Search by BoMiProt ID - Bomi212


Primary Information

BoMiProt ID Bomi212
Protein Name 4-trimethylaminobutyraldehyde dehydrogenase
Organism Bos taurus
Uniprot IdQ2KJH9
Milk FractionExosome
Ref Sequence Id NP_001039888.1
Aminoacid Length 494
Molecular Weight 53977
Fasta Sequence https://www.uniprot.org/uniprot/Q2KJH9.fasta
Gene Name ALDH9A1
Gene Id 537539
Protein Existence Status Reviewed: Experimental evidence at transcript level

Secondary Information

Protein Function cytosolic NAD1-dependent aldehyde dehydrogenase; converts γ-trimethylaminobutyraldehyde into g-butyrobetaine; trimethyllysine released upon protein degradation is oxidized to γ-butyrobetaine (BB) by the action of trimethyllysine dioxygenase (TMLHE), 3-hydroxy-N-TML aldolase and 4-N-trimethylaminobutyraldehyde dehydrogenase
Significance in milk mRNA abundances of 4-N-trimethylaminobutyraldehyde dehydrogenase is increased in liver biopsy samples of cows in late pregnancy and early lactation
PTMs N6-Acetylation at Lys and Ser
Site(s) of PTM(s)

N-glycosylation, O-glycosylation,
Phosphorylation
Predicted Disorder Regions (232-255)
DisProt Annotation
TM Helix Prediction No TM helices
Bibliography 1. Schlegel, G., Keller, J., Hirche, F., Geissler, S., Schwarz, F. J., Ringseis, R., … Eder, K. (2012). Expression of genes involved in hepatic carnitine synthesis and uptake in dairy cows in the transition period and at different stages of lactation. BMC Veterinary Research, 8, 28. https://doi.org/10.1186/1746-6148-8-28.
2. Vaz, F. M., Fouchier, S. W., Ofman, R., Sommer, M., & Wanders, R. J. (2000). Molecular and biochemical characterization of rat gamma-trimethylaminobutyraldehyde dehydrogenase and evidence for the involvement of human aldehyde dehydrogenase 9 in carnitine biosynthesis. The Journal of Biological Chemistry, 275(10), 7390–7394. https://doi.org/10.1074/jbc.275.10.7390.