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Q44238

- PEPQ_ALTSX

UniProt

Q44238 - PEPQ_ALTSX

Protein

Xaa-Pro dipeptidase

Gene

pepQ

Organism
Alteromonas sp.
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 71 (01 Oct 2014)
      Sequence version 3 (15 Jan 2008)
      Previous versions | rss
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    Functioni

    Splits dipeptides with a prolyl or hydroxyprolyl residue in the C-terminal position and a nonpolar amino acid at the N-terminal position. Also catalyzes the hydrolysis of toxic organophosphorus cholinesterase-inhibiting compounds including insecticide paraoxon and nerve gases such as diisopropylfluorophosphate (DFP), O-isopropyl methylphosphonofluoridate (sarin), O-pinacolyl methylphosphonofluoridate (soman), and O-cyclohexyl methylphosphonofluoridate.4 Publications

    Catalytic activityi

    Hydrolysis of Xaa-|-Pro dipeptides; also acts on aminoacyl-hydroxyproline analogs. No action on Pro-|-Pro.
    Diisopropyl fluorophosphate + H2O = diisopropyl phosphate + fluoride.
    An aryl dialkyl phosphate + H2O = dialkyl phosphate + an aryl alcohol.

    Cofactori

    Binds 2 manganese ions per monomer.1 Publication

    Kineticsi

    1. KM=2.99 mM for diisopropylfluorophosphate2 Publications
    2. KM=1.57 mM for O-isopropyl methylphosphonofluoridate2 Publications
    3. KM=2.48 mM for O-pinacolyl methylphosphonofluoridate2 Publications
    4. KM=0.63 mM for O-cyclohexyl methylphosphonofluoridate2 Publications
    5. KM=1.27 mM for a chromogenic soman analog2 Publications

    Vmax=230 µmol/min/mg enzyme with diisopropylfluorophosphate as substrate2 Publications

    Vmax=442 µmol/min/mg enzyme with O-isopropyl methylphosphonofluoridate as substrate2 Publications

    Vmax=151 µmol/min/mg enzyme with O-pinacolyl methylphosphonofluoridate as substrate2 Publications

    Vmax=652 µmol/min/mg enzyme with O-cyclohexyl methylphosphonofluoridate as substrate2 Publications

    Vmax=52 µmol/min/mg enzyme with a chromogenic soman analog as substrate2 Publications

    pH dependencei

    Optimum pH is 8.5 with DFP as substrate.2 Publications

    Temperature dependencei

    Optimum temperature is 50 degrees Celsius.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi244 – 2441Manganese 2By similarity
    Metal bindingi255 – 2551Manganese 1By similarity
    Metal bindingi255 – 2551Manganese 2By similarity
    Metal bindingi336 – 3361Manganese 1By similarity
    Metal bindingi381 – 3811Manganese 1By similarity
    Metal bindingi420 – 4201Manganese 1By similarity
    Metal bindingi420 – 4201Manganese 2By similarity

    GO - Molecular functioni

    1. aryldialkylphosphatase activity Source: UniProtKB-EC
    2. diisopropyl-fluorophosphatase activity Source: UniProtKB-EC
    3. dipeptidase activity Source: UniProtKB-HAMAP
    4. metal ion binding Source: UniProtKB-KW
    5. metalloexopeptidase activity Source: UniProtKB-HAMAP

    GO - Biological processi

    1. response to toxic substance Source: UniProtKB-KW

    Keywords - Molecular functioni

    Dipeptidase, Hydrolase, Metalloprotease, Protease

    Keywords - Biological processi

    Detoxification

    Keywords - Ligandi

    Manganese, Metal-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-7712.

    Protein family/group databases

    MEROPSiM24.003.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Xaa-Pro dipeptidase (EC:3.4.13.9)
    Short name:
    X-Pro dipeptidase
    Alternative name(s):
    DFPase
    Imidodipeptidase
    Organophosphorus acid anhydrolase 2 (EC:3.1.8.2)
    Short name:
    OPAA-2
    Paraoxon hydrolase
    Phosphotriesterase (EC:3.1.8.1)
    Proline dipeptidase
    Short name:
    Prolidase
    Gene namesi
    Name:pepQ
    Synonyms:opaA
    OrganismiAlteromonas sp.
    Taxonomic identifieri232 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesAlteromonadaceaeAlteromonas

    Pathology & Biotechi

    Biotechnological usei

    Can be used for the catalytic detoxification of some nerve agents neurotoxins.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 517517Xaa-Pro dipeptidasePRO_0000298944Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Structurei

    Secondary structure

    1
    517
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi3 – 2523
    Beta strandi29 – 346
    Helixi54 – 574
    Beta strandi69 – 724
    Beta strandi74 – 763
    Beta strandi79 – 835
    Beta strandi88 – 903
    Helixi99 – 1035
    Beta strandi104 – 1118
    Helixi112 – 1143
    Helixi116 – 1183
    Helixi123 – 1253
    Beta strandi126 – 1316
    Helixi133 – 1397
    Beta strandi143 – 1453
    Helixi147 – 15711
    Helixi162 – 18726
    Helixi192 – 20312
    Helixi207 – 2093
    Beta strandi210 – 2123
    Beta strandi215 – 2184
    Helixi219 – 2235
    Beta strandi240 – 24910
    Beta strandi252 – 26413
    Helixi267 – 28317
    Helixi292 – 30918
    Beta strandi312 – 3154
    Helixi317 – 3226
    Helixi326 – 3283
    Beta strandi339 – 3435
    Beta strandi376 – 3805
    Beta strandi383 – 3853
    Helixi388 – 3958
    Helixi398 – 4025
    Helixi405 – 4117
    Helixi412 – 4143
    Beta strandi416 – 4183
    Beta strandi420 – 4256
    Beta strandi430 – 4323
    Helixi433 – 4364

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3L24X-ray2.30A/B/C1-517[»]
    3L7GX-ray2.70A/B/C1-517[»]
    ProteinModelPortaliQ44238.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ44238.

