HMM Summary Page: TIGR03799

AccessionTIGR03799
NameNOD_PanD_pyr
Functionputative pyridoxal-dependent aspartate 1-decarboxylase
Gene SymbolpanP
Trusted Cutoff606.10
Domain Trusted Cutoff606.10
Noise Cutoff375.40
Domain Noise Cutoff375.40
Isology Typeequivalog
EC Number4.1.1.-
HMM Length522
Mainrole CategoryBiosynthesis of cofactors, prosthetic groups, and carriers
Subrole CategoryPantothenate and coenzyme A
Gene Ontology TermGO:0015940: pantothenate biosynthetic process biological_process
GO:0016831: carboxy-lyase activity molecular_function
AuthorHaft DH
Entry DateJul 30 2009 11:04AM
Last ModifiedFeb 14 2011 3:27PM
CommentThis 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 PropertyGenProp0124: pantothenate biosynthesis from aspartate and 2-oxoisovalerate (HMM)