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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)DescriptionActionsGraphical viewLength
    Active sitei169Curated1
    Active sitei276Curated1
    Active sitei306Curated1

    GO - Molecular functioni

    GO - Biological processi

    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)DescriptionActionsGraphical viewLength
    ChainiPRO_00004034821 – 335Carboxylesterase 1Add BLAST335

    Structurei

    Secondary structure

    1335
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Turni19 – 21Combined sources3
    Beta strandi52 – 61Combined sources10
    Turni62 – 65Combined sources4
    Beta strandi66 – 73Combined sources8
    Helixi74 – 78Combined sources5
    Beta strandi83 – 89Combined sources7
    Turni93 – 95Combined sources3
    Helixi102 – 115Combined sources14
    Beta strandi118 – 123Combined sources6
    Turni127 – 130Combined sources4
    Helixi134 – 147Combined sources14
    Helixi152 – 157Combined sources6
    Beta strandi158 – 168Combined sources11
    Helixi170 – 183Combined sources14
    Helixi186 – 189Combined sources4
    Beta strandi194 – 201Combined sources8
    Helixi211 – 215Combined sources5
    Turni216 – 218Combined sources3
    Beta strandi220 – 222Combined sources3
    Helixi224 – 234Combined sources11
    Turni244 – 246Combined sources3
    Helixi257 – 264Combined sources8
    Beta strandi267 – 273Combined sources7
    Helixi279 – 291Combined sources13
    Beta strandi295 – 303Combined sources9
    Helixi308 – 310Combined sources3
    Helixi313 – 327Combined sources15

    3D structure databases

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

    Miscellaneous databases

    EvolutionaryTraceiQ0ZPV7.

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni92 – 93Inhibitor binding2
    Regioni169 – 170Inhibitor binding2

    Motif

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Motifi90 – 92Involved in the stabilization of the negatively charged intermediate by the formation of the oxyanion holeBy similarity3

    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
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2O7RX-ray1.40A1-335[»]
    2O7VX-ray2.30A1-335[»]
    ProteinModelPortaliQ0ZPV7.
    SMRiQ0ZPV7.
    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...

    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: November 2, 2016
    This is version 41 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.