Threonine-phosphate decarboxylase
Details
- Name
- Threonine-phosphate decarboxylase
- Synonyms
- 4.1.1.81
- L-threonine-O-3-phosphate decarboxylase
- Gene Name
- cobD
- Organism
- Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
- Amino acid sequence
>lcl|BSEQ0016507|Threonine-phosphate decarboxylase MALFNSAHGGNIREAATVLGISPDQLLDFSANINPLGMPVSVKRALIDNLDCIERYPDAD YFHLHQALARHHQVPASWILAGNGETESIFTVASGLKPRRAMIVTPGFAEYGRALAQSGC EIRRWSLREADGWQLTDAILEALTPDLDCLFLCTPNNPTGLLPERPLLQAIADRCKSLNI NLILDEAFIDFIPHETGFIPALKDNPHIWVLRSLTKFYAIPGLRLGYLVNSDDAAMARMR RQQMPWSVNALAALAGEVALQDSAWQQATWHWLREEGARFYQALCQLPLLTVYPGRANYL LLRCEREDIDLQRRLLTQRILIRSCANYPGLDSRYYRVAIRSAAQNERLLAALRNVLTGI APAD
- Number of residues
- 364
- Molecular Weight
- 40765.305
- Theoretical pI
- 6.92
- GO Classification
- Functionspyridoxal phosphate binding / threonine-phosphate decarboxylase activityProcessescobalamin biosynthetic process
- General Function
- Threonine-phosphate decarboxylase activity
- Specific Function
- Decarboxylates L-threonine-O-3-phosphate to yield (R)-1-amino-2-propanol O-2-phosphate, the precursor for the linkage between the nucleotide loop and the corrin ring in cobalamin.
- Pfam Domain Function
- Aminotran_1_2 (PF00155)
- Transmembrane Regions
- Not Available
- Cellular Location
- Not Available
- Gene sequence
>lcl|BSEQ0016508|Threonine-phosphate decarboxylase (cobD) ATGGCGTTATTCAACAGCGCGCATGGCGGTAATATTCGGGAAGCCGCGACGGTGTTGGGC ATCTCGCCTGACCAGTTACTGGATTTTAGCGCAAACATTAATCCGCTGGGTATGCCTGTC AGCGTGAAACGCGCGCTTATCGACAATCTGGACTGCATTGAGCGCTACCCGGACGCCGAT TATTTTCATTTGCACCAGGCGCTGGCGCGTCATCATCAGGTGCCGGCATCGTGGATACTG GCGGGAAATGGCGAGACGGAGTCAATCTTTACCGTGGCGAGCGGTCTTAAACCGCGTCGT GCAATGATTGTCACGCCAGGTTTCGCGGAGTATGGCCGGGCGCTGGCGCAAAGTGGCTGT GAAATTCGTCGCTGGTCTCTACGCGAAGCGGATGGCTGGCAGCTTACCGATGCCATTCTT GAGGCGTTGACGCCCGATCTGGACTGCCTGTTTCTGTGTACGCCTAATAATCCTACCGGC CTGCTGCCGGAGCGGCCGTTATTACAGGCCATTGCCGATCGCTGCAAATCGCTGAACATT AACCTGATCCTGGATGAAGCGTTTATCGATTTTATTCCGCATGAGACGGGCTTTATTCCT GCTCTTAAAGATAATCCGCATATCTGGGTGCTGCGTTCGCTGACCAAATTTTATGCCATT CCCGGCCTGCGGTTGGGATATCTCGTCAATAGCGATGACGCGGCGATGGCGCGGATGCGT CGCCAACAAATGCCGTGGTCGGTTAACGCGCTGGCGGCGCTTGCCGGTGAGGTAGCGTTA CAGGATAGCGCCTGGCAACAGGCGACCTGGCATTGGTTACGGGAGGAGGGCGCCCGGTTT TATCAGGCGCTTTGTCAGCTCCCCCTGCTGACGGTTTATCCCGGGCGGGCAAACTATCTG TTGTTACGCTGTGAGCGAGAGGATATTGATCTGCAGCGACGGTTGCTGACGCAGCGGATT TTAATCCGTAGCTGCGCTAACTACCCGGGGCTGGACAGCCGCTATTATCGTGTGGCGATA CGCAGCGCTGCGCAAAACGAGCGTCTGCTGGCGGCGCTGCGCAATGTGCTTACCGGTATA GCCCCTGCTGATTGA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P97084 UniProtKB Entry Name COBD_SALTY GenBank Protein ID 1895094 GenBank Gene ID U90625 - General References
- Brushaber KR, O'Toole GA, Escalante-Semerena JC: 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. 1998 Jan 30;273(5):2684-91. [Article]
- McClelland M, Sanderson KE, Spieth J, Clifton SW, Latreille P, Courtney L, Porwollik S, Ali J, Dante M, Du F, Hou S, Layman D, Leonard S, Nguyen C, Scott K, Holmes A, Grewal N, Mulvaney E, Ryan E, Sun H, Florea L, Miller W, Stoneking T, Nhan M, Waterston R, Wilson RK: Complete genome sequence of Salmonella enterica serovar Typhimurium LT2. Nature. 2001 Oct 25;413(6858):852-6. [Article]
- Cheong CG, Bauer CB, Brushaber KR, Escalante-Semerena JC, Rayment I: Three-dimensional structure of the L-threonine-O-3-phosphate decarboxylase (CobD) enzyme from Salmonella enterica. Biochemistry. 2002 Apr 16;41(15):4798-808. [Article]
- Cheong CG, Escalante-Semerena JC, Rayment I: Structural studies of the L-threonine-O-3-phosphate decarboxylase (CobD) enzyme from Salmonella enterica: the apo, substrate, and product-aldimine complexes. Biochemistry. 2002 Jul 23;41(29):9079-89. [Article]