Parathion hydrolase


NameParathion hydrolase
Synonyms
  • 3.1.8.1
  • Phosphotriesterase
  • PTE
Gene Nameopd
OrganismFlavobacterium sp. (strain ATCC 27551)
Amino acid sequence
>lcl|BSEQ0011087|Parathion hydrolase
MQTRRVVLKSAAAAGTLLGGLAGCASVAGSIGTGDRINTVRGPITISEAGFTLTHEHICG
SSAGFLRAWPEFFGSRKALAEKAVRGLRRARAAGVRTIVDVSTFDIGRDVSLLAEVSRAA
DVHIVAATGLWFDPPLSMRLRSVEELTQFFLREIQYGIEDTGIRAGIIKVATTGKATPFQ
ELVLKAAARASLATGVPVTTHTAASQRDGEQQAAIFESEGLSPSRVCIGHSDDTDDLSYL
TALAARGYLIGLDHIPHSAIGLEDNASASALLGIRSWQTRALLIKALIDQGYMKQILVSN
DWLFGFSSYVTNIMDVMDRVNPDGMAFIPLRVIPFLREKGVPQETLAGITVTNPARFLSP
TLRAS
Number of residuesNone
Molecular Weight39003.24
Theoretical pI8.48
GO Classification
Functions
  • zinc ion binding
  • aryldialkylphosphatase activity
Processes
  • catabolic process
Components
  • plasma membrane
General FunctionZinc ion binding
Specific FunctionHas 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).
Transmembrane Regions
GenBank Protein ID
UniProtKB IDP0A433
UniProtKB Entry Name
Cellular LocationCell 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
GenBank Gene ID
GeneCard IDNone
GenAtlas ID
HGNC ID
Chromosome LocationNone
LocusNone
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. [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. [15369336 ]

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