| Accession | TIGR00674 |
| Name | dapA |
| Function | 4-hydroxy-tetrahydrodipicolinate synthase |
| Gene Symbol | dapA |
| Trusted Cutoff | 206.15 |
| Domain Trusted Cutoff | 206.15 |
| Noise Cutoff | 177.55 |
| Domain Noise Cutoff | 177.55 |
| Isology Type | equivalog |
| EC Number | 4.3.3.7 |
| HMM Length | 286 |
| Mainrole Category | Amino acid biosynthesis |
| Subrole Category | Aspartate family |
| Gene Ontology Term | GO:0008840: dihydrodipicolinate synthase activity molecular_function |
| | GO:0009089: lysine biosynthetic process via diaminopimelate biological_process |
| Author | Haft DH |
| Entry Date | Jan 13 2000 2:40PM |
| Last Modified | Feb 14 2011 3:27PM |
| Comment | Members of this family are 4-hydroxy-tetrahydrodipicolinate synthase, previously (incorrectly) called dihydrodipicolinate synthase. It is a homotetrameric enzyme of lysine biosynthesis. E. coli has several paralogs closely related to dihydrodipicoline synthase (DapA), as well as the more distant N-acetylneuraminate lyase. In Pyrococcus horikoshii, the bidirectional best hit with E. coli is to an uncharacterized paralog of DapA, not DapA itself, and it is omitted from the seed. The putative members from the Chlamydias (pathogens with a parasitic metabolism) are easily the most divergent members of the multiple alignment. |
| References | DR EXPERIMENTAL; EGAD|128581|137272; poplar
DR EXPERIMENTAL; EGAD|128579|137270; tobacco
DR EXPERIMENTAL; EGAD|14906|EC2478; E. coli
DR EXPERIMENTAL; EGAD|10095|9900; Corynebacterium glutamicum
DR EXCEPTION; >EGAD|14762|14776; MosA; Rhizobium meliloti
DR OUTGROUP; EGAD|29522|EC3225; N-acetylneuraminate lyase
DR PFAM; PF00701; DHDPS; dihydrodipicolinate synthase superfamily
DR HAMAP; MF_00418; 355 of 370 |
| Genome Property | GenProp0125: lysine biosynthesis via diaminopimelate (DAP) (HMM) |
| | GenProp0788: lysine biosynthesis via diaminopimelate (DAP) utilizing ammonia and NADPH (HMM) |
