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Protein

Avenacosidase 1

Gene

P60A

Organism
Avena sativa (Oat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Beta-glucosidase acting as a preformed defense system. Hydrolyzes the bisdesmosides avenacosides A and B to 26-desgluco-avenacosides exhibiting fungicidal activity. Can use beta-fucoside > beta-glucoside > beta-galactoside > beta-xyloside as substrates, but not alpha-glycosides, beta-thioglucosides and disaccharides.3 Publications

Catalytic activityi

Avenacoside B + H2O = 26-desgluco-avenacoside B + D-glucose.4 Publications

Enzyme regulationi

Inhibited by N-(3-Dimethylaminopropyl)-N'-ethylcarbodiimide hydrochloride (EDC).1 Publication

Kineticsi

The activity increases with rising aggregation of the enzyme. kcat is 982000 sec(-1) with avenacosides as substrate. kcat is 3090 sec(-1) with p-nitrophenyl-beta-D-glucopyranoside as substrate. kcat is 290 sec(-1) with genistin as substrate.

  1. KM=2.2 mM for p-nitrophenyl-beta-D-glucopyranoside (with native enzyme)3 Publications
  2. KM=1.57 mM for p-nitrophenyl-beta-D-glucopyranoside (with homomultimeric recombinant enzyme)3 Publications
  3. KM=1.48 mM for p-nitrophenyl-beta-D-glucopyranoside (with heteromultimeric recombinant enzyme)3 Publications
  4. KM=12 µM for avenacosides (with native enzyme)3 Publications
  5. KM=0.4 mM for genistin (with native enzyme)3 Publications

    pH dependencei

    Optimum pH is 6.0.3 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei88 – 881SubstrateBy similarity
    Binding sitei237 – 2371SubstrateBy similarity
    Active sitei238 – 2381Proton donorBy similarity
    Active sitei454 – 4541NucleophileBy similarity
    Binding sitei505 – 5051SubstrateBy similarity

    GO - Molecular functioni

    • beta-glucosidase activity Source: UniProtKB
    • identical protein binding Source: UniProtKB

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Plant defense

    Enzyme and pathway databases

    BRENDAi3.2.1.186. 588.

    Protein family/group databases

    CAZyiGH1. Glycoside Hydrolase Family 1.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Avenacosidase 1 (EC:3.2.1.188)
    Alternative name(s):
    26-desgluco-avenacosidase 1
    Protein As-Glu1
    Protein As-P60
    Gene namesi
    Name:P60A
    Synonyms:GLU1
    OrganismiAvena sativa (Oat)
    Taxonomic identifieri4498 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBOP cladePooideaePoodaePoeaeAveninaeAvena

    Subcellular locationi

    GO - Cellular componenti

    • chloroplast Source: UniProtKB
    • chloroplast stroma Source: UniProtKB-SubCell
    Complete GO annotation...

    Keywords - Cellular componenti

    Chloroplast, Plastid

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 5555Chloroplast3 PublicationsAdd
    BLAST
    Chaini56 – 574519Avenacosidase 1PRO_5000146241Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi258 ↔ 264By similarity

    Keywords - PTMi

    Disulfide bond

    Expressioni

    Tissue specificityi

    Expressed in caryopses, coleoptiles, primary leaves, and etiolated and green seedlings, but not in roots.1 Publication

    Interactioni

    Subunit structurei

    Homo- and heteromultimer with P60B in a 1:1 stoichiometry. Aggregates to form the fibrilar stromacentre.2 Publications

    GO - Molecular functioni

    • identical protein binding Source: UniProtKB

    Structurei

    3D structure databases

    ProteinModelPortaliQ38786.
    SMRiQ38786. Positions 62-548.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni512 – 5132Substrate bindingBy similarity

