Accession | TIGR00687 |
Name | pyridox_kin |
Function | pyridoxal kinase |
Trusted Cutoff | 144.50 |
Domain Trusted Cutoff | 144.50 |
Noise Cutoff | 73.45 |
Domain Noise Cutoff | 73.45 |
Isology Type | equivalog |
EC Number | 2.7.1.35 |
HMM Length | 288 |
Mainrole Category | Biosynthesis of cofactors, prosthetic groups, and carriers |
Subrole Category | Pyridoxine |
Gene Ontology Term | GO:0008478: pyridoxal kinase activity molecular_function |
| GO:0009443: pyridoxal 5'-phosphate salvage biological_process |
Author | Haft DH, Loftus BJ |
Entry Date | Jan 13 2000 2:40PM |
Last Modified | Feb 14 2011 3:27PM |
Comment | E. coli has an enzyme PdxK that acts in vitro as a pyridoxine/pyridoxal/pyridoxamine kinase, but mutants lacking PdxK activity retain a specific pyridoxal kinase, PdxY. PdxY acts in the salvage pathway of pyridoxal 5'-phosphate biosynthesis. Mammalian forms of pyridoxal kinase are more similar to PdxY than to PdxK. The PdxK isozyme is omitted from the seed alignment but scores above the trusted cutoff.
ThiD and related proteins form an outgroup.
|
References | AL clustalW
RN [1]
RM 98196726
RN [2]
RM 96291683
DR EXPERIMENTAL; EGAD|91884|EC1636; pdxY
DR EXPERIMENTAL; EGAD|30575|EC2418; pdxK
DR EXPERIMENTAL; GP|2773404|gb|AAB96794.1||AF041255
DR OUTGROUP; EGAD|21177|BS3795
DR OUTGROUP; EGAD|89357|HP0844
DR HAMAP; MF_01639; 57 of 58 |