Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q7SIG4

- DFPA_LOLVU

UniProt

Q7SIG4 - DFPA_LOLVU

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Diisopropyl-fluorophosphatase

Gene
N/A
Organism
Loligo vulgaris (Common European squid)
Status
Reviewed - 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

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

Vmax=130 µmol/min/mg enzyme (in the presence of 10 mM NaCl)1 Publication

Vmax=170 µmol/min/mg enzyme (in the presence of 100 mM NaCl)1 Publication

Vmax=307 µmol/min/mg enzyme (in the presence of 200 mM NaCl)1 Publication

Vmax=326 µmol/min/mg enzyme (in the presence of 500 mM NaCl)1 Publication

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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi21 – 211Calcium 1; catalyticCurated
Metal bindingi120 – 1201Calcium 1; catalyticCurated
Metal bindingi175 – 1751Calcium 1; catalyticCurated
Metal bindingi229 – 2291Calcium 1; catalyticCurated
Metal bindingi232 – 2321Calcium 22 Publications
Metal bindingi273 – 2731Calcium 2; via carbonyl oxygen2 Publications
Metal bindingi274 – 2741Calcium 22 Publications
Active sitei287 – 2871Proton acceptor1 Publication

GO - Molecular functioni

  1. calcium ion binding Source: UniProtKB
  2. diisopropyl-fluorophosphatase activity Source: UniProtKB

GO - Biological processi

  1. metabolic process Source: GOC
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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi21 – 211E → Q: 100% decrease in activity. Loss of calcium 1 binding. 1 Publication
Mutagenesisi37 – 371E → Q: 50% decrease in activity. 1 Publication
Mutagenesisi77 – 771Q → F: 100% decrease in activity. 1 Publication
Mutagenesisi77 – 771Q → W: No effect on activity. 1 Publication
Mutagenesisi77 – 771Q → Y: 6% increase in activity. 1 Publication
Mutagenesisi120 – 1201N → D: 96% decrease in activity. 100% decrease in activity; when associated with N-229. 1 Publication
Mutagenesisi121 – 1211D → F: 100% decrease in activity. 1 Publication
Mutagenesisi144 – 1441Y → S: 8% increase in activity. 1 Publication
Mutagenesisi146 – 1461R → S: 45% decrease in activity. 1 Publication
Mutagenesisi148 – 1481M → A: 26% decrease in activity. 1 Publication
Mutagenesisi173 – 1731F → A: 84% decrease in activity. 1 Publication
Mutagenesisi173 – 1731F → L: 28% decrease in activity. 1 Publication
Mutagenesisi173 – 1731F → S: 68% decrease in activity. 1 Publication
Mutagenesisi173 – 1731F → V: 46% decrease in activity. 1 Publication
Mutagenesisi173 – 1731F → W: 19% decrease in activity. 1 Publication
Mutagenesisi173 – 1731F → Y: 53% decrease in activity. 1 Publication
Mutagenesisi175 – 1751N → D: 98% decrease in activity. 1 Publication
Mutagenesisi181 – 1811H → N: 20% decrease in activity. 2 Publications
Mutagenesisi195 – 1951T → A: 60% decrease in activity. 1 Publication
Mutagenesisi195 – 1951T → L: 11% decrease in activity. 1 Publication
Mutagenesisi195 – 1951T → V: 3% decrease in activity. 1 Publication
Mutagenesisi219 – 2191H → N: 3% increase in activity. 1 Publication
Mutagenesisi224 – 2241H → N: 14% increase in activity. 1 Publication
Mutagenesisi229 – 2291D → N: 100% decrease in activity. Loss of calcium 1 binding. 100% decrease in activity; when associated with D-120. 2 Publications
Mutagenesisi232 – 2321D → S: 3% increase in activity. 19% decrease in activity; when associated with A-271. 1 Publication
Mutagenesisi237 – 2371N → S: 4% decrease in activity. 1 Publication
Mutagenesisi244 – 2441W → F: 44% decrease in activity. 1 Publication
Mutagenesisi244 – 2441W → H: 27% decrease in activity. 1 Publication
Mutagenesisi244 – 2441W → L: 62% decrease in activity. 1 Publication
Mutagenesisi244 – 2441W → Y: No effect on activity. 1 Publication
Mutagenesisi248 – 2481H → N: 4% increase in activity. 1 Publication
Mutagenesisi271 – 2711S → A: 30% increase in activity. 19% decrease in activity; when associated with S-232. 2 Publications
Mutagenesisi272 – 2721N → F: 100% decrease in activity. 1 Publication
Mutagenesisi274 – 2741H → N: 85% decrease in activity. 2 Publications
Mutagenesisi287 – 2871H → A: 90% decrease in activity. 2 Publications
Mutagenesisi287 – 2871H → F: 36% decrease in activity. 2 Publications
Mutagenesisi287 – 2871H → L: 21% decrease in activity. 2 Publications
Mutagenesisi287 – 2871H → N: 97% decrease in activity. 2 Publications
Mutagenesisi287 – 2871H → Q: 54% decrease in activity. 2 Publications
Mutagenesisi287 – 2871H → W: 44% decrease in activity. 2 Publications
Mutagenesisi287 – 2871H → Y: 57% decrease in activity. 2 Publications
Mutagenesisi304 – 3041Q → F: 50% decrease in activity. 1 Publication
Mutagenesisi304 – 3041Q → W: 3% decrease in activity. 1 Publication
Mutagenesisi314 – 3141F → A: 3% increase in activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 314314Diisopropyl-fluorophosphatasePRO_0000248834Add
BLAST

