Activities | Families | Sequences | Fold types | References | Help
B6db families:
Description Threonine-phosphate decarboxylase
Notes Family built around the characterized enzyme from Salmonella enterica.
The proteins are most similar to histidinol phosphate aminotransferases (family
PLP Fold Type I
PLP-dependent Domain
Domain alignment
Domain hmm
Fold type I

Number of sequences 9
Sequences in seed alignment
Bacteria1LC7A (Salmonella enterica); CAC99247 (Listeria monocytogenes); CAE15341 (Photorhabdus luminescens ); AAC79515 (Salmonella typhimurium); BAB80746 (Clostridium perfringens); AAW65978 (Escherichia blattae); AAX14516 (Lactobacillus reuteri); YP_001006940 (Yersinia enterocolitica); YP_001034507 (Streptococcus sanguinis);

DISPLAY: Fasta format, alignment, hmm, hmm_local

Reference sequence 1LC7A
Domain interval 24-353
Catalytic site 216 K
 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
last changed 2008/01/31 12:24

B6db families