| Accession | TIGR01510 |
| Name | coaD_prev_kdtB |
| Function | pantetheine-phosphate adenylyltransferase |
| Gene Symbol | coaD |
| Trusted Cutoff | 103.30 |
| Domain Trusted Cutoff | 103.30 |
| Noise Cutoff | 72.75 |
| Domain Noise Cutoff | 72.75 |
| Isology Type | equivalog |
| EC Number | 2.7.7.3 |
| HMM Length | 155 |
| Mainrole Category | Biosynthesis of cofactors, prosthetic groups, and carriers |
| Subrole Category | Pantothenate and coenzyme A |
| Gene Ontology Term | GO:0004595: pantetheine-phosphate adenylyltransferase activity molecular_function |
| | GO:0015937: coenzyme A biosynthetic process biological_process |
| Author | Haft DH |
| Entry Date | May 16 2002 4:24PM |
| Last Modified | Feb 14 2011 3:27PM |
| Comment | This HMM describes pantetheine-phosphate adenylyltransferase, the penultimate enzyme of coenzyme A (CoA) biosynthesis in bacteria. It does not show any strong homology to eukaryotic enzymes of coenzyme A biosynthesis. This protein was previously designated KdtB and postulated (because of cytidyltransferase homology and proximity to kdtA) to be an enzyme of LPS biosynthesis, a cytidyltransferase for 3-deoxy-D-manno-2-octulosonic acid. However, no activity toward that compound was found with either CTP or ATP. The phylogenetic distribution of this enzyme is more consistent with coenzyme A biosynthesis than with LPS biosynthesis. |
| References | RM 10480925
RT Purification and characterization of phosphopantetheine adenylyltransferase from Escherichia coli.
RA Geerlof A, Lewendon A, Shaw WV.
RL J Biol Chem 1999 Sep 17;274(38):27105-11
DR HAMAP; MF_00151; 431 of 437 |
| Genome Property | GenProp0171: coenzyme A biosynthesis from pantothenate (HMM) |
