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Protein

Diisopropyl-fluorophosphatase

Gene
N/A
Organism
Loligo vulgaris (Common European squid)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Biological function and substrate unknown. However, it is capable of acting on phosphorus anhydride bonds (such as phosphorus-halide and phosphorus-cyanide) in organophosphorus compounds (including nerve gases).1 Publication

Catalytic activityi

Diisopropyl fluorophosphate + H2O = diisopropyl phosphate + fluoride.2 Publications

Cofactori

Ca2+3 PublicationsNote: Binds 2 calcium ions per subunit.3 Publications

Enzyme regulationi

Inhibited by chelating agents.1 Publication

Kineticsi

  1. KM=0.54 mM for diisopropyl-fluorophosphate (in the presence of 10 mM NaCl)1 Publication
  2. KM=0.42 mM for diisopropyl-fluorophosphate (in the presence of 100 mM NaCl)1 Publication
  3. KM=0.34 mM for diisopropyl-fluorophosphate (in the presence of 200 mM NaCl)1 Publication
  4. KM=0.25 mM for diisopropyl-fluorophosphate (in the presence of 500 mM NaCl)1 Publication
  5. KM=0.17 mM for diisopropyl-fluorophosphate (in the presence of 1000 mM NaCl)1 Publication
  1. Vmax=130 µmol/min/mg enzyme (in the presence of 10 mM NaCl)1 Publication
  2. Vmax=170 µmol/min/mg enzyme (in the presence of 100 mM NaCl)1 Publication
  3. Vmax=307 µmol/min/mg enzyme (in the presence of 200 mM NaCl)1 Publication
  4. Vmax=326 µmol/min/mg enzyme (in the presence of 500 mM NaCl)1 Publication
  5. Vmax=214 µmol/min/mg enzyme (in the presence of 1000 mM NaCl)1 Publication

pH dependencei

Optimum pH is 8.0.1 Publication

Temperature dependencei

Optimum temperature is 35 degrees Celsius.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi21Calcium 1; catalyticCurated1
Metal bindingi120Calcium 1; catalyticCurated1
Metal bindingi175Calcium 1; catalyticCurated1
Metal bindingi229Calcium 1; catalyticCurated1
Metal bindingi232Calcium 22 Publications1
Metal bindingi273Calcium 2; via carbonyl oxygen2 Publications1
Metal bindingi274Calcium 22 Publications1
Active sitei287Proton acceptor1 Publication1

GO - Molecular functioni

  • calcium ion binding Source: UniProtKB
  • diisopropyl-fluorophosphatase activity Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

BRENDAi3.1.8.2. 3066.
SABIO-RKQ7SIG4.

Names & Taxonomyi

Protein namesi
Recommended name:
Diisopropyl-fluorophosphatase (EC:3.1.8.2)
Short name:
DFPase
OrganismiLoligo vulgaris (Common European squid)
Taxonomic identifieri6622 [NCBI]
Taxonomic lineageiEukaryotaMetazoaLophotrochozoaMolluscaCephalopodaColeoideaNeocoleoideaDecapodiformesTeuthidaMyopsinaLoliginidaeLoligo

