| Accession | TIGR03799 |
| Name | NOD_PanD_pyr |
| Function | putative pyridoxal-dependent aspartate 1-decarboxylase |
| Gene Symbol | panP |
| Trusted Cutoff | 606.10 |
| Domain Trusted Cutoff | 606.10 |
| Noise Cutoff | 375.40 |
| Domain Noise Cutoff | 375.40 |
| Isology Type | equivalog |
| EC Number | 4.1.1.- |
| HMM Length | 522 |
| Mainrole Category | Biosynthesis of cofactors, prosthetic groups, and carriers |
| Subrole Category | Pantothenate and coenzyme A |
| Gene Ontology Term | GO:0015940: pantothenate biosynthetic process biological_process |
| | GO:0016831: carboxy-lyase activity molecular_function |
| Author | Haft DH |
| Entry Date | Jul 30 2009 11:04AM |
| Last Modified | Feb 14 2011 3:27PM |
| Comment | This enzyme is proposed here to be a form of aspartate 1-decarboxylase, pyridoxal-dependent, that represents a non-orthologous displacement to the more widely distributed pyruvoyl-dependent form (TIGR00223). Aspartate 1-decarboxylase makes beta-alanine, used usually in pathothenate biosynthesis, by decarboxylation from asparatate. A number of species with the PanB and PanC enzymes, however, lack PanD. This protein family occurs in a number of Proteobacteria that lack PanD. This enzyme family appears to be a pyridoxal-dependent enzyme (see PF00282). The family was identified by Partial Phylogenetic Profiling; members in Geobacter sulfurreducens, G. metallireducens, and Pseudoalteromonas atlantica are clustered with the genes for PanB and PanC. We suggest the gene symbol panP (panthothenate biosynthesis enzyme, Pyridoxal-dependent). |
| Genome Property | GenProp0124: pantothenate biosynthesis from aspartate and 2-oxoisovalerate (HMM) |
