Phosphotriesterase
Details
- Name
- Phosphotriesterase
- Kind
- protein
- Synonyms
- Not Available
- Gene Name
- opdA
- UniProtKB Entry
- Q93LD7TrEMBL
- Organism
- Agrobacterium tumefaciens
- NCBI Taxonomy ID
- 358
- 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
- Functionshydrolase activity, acting on ester bonds / zinc ion bindingProcessescatabolic process
- General Function
- Not Available
- Specific Function
- hydrolase activity, acting on ester bonds
- Pfam Domain Function
- PTE (PF02126)
- Signal Regions
- 1-27
- 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
Resource Link UniProtKB ID Q93LD7 UniProtKB Entry Name Q93LD7_RHIRD GenBank Gene ID AY043245 PDB ID(s) 2D2G, 2D2H, 2D2J, 2R1K, 2R1L, 2R1M, 2R1N, 2R1P, 3A3W, 3A3X, 3A4J, 3C86, 3OOD, 3OQE, 3SO7, 3WML, 4NP7 - General References
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
Associated Data
- Drug Relations
Drug Drug group Pharmacological action? Type Actions Details DIMETHYL THIOPHOSPHATE experimental unknown target Details O,O-DIETHYL HYDROGEN THIOPHOSPHATE experimental unknown target Details DIETHYL 4-METHOXYPHENYL PHOSPHATE experimental unknown target Details