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Protein

Carboxylesterase 1

Gene

CXE1

Organism
Actinidia eriantha (Velvet vine) (Actinidia fulvicoma var. lanata)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Carboxylesterase acting on esters with varying acyl chain length.1 Publication

Catalytic activityi

A carboxylic ester + H2O = an alcohol + a carboxylate.

Kineticsi

  1. KM=33.3 µM for 4-methylumbelliferyl acetate1 Publication
  2. KM=16.7 µM for 4-methylumbelliferyl butyrate1 Publication
  3. KM=19.1 µM for 4-methylumbelliferyl heptanoate1 Publication
  4. KM=6.34 µM for 4-methylumbelliferyl octanoate1 Publication
  5. KM=0.117 µM for 4-methylumbelliferyl laureate1 Publication
  6. KM=0.024 µM for 4-methylumbelliferyl palmitate1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei169 – 1691Curated
    Active sitei276 – 2761Curated
    Active sitei306 – 3061Curated

    GO - Molecular functioni

    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase, Serine esterase

    Enzyme and pathway databases

    BRENDAi3.1.1.1. 9380.
    SABIO-RKQ0ZPV7.

    Protein family/group databases

    ESTHERiactde-CXE1. Plant_carboxylesterase.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Carboxylesterase 1 (EC:3.1.1.1)
    Short name:
    AeCXE1
    Gene namesi
    Name:CXE1
    OrganismiActinidia eriantha (Velvet vine) (Actinidia fulvicoma var. lanata)
    Taxonomic identifieri165200 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridsEricalesActinidiaceaeActinidia

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 335335Carboxylesterase 1PRO_0000403482Add
    BLAST

    Structurei

    Secondary structure

    1
    335
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni19 – 213Combined sources
    Beta strandi52 – 6110Combined sources
    Turni62 – 654Combined sources
    Beta strandi66 – 738Combined sources
    Helixi74 – 785Combined sources
    Beta strandi83 – 897Combined sources
    Turni93 – 953Combined sources
    Helixi102 – 11514Combined sources
    Beta strandi118 – 1236Combined sources
    Turni127 – 1304Combined sources
    Helixi134 – 14714Combined sources
    Helixi152 – 1576Combined sources
    Beta strandi158 – 16811Combined sources
    Helixi170 – 18314Combined sources
    Helixi186 – 1894Combined sources
    Beta strandi194 – 2018Combined sources
    Helixi211 – 2155Combined sources
    Turni216 – 2183Combined sources
    Beta strandi220 – 2223Combined sources
    Helixi224 – 23411Combined sources
    Turni244 – 2463Combined sources
    Helixi257 – 2648Combined sources
    Beta strandi267 – 2737Combined sources
    Helixi279 – 29113Combined sources
    Beta strandi295 – 3039Combined sources
    Helixi308 – 3103Combined sources
    Helixi313 – 32715Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2O7RX-ray1.40A1-335[»]
    2O7VX-ray2.30A1-335[»]
    ProteinModelPortaliQ0ZPV7.
    SMRiQ0ZPV7. Positions 18-328.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ0ZPV7.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni92 – 932Inhibitor binding
    Regioni169 – 1702Inhibitor binding

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi90 – 923Involved in the stabilization of the negatively charged intermediate by the formation of the oxyanion holeBy similarity

    Sequence similaritiesi

    Belongs to the 'GDXG' lipolytic enzyme family.Curated

    Family and domain databases

    Gene3Di3.40.50.1820. 1 hit.
    InterProiIPR029058. AB_hydrolase.
    IPR013094. AB_hydrolase_3.
    IPR002168. Lipase_GDXG_HIS_AS.
    [Graphical view]
    PfamiPF07859. Abhydrolase_3. 1 hit.
    [Graphical view]
    SUPFAMiSSF53474. SSF53474. 1 hit.
    PROSITEiPS01173. LIPASE_GDXG_HIS. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q0ZPV7-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MSNDHLETTG SSDPNTNLLK YLPIVLNPDR TITRPIQIPS TAASPDPTSS
    60 70 80 90 100
    SPVLTKDLAL NPLHNTFVRL FLPRHALYNS AKLPLVVYFH GGGFILFSAA
    110 120 130 140 150
    STIFHDFCCE MAVHAGVVIA SVDYRLAPEH RLPAAYDDAM EALQWIKDSR
    160 170 180 190 200
    DEWLTNFADF SNCFIMGESA GGNIAYHAGL RAAAVADELL PLKIKGLVLD
    210 220 230 240 250
    EPGFGGSKRT GSELRLANDS RLPTFVLDLI WELSLPMGAD RDHEYCNPTA
    260 270 280 290 300
    ESEPLYSFDK IRSLGWRVMV VGCHGDPMID RQMELAERLE KKGVDVVAQF
    310 320 330
    DVGGYHAVKL EDPEKAKQFF VILKKFVVDS CTTKL
    Length:335
    Mass (Da):37,052
    Last modified:August 22, 2006 - v1
    Checksum:iCA859F19267B8434
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    DQ279914 mRNA. Translation: ABB89013.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    DQ279914 mRNA. Translation: ABB89013.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2O7RX-ray1.40A1-335[»]
    2O7VX-ray2.30A1-335[»]
    ProteinModelPortaliQ0ZPV7.
    SMRiQ0ZPV7. Positions 18-328.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein family/group databases

    ESTHERiactde-CXE1. Plant_carboxylesterase.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Enzyme and pathway databases

    BRENDAi3.1.1.1. 9380.
    SABIO-RKQ0ZPV7.

    Miscellaneous databases

    EvolutionaryTraceiQ0ZPV7.

    Family and domain databases

    Gene3Di3.40.50.1820. 1 hit.
    InterProiIPR029058. AB_hydrolase.
    IPR013094. AB_hydrolase_3.
    IPR002168. Lipase_GDXG_HIS_AS.
    [Graphical view]
    PfamiPF07859. Abhydrolase_3. 1 hit.
    [Graphical view]
    SUPFAMiSSF53474. SSF53474. 1 hit.
    PROSITEiPS01173. LIPASE_GDXG_HIS. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    1. "Biochemical characterization and comparison of plant CXE carboxylesterases from Actinidia spp., Arabidopsis thaliana, and Malus pumila."
      Marshall S.D., Oakeshott J.G., Russell R.J., Plummer K.M., Newcomb R.D.
      Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "High-resolution crystal structure of plant carboxylesterase AeCXE1, from Actinidia eriantha, and its complex with a high-affinity inhibitor paraoxon."
      Ileperuma N.R., Marshall S.D., Squire C.J., Baker H.M., Oakeshott J.G., Russell R.J., Plummer K.M., Newcomb R.D., Baker E.N.
      Biochemistry 46:1851-1859(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) IN COMPLEX WITH INHIBITOR, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.

    Entry informationi

    Entry nameiCXE1_ACTER
    AccessioniPrimary (citable) accession number: Q0ZPV7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 11, 2011
    Last sequence update: August 22, 2006
    Last modified: March 16, 2016
    This is version 38 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure

    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.