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
Functions
pyridoxal phosphate binding / threonine-phosphate decarboxylase activity
Processes
cobalamin 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
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
ResourceLink
UniProtKB IDP97084
UniProtKB Entry NameCOBD_SALTY
GenBank Protein ID1895094
GenBank Gene IDU90625
General References
  1. 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. [PubMed:9446573]
  2. 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. [PubMed:11677609]
  3. 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. [PubMed:11939774]
  4. 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. [PubMed:12119022]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB02482PhosphonothreonineexperimentalunknownDetails
DB03433{3-[(3-Hydroxy-2-Methyl-5-Phosphonooxymethyl-Pyridin-4-Ylmethyl)-Amino]-2-Methyl-Propyl}-Phosphonic AcidexperimentalunknownDetails