HMM Summary Page: TIGR01526

Functionnicotinamide-nucleotide adenylyltransferase
Trusted Cutoff341.15
Domain Trusted Cutoff341.15
Noise Cutoff78.30
Domain Noise Cutoff78.30
Isology Typeequivalog_domain
EC Number2.7.7.1
HMM Length325
Gene Ontology TermGO:0000309: nicotinamide-nucleotide adenylyltransferase activity molecular_function
GO:0009435: NAD biosynthetic process biological_process
AuthorHaft DH
Entry DateMay 31 2002 12:01AM
Last ModifiedFeb 14 2011 3:27PM
CommentThe NadR protein of E. coli and closely related bacteria is both enzyme and regulatory protein. The first 60 or so amino acids, N-terminal to the region covered by this model, is a DNA-binding helix-turn-helix domain (PF01381) responsible for repressing the nadAB genes of NAD de novo biosynthesis. The NadR homologs in Mycobacterium tuberculosis, Haemophilus influenzae, and others appear to lack the repressor domain. NadR has recently been shown to act as an enzyme of the salvage pathway of NAD biosynthesis, nicotinamide-nucleotide adenylyltransferase; members of this family are presumed to share this activity. E. coli NadR has also been found to regulate the import of its substrate, nicotinamide ribonucleotide, but it is not known if the other members of this model share that activity.
ReferencesRM 10464228 RT The Escherichia coli NadR regulator is endowed with nicotinamide mononucleotide adenylyltransferase activity. RA Raffaelli N, Lorenzi T, Mariani PL, Emanuelli M, Amici A, Ruggieri S, Magni G. RL J Bacteriol 1999 Sep;181(17):5509-11