Activities | Families | Sequences | Fold types | References | Help
B6db families: 4.1.1.81

4.1.1.81
Activity 4.1.1.81
Description Threonine-phosphate decarboxylase.
Notes Family built around the characterized enzyme from Salmonella enterica.
The proteins are most similar to histidinol phosphate aminotransferases (family 2.6.1.9)
PDB 1LKC;
PLP Fold Type I
PLP-dependent Domain
Domain alignment
Domain hmm
Fold type I

Number of sequences
9
Sequences in seed alignment
BacteriaAAX14516 (Lactobacillus reuteri); AAC79515 (Salmonella typhimurium); CAE15341 (Photorhabdus luminescens ); BAB80746 (Clostridium perfringens); CAC99247 (Listeria monocytogenes); YP_001034507 (Streptococcus sanguinis); AAW65978 (Escherichia blattae); 1LC7A (Salmonella enterica); YP_001006940 (Yersinia enterocolitica);

DISPLAY: Fasta format, alignment, hmm, hmm_local


Reference sequence 1LC7A
Domain interval 24-353
Catalytic site 216 K
 
References
 Santos F, Vera JL, van der Heijden R, Valdez G, de Vos WM, Sesma F, Hugenholtz J. (2008) The complete coenzyme B12 biosynthesis gene cluster of Lactobacillus reuteri CRL1098 Microbiology 154 81-93.

 Cheong, C.G.; Bauer, C.B.; Brushaber, K.R.; Escalante-Semerena, J.C.; Rayment, I. (2002) Three-dimensional structure of the L-threonine-O-3-phosphate decarboxylase (CobD) enzyme from Salmonella enterica Biochemistry 41 4798-808.

 Brushaber, K.R.; O'Toole, G.A.;Escalante-Semerena, J.C. (1998) CobD, a novel enzyme with L-threonine-O-3-phosphate decarboxylase activity, is responsible for the synthesis of (R)-1-amino-2-propanol O-2-phosphate, a proposed new intermediate in cobalamin biosynthesis in Salmonella typhimurium LT2 J Biol Chem 273 2684-91.

Articles on 4.1.1.81
last changed 2008/01/31 12:24

B6db families