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Q7SIG4

- DFPA_LOLVU

UniProt

Q7SIG4 - DFPA_LOLVU

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
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    • History
      Entry version 52 (01 Oct 2014)
      Sequence version 1 (15 Dec 2003)
      Previous versions | rss
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    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

    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

    MEIPVIEPLF TKVTEDIPGA EGPVFDKNGD FYIVAPEVEV NGKPAGEILR    50
    IDLKTGKKTV ICKPEVNGYG GIPAGCQCDR DANQLFVADM RLGLLVVQTD 100
    GTFEEIAKKD SEGRRMQGCN DCAFDYEGNL WITAPAGEVA PADYTRSMQE 150
    KFGSIYCFTT DGQMIQVDTA FQFPNGIAVR HMNDGRPYQL IVAETPTKKL 200
    WSYDIKGPAK IENKKVWGHI PGTHEGGADG MDFDEDNNLL VANWGSSHIE 250
    VFGPDGGQPK MRIRCPFEKP SNLHFKPQTK TIFVTEHENN AVWKFEWQRN 300
    GKKQYCETLK FGIF 314
    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