Parathion hydrolase

Details

Name
Parathion hydrolase
Synonyms
  • 3.1.8.1
  • Phosphotriesterase
  • PTE
Gene Name
opd
Organism
Sphingobium fuliginis (strain ATCC 27551)
Amino acid sequence
>lcl|BSEQ0011087|Parathion hydrolase
MQTRRVVLKSAAAAGTLLGGLAGCASVAGSIGTGDRINTVRGPITISEAGFTLTHEHICG
SSAGFLRAWPEFFGSRKALAEKAVRGLRRARAAGVRTIVDVSTFDIGRDVSLLAEVSRAA
DVHIVAATGLWFDPPLSMRLRSVEELTQFFLREIQYGIEDTGIRAGIIKVATTGKATPFQ
ELVLKAAARASLATGVPVTTHTAASQRDGEQQAAIFESEGLSPSRVCIGHSDDTDDLSYL
TALAARGYLIGLDHIPHSAIGLEDNASASALLGIRSWQTRALLIKALIDQGYMKQILVSN
DWLFGFSSYVTNIMDVMDRVNPDGMAFIPLRVIPFLREKGVPQETLAGITVTNPARFLSP
TLRAS
Number of residues
365
Molecular Weight
39003.24
Theoretical pI
8.48
GO Classification
Functions
aryldialkylphosphatase activity / zinc ion binding
Processes
catabolic process
Components
plasma membrane
General Function
Zinc ion binding
Specific Function
Has an unusual substrate specificity for synthetic organophosphate triesters and phosphorofluoridates. All of the phosphate triesters found to be substrates are synthetic compounds. The identity of any naturally occurring substrate for the enzyme is unknown. Has no detectable activity with phosphate monoesters or diesters and no activity as an esterase or protease. It catalyzes the hydrolysis of the insecticide paraoxon at a rate approaching the diffusion limit and thus appears to be optimally evolved for utilizing this synthetic substrate (By similarity).
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Cell membrane
Gene sequence
>lcl|BSEQ0003047|1098 bp
ATGCAAACGAGAAGGGTTGTGCTCAAGTCTGCGGCCGCCGCAGGAACTCTGCTCGGCGGC
CTGGCTGGGTGCGCGAGCGTGGCTGGATCGATCGGCACAGGCGATCGGATCAATACCGTG
CGCGGTCCTATCACAATCTCTGAAGCGGGTTTCACACTGACTCACGAGCACATCTGCGGC
AGCTCGGCAGGATTCTTGCGTGCTTGGCCAGAGTTCTTCGGTAGCCGCAAAGCTCTAGCG
GAAAAGGCTGTGAGAGGATTGCGCCGCGCCAGAGCGGCTGGCGTGCGAACGATTGTCGAT
GTGTCGACTTTCGATATCGGTCGCGACGTCAGTTTATTGGCCGAGGTTTCGCGGGCTGCC
GACGTTCATATCGTGGCGGCGACCGGCTTGTGGTTCGACCCGCCACTTTCGATGCGATTG
AGGAGTGTAGAGGAACTCACACAGTTCTTCCTGCGTGAGATTCAATATGGCATCGAAGAC
ACCGGAATTAGGGCGGGCATTATCAAGGTCGCGACCACAGGCAAGGCGACCCCCTTTCAG
GAGTTAGTGTTAAAGGCGGCCGCCCGGGCCAGCTTGGCCACCGGTGTTCCGGTAACCACT
CACACGGCAGCAAGTCAGCGCGATGGTGAGCAGCAGGCCGCCATTTTTGAGTCCGAAGGC
TTGAGCCCCTCACGGGTTTGTATTGGTCACAGCGATGATACTGACGATTTGAGCTATCTC
ACCGCCCTCGCTGCGCGCGGATACCTCATCGGTCTAGACCACATCCCGCACAGTGCGATT
GGTCTAGAAGATAATGCGAGTGCATCAGCCCTCCTGGGCATCCGTTCGTGGCAAACACGG
GCTCTCTTGATCAAGGCGCTCATCGACCAAGGCTACATGAAACAAATCCTCGTTTCGAAT
GACTGGCTGTTCGGGTTTTCGAGCTATGTCACCAACATCATGGACGTGATGGATCGCGTG
AACCCCGACGGGATGGCCTTCATTCCACTGAGAGTGATCCCATTCCTACGAGAGAAGGGC
GTCCCACAGGAAACGCTGGCAGGCATCACTGTGACTAACCCGGCGCGGTTCTTGTCACCG
ACCTTGCGGGCGTCATGA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP0A433
UniProtKB Entry NameOPD_SPHSA
GenBank Protein ID148713
GenBank Gene IDM29593
General References
  1. Mulbry WW, Karns JS: Parathion hydrolase specified by the Flavobacterium opd gene: relationship between the gene and protein. J Bacteriol. 1989 Dec;171(12):6740-6. [PubMed:2556372]
  2. Hill CM, Li WS, Thoden JB, Holden HM, Raushel FM: Enhanced degradation of chemical warfare agents through molecular engineering of the phosphotriesterase active site. J Am Chem Soc. 2003 Jul 30;125(30):8990-1. [PubMed:15369336]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB02127Diisopropyl methylphosphonateexperimentalunknownDetails
DB02138Diethyl 4-MethylbenzylphosphonateexperimentalunknownDetails
DB02192Phenylethyl alcoholexperimentalunknownDetails
DB02437(5r)-5-Amino-6-Hydroxyhexylcarbamic AcidexperimentalunknownDetails
DB03347Triethyl phosphateexperimentalunknownDetails
DB03801Lysine Nz-Carboxylic AcidexperimentalunknownDetails
DB03822Ethyl dihydrogen phosphateexperimentalunknownDetails