Interactioni

Subunit structurei

Monomer.2 Publications

Structurei

Secondary structure

1
314
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi11 – 144
Beta strandi21 – 255
Beta strandi31 – 355
Helixi36 – 416
Beta strandi47 – 515
Turni53 – 553
Beta strandi58 – 625
Beta strandi73 – 786
Beta strandi80 – 8910
Turni90 – 923
Beta strandi93 – 986
Turni99 – 1013
Beta strandi103 – 1053
Beta strandi121 – 1244
Beta strandi130 – 1345
Beta strandi136 – 1383
Beta strandi149 – 1513
Beta strandi153 – 1586
Beta strandi164 – 18118
Beta strandi187 – 1948
Turni195 – 1984
Beta strandi199 – 2079
Beta strandi210 – 21910
Beta strandi223 – 2253
Beta strandi227 – 2348
Beta strandi239 – 2446
Turni245 – 2473
Beta strandi248 – 2525
Beta strandi260 – 2645
Beta strandi266 – 2683
Beta strandi270 – 2756
Beta strandi279 – 2868
Turni287 – 2904
Beta strandi291 – 2966
Helixi305 – 3073
Beta strandi310 – 3123

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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. Positions 1-314.
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:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1E1A X-ray 1.80 A 1-314 [» ]
1PJX X-ray 0.85 A 1-314 [» ]
2GVU X-ray 2.00 A 1-314 [» ]
2GVV X-ray 1.73 A 1-314 [» ]
2GVW X-ray 1.86 A 1-314 [» ]
2GVX X-ray 2.00 A 1-314 [» ]
2IAO X-ray 2.00 A 3-314 [» ]
2IAP X-ray 1.90 A 3-314 [» ]
2IAQ X-ray 2.10 A 3-314 [» ]
2IAR X-ray 1.90 A 3-314 [» ]
2IAS X-ray 2.00 A 3-314 [» ]
2IAT X-ray 1.90 A 3-314 [» ]
2IAU X-ray 2.00 A 3-314 [» ]
2IAV X-ray 1.07 A 3-314 [» ]
2IAW X-ray 1.74 A 3-314 [» ]
2IAX X-ray 1.10 A 3-314 [» ]
3BYC X-ray 2.20 A 1-314 [» ]
3HLH X-ray 1.80 A/B/C/D 1-314 [» ]
3HLI X-ray 1.40 A/B/C/D 1-314 [» ]
3I1C X-ray 2.20 A 1-314 [» ]
3KGG X-ray 2.10 A 1-314 [» ]
3LI3 X-ray 1.66 A 1-314 [» ]
3LI4 X-ray 1.35 A 1-314 [» ]
3LI5 X-ray 1.36 A 1-314 [» ]
3O4P X-ray 0.85 A 1-314 [» ]
3U0S X-ray 2.60 A/B 1-314 [» ]
4O5S X-ray 1.80 A/B 1-314 [» ]
4O5T X-ray 2.90 A/B 1-314 [» ]
ProteinModelPortali Q7SIG4.
SMRi Q7SIG4. Positions 1-314.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

BRENDAi 3.1.8.2. 3066.
SABIO-RK Q7SIG4.

Miscellaneous databases

EvolutionaryTracei Q7SIG4.

Family and domain databases

Gene3Di 2.120.10.30. 1 hit.
InterProi IPR011042. 6-blade_b-propeller_TolB-like.
IPR013658. SGL.
[Graphical view ]
Pfami PF08450. SGL. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Insights into the reaction mechanism of the diisopropyl fluorophosphatase from Loligo vulgaris by means of kinetic studies, chemical modification and site-directed mutagenesis."
    Hartleib J., Rueterjans H.
    Biochim. Biophys. Acta 1546:312-324(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF HIS-181; HIS-219; HIS-224; HIS-248; HIS-274 AND HIS-287.
  2. "Role of calcium ions in the structure and function of the di-isopropylfluorophosphatase from Loligo vulgaris."
    Hartleib J., Geschwindner S., Scharff E.I., Rueterjans H.
    Biochem. J. 353:579-589(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, COFACTOR, ENZYME REGULATION.
  3. "Mutational and structural studies of the diisopropylfluorophosphatase from Loligo vulgaris shed new light on the catalytic mechanism of the enzyme."
    Katsemi V., Luecke C., Koepke J., Lohr F., Maurer S., Fritzsch G., Rueterjans H.
    Biochemistry 44:9022-9033(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF GLN-77; ASN-120; ASP-121; TYR-144; ARG-146; MET-148; PHE-173; ASN-175; HIS-181; THR-195; ASP-229; ASP-232; ASN-237; SER-271; ASN-272; HIS-274; HIS-287; GLN-304 AND PHE-314.
  4. "Crystallization and preliminary X-ray crystallographic analysis of DFPase from Loligo vulgaris."
    Scharff E.I., Lucke C., Fritzsch G., Koepke J., Hartleib J., Dierl S., Rueterjans H.
    Acta Crystallogr. D 57:148-149(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: CRYSTALLIZATION, X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), BIOTECHNOLOGY.
  5. "Crystal structure of diisopropylfluorophosphatase from Loligo vulgaris."
    Scharff E.I., Koepke J., Fritzsch G., Lucke C., Rueterjans H.
    Structure 9:493-502(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), COFACTOR, SUBUNIT, MUTAGENESIS OF GLU-21; GLU-37; ASP-229; TRP-244 AND SER-271.
  6. "Statistical analysis of crystallographic data obtained from squid ganglion DFPase at 0.85 A resolution."
    Koepke J., Scharff E.I., Lucke C., Rueterjans H., Fritzsch G.
    Acta Crystallogr. D 59:1744-1754(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (0.85 ANGSTROMS), COFACTOR, SUBUNIT.

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: October 1, 2014
This is version 52 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

External Data

Dasty 3