Pathology & Biotechi

Biotechnological usei

Has potential application in bio-remediation by detoxification of organo-phosphates used in insecticides or nerve agents used in chemical warfare such as soman, tabun and sarin.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi21E → Q: 100% decrease in activity. Loss of calcium 1 binding. 1 Publication1
Mutagenesisi37E → Q: 50% decrease in activity. 1 Publication1
Mutagenesisi77Q → F: 100% decrease in activity. 1 Publication1
Mutagenesisi77Q → W: No effect on activity. 1 Publication1
Mutagenesisi77Q → Y: 6% increase in activity. 1 Publication1
Mutagenesisi120N → D: 96% decrease in activity. 100% decrease in activity; when associated with N-229. 1 Publication1
Mutagenesisi121D → F: 100% decrease in activity. 1 Publication1
Mutagenesisi144Y → S: 8% increase in activity. 1 Publication1
Mutagenesisi146R → S: 45% decrease in activity. 1 Publication1
Mutagenesisi148M → A: 26% decrease in activity. 1 Publication1
Mutagenesisi173F → A: 84% decrease in activity. 1 Publication1
Mutagenesisi173F → L: 28% decrease in activity. 1 Publication1
Mutagenesisi173F → S: 68% decrease in activity. 1 Publication1
Mutagenesisi173F → V: 46% decrease in activity. 1 Publication1
Mutagenesisi173F → W: 19% decrease in activity. 1 Publication1
Mutagenesisi173F → Y: 53% decrease in activity. 1 Publication1
Mutagenesisi175N → D: 98% decrease in activity. 1 Publication1
Mutagenesisi181H → N: 20% decrease in activity. 2 Publications1
Mutagenesisi195T → A: 60% decrease in activity. 1 Publication1
Mutagenesisi195T → L: 11% decrease in activity. 1 Publication1
Mutagenesisi195T → V: 3% decrease in activity. 1 Publication1
Mutagenesisi219H → N: 3% increase in activity. 1 Publication1
Mutagenesisi224H → N: 14% increase in activity. 1 Publication1
Mutagenesisi229D → N: 100% decrease in activity. Loss of calcium 1 binding. 100% decrease in activity; when associated with D-120. 2 Publications1
Mutagenesisi232D → S: 3% increase in activity. 19% decrease in activity; when associated with A-271. 1 Publication1
Mutagenesisi237N → S: 4% decrease in activity. 1 Publication1
Mutagenesisi244W → F: 44% decrease in activity. 1 Publication1
Mutagenesisi244W → H: 27% decrease in activity. 1 Publication1
Mutagenesisi244W → L: 62% decrease in activity. 1 Publication1
Mutagenesisi244W → Y: No effect on activity. 1 Publication1
Mutagenesisi248H → N: 4% increase in activity. 1 Publication1
Mutagenesisi271S → A: 30% increase in activity. 19% decrease in activity; when associated with S-232. 2 Publications1
Mutagenesisi272N → F: 100% decrease in activity. 1 Publication1
Mutagenesisi274H → N: 85% decrease in activity. 2 Publications1
Mutagenesisi287H → A: 90% decrease in activity. 2 Publications1
Mutagenesisi287H → F: 36% decrease in activity. 2 Publications1
Mutagenesisi287H → L: 21% decrease in activity. 2 Publications1
Mutagenesisi287H → N: 97% decrease in activity. 2 Publications1
Mutagenesisi287H → Q: 54% decrease in activity. 2 Publications1
Mutagenesisi287H → W: 44% decrease in activity. 2 Publications1
Mutagenesisi287H → Y: 57% decrease in activity. 2 Publications1
Mutagenesisi304Q → F: 50% decrease in activity. 1 Publication1
Mutagenesisi304Q → W: 3% decrease in activity. 1 Publication1
Mutagenesisi314F → A: 3% increase in activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002488341 – 314Diisopropyl-fluorophosphataseAdd BLAST314

Interactioni

Subunit structurei

Monomer.2 Publications

Structurei

Secondary structure

1314
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi11 – 14Combined sources4
Beta strandi21 – 25Combined sources5
Beta strandi31 – 35Combined sources5
Helixi37 – 44Combined sources8
Beta strandi47 – 51Combined sources5
Turni53 – 55Combined sources3
Beta strandi58 – 62Combined sources5
Beta strandi73 – 78Combined sources6
Beta strandi80 – 89Combined sources10
Turni90 – 92Combined sources3
Beta strandi93 – 98Combined sources6
Turni99 – 101Combined sources3
Beta strandi103 – 105Combined sources3
Beta strandi121 – 124Combined sources4
Beta strandi130 – 134Combined sources5
Beta strandi136 – 138Combined sources3
Beta strandi149 – 151Combined sources3
Beta strandi153 – 158Combined sources6
Beta strandi164 – 181Combined sources18
Beta strandi187 – 194Combined sources8
Turni195 – 198Combined sources4
Beta strandi199 – 207Combined sources9
Beta strandi210 – 219Combined sources10
Beta strandi223 – 225Combined sources3
Beta strandi227 – 234Combined sources8
Beta strandi239 – 244Combined sources6
Turni245 – 247Combined sources3
Beta strandi248 – 252Combined sources5
Beta strandi260 – 264Combined sources5
Beta strandi266 – 268Combined sources3
Beta strandi270 – 275Combined sources6
Beta strandi279 – 286Combined sources8
Turni287 – 290Combined sources4
Beta strandi291 – 296Combined sources6
Helixi305 – 307Combined sources3
Beta strandi310 – 312Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1E1AX-ray1.80A1-314[»]
1PJXX-ray0.85A1-314[»]
2GVUX-ray2.00A1-314[»]
2GVVX-ray1.73A1-314[»]
2GVWX-ray1.86A1-314[»]
2GVXX-ray2.00A1-314[»]
2IAOX-ray2.00A3-314[»]
2IAPX-ray1.90A3-314[»]
2IAQX-ray2.10A3-314[»]
2IARX-ray1.90A3-314[»]
2IASX-ray2.00A3-314[»]
2IATX-ray1.90A3-314[»]
2IAUX-ray2.00A3-314[»]
2IAVX-ray1.07A3-314[»]
2IAWX-ray1.74A3-314[»]
2IAXX-ray1.10A3-314[»]
3BYCX-ray2.20A1-314[»]
3HLHX-ray1.80A/B/C/D1-314[»]
3HLIX-ray1.40A/B/C/D1-314[»]
3I1CX-ray2.20A1-314[»]
3KGGX-ray2.10A1-314[»]
3LI3X-ray1.66A1-314[»]
3LI4X-ray1.35A1-314[»]
3LI5X-ray1.36A1-314[»]
3O4PX-ray0.85A1-314[»]
3U0SX-ray2.60A/B1-314[»]
4O5SX-ray1.80A/B1-314[»]
4O5TX-ray2.90A/B1-314[»]
ProteinModelPortaliQ7SIG4.
SMRiQ7SIG4.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ7SIG4.

