| Accession | TIGR00525 |
| Name | folB |
| Function | dihydroneopterin aldolase |
| Gene Symbol | folB |
| Trusted Cutoff | 72.15 |
| Domain Trusted Cutoff | 72.15 |
| Noise Cutoff | 23.40 |
| Domain Noise Cutoff | 23.40 |
| Isology Type | equivalog |
| EC Number | 4.1.2.25 |
| HMM Length | 116 |
| Mainrole Category | Biosynthesis of cofactors, prosthetic groups, and carriers |
| Subrole Category | Folic acid |
| Gene Ontology Term | GO:0004150: dihydroneopterin aldolase activity molecular_function |
| | GO:0006760: folic acid-containing compound metabolic process biological_process |
| Author | Haft DH |
| Entry Date | Oct 18 1999 5:03PM |
| Last Modified | Feb 14 2011 3:27PM |
| Comment | This model describes a bacterial dihydroneopterin aldolase, shown to form homo-octamers in E. coli. The equivalent activity is catalyzed by domains of larger folate biosynthesis proteins in other systems. The closely related parologous enzyme in E. coli, dihydroneopterin triphosphate epimerase, which is also homo-octameric, and dihydroneopterin aldolase domains of larger proteins, score below the trusted cutoff but may score well above the noise cutoff. |
| References | A2 hmmalign
AL ClustalW_manual
RM 98316300
RT Biosynthesis of pteridines in Escherichia coli. Structural and mechanistic similarity of dihydroneopterin-triphosphate epimerase and dihydroneopterin aldolase.
RA Haussmann C, Rohdich F, Schmidt E, Bacher A, Richter G
RL J Biol Chem 1998 Jul 10;273(28):17418-24 |
| Genome Property | GenProp0038: tetrahydrofolate biosynthesis from GTP and PABA (HMM) |