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 1 family.Curated

    Keywords - Domaini

    Transit peptide

    Family and domain databases

    Gene3Di3.20.20.80. 1 hit.
    InterProiIPR001360. Glyco_hydro_1.
    IPR033132. Glyco_hydro_1_N_CS.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PANTHERiPTHR10353. PTHR10353. 1 hit.
    PfamiPF00232. Glyco_hydro_1. 1 hit.
    [Graphical view]
    PRINTSiPR00131. GLHYDRLASE1.
    SUPFAMiSSF51445. SSF51445. 1 hit.
    PROSITEiPS00653. GLYCOSYL_HYDROL_F1_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q38786-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MALLCSALSN STHPSFRSHI GANSENLWHL SADPAQKSKR RCNLTLSSRA
    60 70 80 90 100
    ARISSALESA KQVKPWQVPK RDWFPPEFMF GAASAAYQIE GAWNEGGKGP
    110 120 130 140 150
    SSWDNFCHSH PDRIMDKSNA DVAANSYYMY KEDVRMLKEI GMDSYRFSIS
    160 170 180 190 200
    WPRILPKGTL DGGINHEGIQ YYNDLLDCLI ENGIKPYITL FHWDTPQALA
    210 220 230 240 250
    DEYKDFLDRR IVKDYTDYAT VCFEHFGDKV KNWFTFNEPH SFCGLGYGTG
    260 270 280 290 300
    LHAPGARCSA GMTCVIPEED ALRNPYIVGH NLLLAHAETV DVYNKFYKGD
    310 320 330 340 350
    DGQIGMVLDV MAYEPYGNNF LDQQAQERAI DFHIGWFLEP MVRGDYPFSM
    360 370 380 390 400
    RSLVGDRLPF FTKSEQEKLV SSYDFVGINY YTSRFAKHID ISPEFIPKIN
    410 420 430 440 450
    TDDVYSNPEV NDSNGIPIGP DVGMYFIYSY PKGLKNILLR MKEKYGNPPI
    460 470 480 490 500
    YITENGTADM DGWGNPPMTD PLDDPLRIEY LQQHMTAIKE AIDLGRRTLR
    510 520 530 540 550
    GHFTWSLIDN FEWSLGYLSR FGIVYIDRND GCKRIMKKSA KWLKEFNGAT
    560 570
    KKLNNKILGA SSCCSGVTHG GGTA
    Length:574
    Mass (Da):65,041
    Last modified:November 1, 1996 - v1
    Checksum:i5C6312DCAF251631
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X78433 mRNA. Translation: CAA55196.1.
    PIRiS43128.
    S45723.
    S50756.

    Genome annotation databases

    KEGGiag:CAA55196.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X78433 mRNA. Translation: CAA55196.1.
    PIRiS43128.
    S45723.
    S50756.

    3D structure databases

    ProteinModelPortaliQ38786.
    SMRiQ38786. Positions 62-548.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein family/group databases

    CAZyiGH1. Glycoside Hydrolase Family 1.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    KEGGiag:CAA55196.

    Enzyme and pathway databases

    BRENDAi3.2.1.186. 588.

    Family and domain databases

    Gene3Di3.20.20.80. 1 hit.
    InterProiIPR001360. Glyco_hydro_1.
    IPR033132. Glyco_hydro_1_N_CS.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PANTHERiPTHR10353. PTHR10353. 1 hit.
    PfamiPF00232. Glyco_hydro_1. 1 hit.
    [Graphical view]
    PRINTSiPR00131. GLHYDRLASE1.
    SUPFAMiSSF51445. SSF51445. 1 hit.
    PROSITEiPS00653. GLYCOSYL_HYDROL_F1_2. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiAVCO1_AVESA
    AccessioniPrimary (citable) accession number: Q38786
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 16, 2014
    Last sequence update: November 1, 1996
    Last modified: March 16, 2016
    This is version 78 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Long fibrillar homomultimers are formed by linear stacking of trimeric units. The multimerization of the enzyme promotes formation of a long central channel with narrow openings at the sides. The active sites are localized inside the tunnels, constraining the accessibility of substrates and products.

    Keywords - Technical termi

    Direct protein sequencing

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    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.