Family & Domainsi

Family and domain databases

Gene3Di2.120.10.30. 1 hit.
InterProiIPR011042. 6-blade_b-propeller_TolB-like.
IPR013658. SGL.
[Graphical view]
PfamiPF08450. SGL. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q7SIG4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEIPVIEPLF TKVTEDIPGA EGPVFDKNGD FYIVAPEVEV NGKPAGEILR
60 70 80 90 100
IDLKTGKKTV ICKPEVNGYG GIPAGCQCDR DANQLFVADM RLGLLVVQTD
110 120 130 140 150
GTFEEIAKKD SEGRRMQGCN DCAFDYEGNL WITAPAGEVA PADYTRSMQE
160 170 180 190 200
KFGSIYCFTT DGQMIQVDTA FQFPNGIAVR HMNDGRPYQL IVAETPTKKL
210 220 230 240 250
WSYDIKGPAK IENKKVWGHI PGTHEGGADG MDFDEDNNLL VANWGSSHIE
260 270 280 290 300
VFGPDGGQPK MRIRCPFEKP SNLHFKPQTK TIFVTEHENN AVWKFEWQRN
310
GKKQYCETLK FGIF
Length:314
Mass (Da):35,080
Last modified:December 15, 2003 - v1
Checksum:i8A3F3D84002A6EA8
GO

Cross-referencesi

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1E1AX-ray1.80A1-314[»]
1PJXX-ray0.85A1-314[»]
2GVUX-ray2.00A1-314[»]
2GVVX-ray1.73A1-314[»]
2GVWX-ray1.86A1-314[»]
2GVXX-ray2.00A1-314[»]
2IAOX-ray2.00A3-314[»]
2IAPX-ray1.90A3-314[»]
2IAQX-ray2.10A3-314[»]
2IARX-ray1.90A3-314[»]
2IASX-ray2.00A3-314[»]
2IATX-ray1.90A3-314[»]
2IAUX-ray2.00A3-314[»]
2IAVX-ray1.07A3-314[»]
2IAWX-ray1.74A3-314[»]
2IAXX-ray1.10A3-314[»]
3BYCX-ray2.20A1-314[»]
3HLHX-ray1.80A/B/C/D1-314[»]
3HLIX-ray1.40A/B/C/D1-314[»]
3I1CX-ray2.20A1-314[»]
3KGGX-ray2.10A1-314[»]
3LI3X-ray1.66A1-314[»]
3LI4X-ray1.35A1-314[»]
3LI5X-ray1.36A1-314[»]
3O4PX-ray0.85A1-314[»]
3U0SX-ray2.60A/B1-314[»]
4O5SX-ray1.80A/B1-314[»]
4O5TX-ray2.90A/B1-314[»]
ProteinModelPortaliQ7SIG4.
SMRiQ7SIG4.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi3.1.8.2. 3066.
SABIO-RKQ7SIG4.

Miscellaneous databases

EvolutionaryTraceiQ7SIG4.

Family and domain databases

Gene3Di2.120.10.30. 1 hit.
InterProiIPR011042. 6-blade_b-propeller_TolB-like.
IPR013658. SGL.
[Graphical view]
PfamiPF08450. SGL. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiDFPA_LOLVU
AccessioniPrimary (citable) accession number: Q7SIG4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: December 15, 2003
Last modified: November 2, 2016
This is version 59 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

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.