F
IPR020852

Ribonucleotide reductase, class Ib, NrdI, bacterial

InterPro entry
Short nameRNR_Ib_NrdI_bac
Overlapping
homologous
superfamilies
 
family relationships

Description

Ribonucleotide reductases (RNRs) are enzymes that catalyse the conversion of ribonucleotides to the corresponding deoxyribonucleotides to provide the precursors of DNA synthesis. There are three classes (I-III) of RNRs and four known subclasses within class I RNRs (Ia-Id)
[3]
, which differ by their metal cofactor, their stable organic radical and sequence
[2]
. Class I consists of two homodimeric subunits: alpha2, which catalyses the reversible one-electron oxidation of a conserved cysteine residue to a thiyl radical, which is initiated by a dinuclear metallocofactor and tyrosyl radical positioned in the beta2 subunit. Class Ib RNR is encoded in four different genes: nrdH, nrdI, nrdE (alpha subunit) and nrdF (beta subunit)
[1]
and has Mn2 in the dimetal cluster to oxidize a nearby tyrosine residue to a stable radical.

This family represents NrdI, a flavoprotein activase which provides superoxide that binds to the beta subunit and forms a hydrophilic channel connecting their active sites
[1]
.

Note, this entry also includes Bacillus phage proteins.

References

1.Corynebacterium ammoniagenes class Ib ribonucleotide reductase: transcriptional regulation of an atypical genomic organization in the nrd cluster. Torrents E, Roca I, Gibert I. Microbiology (Reading, Engl.) 149, 1011-20, (2003). View articlePMID: 12686643

2.Crystal structure of Bacillus cereus class Ib ribonucleotide reductase di-iron NrdF in complex with NrdI. Hammerstad M, Hersleth HP, Tomter AB, Rohr AK, Andersson KK. ACS Chem Biol 9, 526-37, (2014). PMID: 24295378

3.Metal-free class Ie ribonucleotide reductase from pathogens initiates catalysis with a tyrosine-derived dihydroxyphenylalanine radical. Blaesi EJ, Palowitch GM, Hu K, Kim AJ, Rose HR, Alapati R, Lougee MG, Kim HJ, Taguchi AT, Tan KO, Laremore TN, Griffin RG, Krebs C, Matthews ML, Silakov A, Bollinger JM Jr, Allen BD, Boal AK. Proc Natl Acad Sci U S A 115, 10022-10027, (2018). PMID: 30224458

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