Phosphotriesterase

Details

Name
Phosphotriesterase
Synonyms
Not Available
Gene Name
opdA
Organism
Agrobacterium tumefaciens
Amino acid sequence
>lcl|BSEQ0019412|Phosphotriesterase
MQTRRDALKSAAAITLLGGLAGCASMARPIGTGDLINTVRGPIPVSEAGFTLTHEHICGS
SAGFLRAWPEFFGSRKALAEKAVRGLRHARSAGVQTIVDVSTFDIGRDVRLLAEVSRAAD
VHIVAATGLWFDPPLSMRMRSVEELTQFFLREIQHGIEDTGIRAGIIKVATTGKATPFQE
LVLKAAARASLATGVPVTTHTSASQRDGEQQAAIFESEGLSPSRVCIGHSDDTDDLSYLT
GLAARGYLVGLDRMPYSAIGLEGNASALALFGTRSWQTRALLIKALIDRGYKDRILVSHD
WLFGFSSYVTNIMDVMDRINPDGMAFVPLRVIPFLREKGVPPETLAGVTVANPARFLSPT
VRAVVTRSETSRPAAPIPRQDTER
Number of residues
384
Molecular Weight
41362.905
Theoretical pI
9.17
GO Classification
Functions
hydrolase activity, acting on ester bonds / zinc ion binding
Processes
catabolic process
General Function
Zinc ion binding
Specific Function
Not Available
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Cytoplasmic
Gene sequence
>lcl|BSEQ0006533|1155 bp
ATGCAAACGAGAAGAGATGCACTTAAGTCTGCGGCCGCAATAACTCTGCTCGGCGGCTTG
GCTGGGTGTGCAAGCATGGCCCGACCAATCGGTACAGGCGATCTGATTAATACTGTTCGC
GGCCCCATTCCAGTTTCGGAAGCGGGCTTCACACTGACCCATGAGCATATCTGCGGCAGT
TCGGCGGGATTCCTACGTGCGTGGCCGGAGTTTTTCGGTAGCCGCAAAGCTCTAGCGGAA
AAGGCTGTGAGAGGATTACGCCATGCCAGATCGGCTGGCGTGCAAACCATCGTCGATGTG
TCGACTTTCGATATCGGTCGTGACGTCCGTTTATTGGCCGAAGTTTCGCGGGCCGCCGAC
GTGCATATCGTGGCGGCGACTGGCTTATGGTTCGACCCGCCACTTTCAATGCGAATGCGC
AGCGTCGAAGAACTGACCCAGTTCTTCCTGCGTGAAATCCAACATGGCATCGAAGACACC
GGTATTAGGGCGGGCATTATCAAGGTCGCGACCACAGGGAAGGCGACCCCCTTTCAAGAG
TTGGTGTTAAAGGCAGCCGCGCGGGCCAGCTTGGCCACCGGTGTTCCGGTAACCACTCAC
ACGTCAGCAAGTCAGCGCGATGGCGAGCAGCAGGCAGCCATATTTGAATCCGAAGGTTTG
AGCCCCTCACGGGTTTGTATCGGTCACAGCGATGATACTGACGATTTGAGCTACCTAACC
GGCCTCGCTGCGCGCGGATACCTCGTCGGTTTAGATCGCATGCCGTACAGTGCGATTGGT
CTAGAAGGCAATGCGAGTGCATTAGCGCTCTTTGGTACTCGGTCGTGGCAAACAAGGGCT
CTCTTGATCAAGGCGCTCATCGACCGAGGCTACAAGGATCGAATCCTCGTCTCCCATGAC
TGGCTGTTCGGGTTTTCGAGCTATGTCACGAACATCATGGACGTAATGGATCGCATAAAC
CCAGATGGAATGGCCTTCGTCCCTCTGAGAGTGATCCCATTCCTACGAGAGAAGGGCGTC
CCGCCGGAAACGCTAGCAGGCGTAACCGTGGCCAATCCCGCGCGGTTCTTGTCACCGACC
GTGCGGGCCGTCGTGACACGATCTGAAACTTCCCGCCCTGCCGCGCCTATTCCCCGTCAA
GATACCGAACGATGA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDQ93LD7
UniProtKB Entry NameQ93LD7_RHIRD
GenBank Gene IDAY043245
General References
  1. Jackson C, Kim HK, Carr PD, Liu JW, Ollis DL: The structure of an enzyme-product complex reveals the critical role of a terminal hydroxide nucleophile in the bacterial phosphotriesterase mechanism. Biochim Biophys Acta. 2005 Aug 31;1752(1):56-64. [Article]
  2. Jackson CJ, Foo JL, Kim HK, Carr PD, Liu JW, Salem G, Ollis DL: In crystallo capture of a Michaelis complex and product-binding modes of a bacterial phosphotriesterase. J Mol Biol. 2008 Feb 1;375(5):1189-96. Epub 2007 Nov 1. [Article]
  3. Jackson CJ, Foo JL, Tokuriki N, Afriat L, Carr PD, Kim HK, Schenk G, Tawfik DS, Ollis DL: Conformational sampling, catalysis, and evolution of the bacterial phosphotriesterase. Proc Natl Acad Sci U S A. 2009 Dec 22;106(51):21631-6. doi: 10.1073/pnas.0907548106. Epub 2009 Dec 4. [Article]
  4. Ely F, Hadler KS, Gahan LR, Guddat LW, Ollis DL, Schenk G: The organophosphate-degrading enzyme from Agrobacterium radiobacter displays mechanistic flexibility for catalysis. Biochem J. 2010 Dec 15;432(3):565-73. doi: 10.1042/BJ20101054. [Article]
  5. Ely F, Pedroso MM, Gahan LR, Ollis DL, Guddat LW, Schenk G: Phosphate-bound structure of an organophosphate-degrading enzyme from Agrobacterium radiobacter. J Inorg Biochem. 2012 Jan;106(1):19-22. doi: 10.1016/j.jinorgbio.2011.09.015. Epub 2011 Sep 17. [Article]
  6. Naqvi T, Warden AC, French N, Sugrue E, Carr PD, Jackson CJ, Scott C: A 5000-fold increase in the specificity of a bacterial phosphotriesterase for malathion through combinatorial active site mutagenesis. PLoS One. 2014 Apr 10;9(4):e94177. doi: 10.1371/journal.pone.0094177. eCollection 2014. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB04687DIMETHYL THIOPHOSPHATEexperimentalunknownDetails
DB07674O,O-DIETHYL HYDROGEN THIOPHOSPHATEexperimentalunknownDetails
DB07721DIETHYL 4-METHOXYPHENYL PHOSPHATEexperimentalunknownDetails