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Protein

Parathion hydrolase

Gene

opd

Organism
Sphingobium fuliginis (strain ATCC 27551)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity

Catalytic activityi

An aryl dialkyl phosphate + H2O = dialkyl phosphate + an aryl alcohol.

Cofactori

Zn2+PROSITE-ProRule annotationNote: Binds 2 Zn2+ ions per subunit.PROSITE-ProRule annotation

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi55Zinc 1; via tele nitrogenCombined sources1 Publication1
Metal bindingi57Zinc 1; via tele nitrogenCombined sources1 Publication1
Metal bindingi169Zinc 1; via carbamate groupCombined sources1 Publication1
Metal bindingi169Zinc 2; via carbamate groupCombined sources1 Publication1
Metal bindingi201Zinc 2; via pros nitrogenCombined sources1 Publication1
Metal bindingi230Zinc 2; via tele nitrogenCombined sources1 Publication1
Metal bindingi301Zinc 1Combined sources1 Publication1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-3321.
BRENDAi3.1.8.1. 2302.

Names & Taxonomyi

Protein namesi
Recommended name:
Parathion hydrolase (EC:3.1.8.1)
Alternative name(s):
Phosphotriesterase
Short name:
PTE
Gene namesi
Name:opd
Encoded oniPlasmid pPDL20 Publication
OrganismiSphingobium fuliginis (strain ATCC 27551)
Taxonomic identifieri336203 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaSphingomonadalesSphingomonadaceaeSphingobium

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 29Tat-type signalPROSITE-ProRule annotation1 PublicationAdd BLAST29
ChainiPRO_000002986130 – 365Parathion hydrolaseAdd BLAST336

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei169N6-carboxylysinePROSITE-ProRule annotationCombined sources1 Publication1

Post-translational modificationi

Predicted to be exported by the Tat system. The position of the signal peptide cleavage has been experimentally proven.

Interactioni

Subunit structurei

Homodimer.By similarity

Structurei

Secondary structure

1365
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi36 – 39Combined sources4
Beta strandi42 – 45Combined sources4
Helixi46 – 48Combined sources3
Beta strandi51 – 56Combined sources6
Beta strandi58 – 60Combined sources3
Helixi65 – 68Combined sources4
Helixi70 – 73Combined sources4
Helixi76 – 92Combined sources17
Beta strandi97 – 100Combined sources4
Helixi104 – 106Combined sources3
Helixi110 – 120Combined sources11
Beta strandi123 – 125Combined sources3
Beta strandi127 – 129Combined sources3
Helixi136 – 139Combined sources4
Helixi143 – 155Combined sources13
Beta strandi167 – 171Combined sources5
Beta strandi173 – 175Combined sources3
Helixi178 – 194Combined sources17
Beta strandi198 – 201Combined sources4
Helixi204 – 206Combined sources3
Helixi208 – 218Combined sources11
Helixi223 – 225Combined sources3
Beta strandi226 – 228Combined sources3
Helixi231 – 233Combined sources3
Helixi237 – 245Combined sources9
Beta strandi249 – 252Combined sources4
Helixi266 – 272Combined sources7
Helixi277 – 289Combined sources13
Helixi293 – 295Combined sources3
Beta strandi296 – 298Combined sources3
Beta strandi304 – 306Combined sources3
Beta strandi308 – 310Combined sources3
Helixi313 – 320Combined sources8
Helixi324 – 326Combined sources3
Helixi327 – 337Combined sources11
Turni338 – 340Combined sources3
Helixi343 – 350Combined sources8
Helixi352 – 358Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1P6BX-ray1.90A/B30-365[»]
1P6CX-ray2.00A/B30-365[»]
ProteinModelPortaliP0A433.
SMRiP0A433.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A433.

Family & Domainsi

Sequence similaritiesi

Belongs to the phosphotriesterase family.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Family and domain databases

CDDicd00530. PTE. 1 hit.
InterProiIPR017947. AryldialkylPase_Zn-BS.
IPR032466. Metal_Hydrolase.
IPR001559. Phosphotriesterase.
IPR006311. TAT_signal.
[Graphical view]
PANTHERiPTHR10819. PTHR10819. 1 hit.
PfamiPF02126. PTE. 1 hit.
[Graphical view]
SUPFAMiSSF51556. SSF51556. 1 hit.
PROSITEiPS01322. PHOSPHOTRIESTERASE_1. 1 hit.
PS51347. PHOSPHOTRIESTERASE_2. 1 hit.
PS51318. TAT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0A433-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQTRRVVLKS AAAAGTLLGG LAGCASVAGS IGTGDRINTV RGPITISEAG
60 70 80 90 100
FTLTHEHICG SSAGFLRAWP EFFGSRKALA EKAVRGLRRA RAAGVRTIVD
110 120 130 140 150
VSTFDIGRDV SLLAEVSRAA DVHIVAATGL WFDPPLSMRL RSVEELTQFF
160 170 180 190 200
LREIQYGIED TGIRAGIIKV ATTGKATPFQ ELVLKAAARA SLATGVPVTT
210 220 230 240 250
HTAASQRDGE QQAAIFESEG LSPSRVCIGH SDDTDDLSYL TALAARGYLI
260 270 280 290 300
GLDHIPHSAI GLEDNASASA LLGIRSWQTR ALLIKALIDQ GYMKQILVSN
310 320 330 340 350
DWLFGFSSYV TNIMDVMDRV NPDGMAFIPL RVIPFLREKG VPQETLAGIT
360
VTNPARFLSP TLRAS
Length:365
Mass (Da):39,004
Last modified:March 15, 2005 - v1
Checksum:i41FF8E4B029B46DC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M29593 Genomic DNA. Translation: AAA24930.1.
PIRiA43720.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M29593 Genomic DNA. Translation: AAA24930.1.
PIRiA43720.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1P6BX-ray1.90A/B30-365[»]
1P6CX-ray2.00A/B30-365[»]
ProteinModelPortaliP0A433.
SMRiP0A433.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-3321.
BRENDAi3.1.8.1. 2302.

Miscellaneous databases

EvolutionaryTraceiP0A433.

Family and domain databases

CDDicd00530. PTE. 1 hit.
InterProiIPR017947. AryldialkylPase_Zn-BS.
IPR032466. Metal_Hydrolase.
IPR001559. Phosphotriesterase.
IPR006311. TAT_signal.
[Graphical view]
PANTHERiPTHR10819. PTHR10819. 1 hit.
PfamiPF02126. PTE. 1 hit.
[Graphical view]
SUPFAMiSSF51556. SSF51556. 1 hit.
PROSITEiPS01322. PHOSPHOTRIESTERASE_1. 1 hit.
PS51347. PHOSPHOTRIESTERASE_2. 1 hit.
PS51318. TAT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiOPD_SPHSA
AccessioniPrimary (citable) accession number: P0A433
Secondary accession number(s): P13739, P16648
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: March 15, 2005
Last modified: November 2, 2016
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing, Plasmid

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.