness for a particular purpose or that the use of this software or data will not infringe any third party patents, copyrights, trademarks, or other rights. the software and data are provided "as is". This software and data are provided to enhance knowledge and encourage progress in the scientific community and are to be used only for research and educational purposes. Any reproduction or use for commercial purpose is prohibited without the prior express written permission of the Jackson Laboratory.

Copyright © 2017 by The Jackson Laboratory. All Rights Reserved

© 2002 - 2017 Department of Genetics, University of Cambridge, Downing Street,
Cambridge CB2 3EH, United Kingdom