| Accession | TIGR00551 |
| Name | nadB |
| Function | L-aspartate oxidase |
| Gene Symbol | nadB |
| Trusted Cutoff | 452.75 |
| Domain Trusted Cutoff | 452.75 |
| Noise Cutoff | 425.60 |
| Domain Noise Cutoff | 425.60 |
| Isology Type | equivalog |
| EC Number | 1.4.3.16 |
| HMM Length | 489 |
| Mainrole Category | Biosynthesis of cofactors, prosthetic groups, and carriers |
| Subrole Category | Pyridine nucleotides |
| Gene Ontology Term | GO:0008734: L-aspartate oxidase activity molecular_function |
| | GO:0019363: pyridine nucleotide biosynthetic process biological_process |
| | GO:0019804: quinolinate synthetase complex cellular_component |
| Author | Haft DH |
| Entry Date | Oct 19 1999 4:30PM |
| Last Modified | Feb 14 2011 3:27PM |
| Comment | L-aspartate oxidase is the B protein, NadB, of the quinolinate synthetase complex. Quinolinate synthetase makes a precursor of the pyridine nucleotide portion of NAD. This model identifies proteins that cluster as L-aspartate oxidase (a flavoprotein difficult to separate from the set of closely related flavoprotein subunits of succinate dehydrogenase and fumarate reductase) by both UPGMA and neighbor-joining trees. The most distant protein accepted as an L-aspartate oxidase (NadB), that from Pyrococcus horikoshii, not only clusters with other NadB but is just one gene away from NadA.
|
| References | A2 hmmalign
DR PFAM; PF00890; FAD_binding_2
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| Genome Property | GenProp0057: NAD(P) biosynthesis from L-aspartate and DHAP (HMM) |
