HMM Summary Page: TIGR02487

Functionanaerobic ribonucleoside-triphosphate reductase
Gene SymbolnrdD
Trusted Cutoff326.35
Domain Trusted Cutoff326.35
Noise Cutoff261.75
Domain Noise Cutoff261.75
Isology Typeequivalog
EC Number1.17.4.2
HMM Length581
Mainrole CategoryPurines, pyrimidines, nucleosides, and nucleotides
Subrole Category2'-Deoxyribonucleotide metabolism
Gene Ontology TermGO:0008998: ribonucleoside-triphosphate reductase activity molecular_function
GO:0009265: 2'-deoxyribonucleotide biosynthetic process biological_process
AuthorSelengut J
Entry DateFeb 24 2005 12:08PM
Last ModifiedFeb 14 2011 3:27PM
CommentThis model represents the oxygen-sensitive (anaerobic, class III) ribonucleotide reductase. The mechanism of the enzyme involves a glycine-centered radical [1], a C-terminal zinc binding site [2], and a set of conserved active site cysteines and asparagines [3]. This enzyme requires an activating component, NrdG, a radical-SAM domain containing enzyme (TIGR02491). Together the two form an alpha-2/beta-2 heterodimer.
ReferencesRN [1] RM PMID: 10066165 RT A glycyl radical site in the crystal structure of a class III ribonucleotide reductase. RA Logan DT, Andersson J, Sjoberg BM, Nordlund P. RL Science. 1999 Mar 5;283(5407):1499-504. RN [2] RM PMID: 12655046 RT A metal-binding site in the catalytic subunit of anaerobic ribonucleotide reductase. RA Logan DT, Mulliez E, Larsson KM, Bodevin S, Atta M, Garnaud PE, Sjoberg BM, Fontecave M. RL Proc Natl Acad Sci U S A. 2003 Apr 1;100(7):3826-31. Epub 2003 Mar 24. RN [3] RM PMID: 11526118 RT Two active site asparagines are essential for the reaction mechanism of the class III anaerobic ribonucleotide reductase from bacteriophage T4. RA Andersson J, Bodevin S, Westman M, Sahlin M, Sjoberg BM. RL J Biol Chem. 2001 Nov 2;276(44):40457-63. Epub 2001 Aug 28.
Genome PropertyGenProp0291: class III (anaerobic) ribonucleotide reductase (HMM)