B6db families : 4_1_1

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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

PLP-dependent Domain

Domain alignment
Domain hmm

Fold type I

Number of sequences

Sequences in seed alignment

Bacteria

BAB80746 (Clostridium perfringens); AAC79515 (Salmonella typhimurium); 1LC7A (Salmonella enterica); AAX14516 (Lactobacillus reuteri); AAW65978 (Escherichia blattae); YP_001034507 (Streptococcus sanguinis); YP_001006940 (Yersinia enterocolitica); CAE15341 (Photorhabdus luminescens ); CAC99247 (Listeria monocytogenes);

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