    Family & Domainsi

    Sequence similaritiesi

    Family and domain databases

    Gene3Di3.90.230.10. 1 hit.
    HAMAPiMF_01279. X_Pro_dipeptid.
    InterProiIPR000994. Pept_M24_structural-domain.
    IPR001131. Peptidase_M24B_aminopep-P_CS.
    IPR022846. X_Pro_dipept.
    [Graphical view]
    PfamiPF00557. Peptidase_M24. 1 hit.
    [Graphical view]
    SUPFAMiSSF55920. SSF55920. 1 hit.
    PROSITEiPS00491. PROLINE_PEPTIDASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q44238-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNKLAVLYAE HIATLQKRTR EIIERENLDG VVFHSGQAKR QFLDDMYYPF    50
    KVNPQFKAWL PVIDNPHCWI VANGTDKPKL IFYRPVDFWH KVPDEPNEYW 100
    ADYFDIELLV KPDQVEKLLP YDKARFAYIG EYLEVAQALG FELMNPEPVM 150
    NFYHYHRAYK TQYELACMRE ANKIAVQGHK AARDAFFQGK SEFEIQQAYL 200
    LATQHSENDN AYGNIVALNE NCAILHYTHF DRVAPATHRS FLIDAGANFN 250
    GYAADITRTY DFTGEGEFAE LVATMKQHQI ALCNQLAPGK LYGELHLDCH 300
    QRVAQTLSDF NIVDLSADEI VAKGITSTFF PHGLGHHIGL QVHDVGGFMA 350
    DEQGAHQEPP EGHPFLRCTR KIEANQVFTI EPGLYFIDSL LGDLAATDNN 400
    QHINWDKVAE LKPFGGIRIE DNIIVHEDSL ENMTRELRAR LTTHSLRGLS 450
    APQFSINDPA VMSEYSYPSE PLSYEEEIKK STFIVHVRTR RILVRRRTLS 500
    PILIAVTPMP AITAGLM 517
    Length:517
    Mass (Da):58,998
    Last modified:January 15, 2008 - v3
    Checksum:i9B92D811445C72A3
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U29240 Genomic DNA. Translation: AAB05590.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U29240 Genomic DNA. Translation: AAB05590.1 .

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3L24 X-ray 2.30 A/B/C 1-517 [» ]
    3L7G X-ray 2.70 A/B/C 1-517 [» ]
    ProteinModelPortali Q44238.
    ModBasei Search...
    MobiDBi Search...

    Chemistry

    ChEMBLi CHEMBL4252.

    Protein family/group databases

    MEROPSi M24.003.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    BioCyci MetaCyc:MONOMER-7712.

    Miscellaneous databases

    EvolutionaryTracei Q44238.

    Family and domain databases

    Gene3Di 3.90.230.10. 1 hit.
    HAMAPi MF_01279. X_Pro_dipeptid.
    InterProi IPR000994. Pept_M24_structural-domain.
    IPR001131. Peptidase_M24B_aminopep-P_CS.
    IPR022846. X_Pro_dipept.
    [Graphical view ]
    Pfami PF00557. Peptidase_M24. 1 hit.
    [Graphical view ]
    SUPFAMi SSF55920. SSF55920. 1 hit.
    PROSITEi PS00491. PROLINE_PEPTIDASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and expression of a gene encoding a bacterial enzyme for decontamination of organophosphorus nerve agents and nucleotide sequence of the enzyme."
      Cheng T.-C., Harvey S.P., Chen G.L.
      Appl. Environ. Microbiol. 62:1636-1641(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES.
      Strain: JD6.5.
    2. "Purification and properties of an organophosphorus acid anhydrase from a halophilic bacterial isolate."
      DeFrank J.J., Cheng T.-C.
      J. Bacteriol. 173:1938-1943(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES.
      Strain: JD6.5.
    3. "Nucleotide sequence of a gene encoding an organophosphorus nerve agent degrading enzyme from Alteromonas haloplanktis."
      Cheng T.-C., Liu L., Wang B., Wu J., DeFrank J.J., Anderson D.M., Rastogi V.K., Hamilton A.B.
      J. Ind. Microbiol. Biotechnol. 18:49-55(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
      Strain: JD6.5.
    4. "Substrate and stereochemical specificity of the organophosphorus acid anhydrolase from Alteromonas sp. JD6.5 toward p-nitrophenyl phosphotriesters."
      Hill C.M., Wu F., Cheng T.-C., DeFrank J.J., Raushel F.M.
      Bioorg. Med. Chem. Lett. 10:1285-1288(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBSTRATE SPECIFICITY, STEREOSELECTIVITY.
      Strain: JD6.5.
    5. "Stereochemical specificity of organophosphorus acid anhydrolase toward p-nitrophenyl analogs of soman and sarin."
      Hill C.M., Li W.-S., Cheng T.-C., DeFrank J.J., Raushel F.M.
      Bioorg. Chem. 29:27-35(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: STEREOSELECTIVITY.

    Entry informationi

    Entry nameiPEPQ_ALTSX
    AccessioniPrimary (citable) accession number: Q44238
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 21, 2007
    Last sequence update: January 15, 2008
    Last modified: October 1, 2014
    This is version 71 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Has a stereoselective preference for isomers with R-configuration at the phosphorous center of sarin and soman, and with S-configuration in phosphotriesters.

    Keywords - Technical termi

    3D-structure

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. Peptidase families
      Classification of peptidase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3