Accession | TIGR01527 |
Name | arch_NMN_Atrans |
Function | nicotinamide-nucleotide adenylyltransferase |
Trusted Cutoff | 181.20 |
Domain Trusted Cutoff | 181.20 |
Noise Cutoff | 73.45 |
Domain Noise Cutoff | 73.45 |
Isology Type | equivalog |
EC Number | 2.7.7.1 |
HMM Length | 167 |
Mainrole Category | Biosynthesis of cofactors, prosthetic groups, and carriers |
Subrole Category | Pyridine nucleotides |
Gene Ontology Term | GO:0000309: nicotinamide-nucleotide adenylyltransferase activity molecular_function |
| GO:0009435: NAD biosynthetic process biological_process |
Author | Haft DH |
Entry Date | May 31 2002 10:28AM |
Last Modified | Feb 14 2011 3:27PM |
Comment | This HMM describes a family of archaeal proteins with the activity of the NAD salvage biosynthesis enzyme nicotinamide-nucleotide adenylyltransferase (EC 2.7.7.1). In some cases, the enzyme was tested and found also to have the activity of nicotinate-nucleotide adenylyltransferase (EC 2.7.7.18), an enzyme of NAD de novo biosynthesis, although with a higher Km.
In some archaeal species, a lower-scoring paralog, uncharacterized with respect to activity, is also present. These score between trusted and noise cutoffs. |
References | RM 9401030
RT Characterization of nicotinamide mononucleotide adenylyltransferase from thermophilic archaea.
RA Raffaelli N, Pisani FM, Lorenzi T, Emanuelli M, Amici A, Ruggieri S, Magni G.
RL J Bacteriol. 1997 Dec;179(24):7718-23.
DR HAMAP; MF_00243; 33 of 36 |
Genome Property | GenProp0057: NAD(P) biosynthesis from L-aspartate and DHAP (HMM) |