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Q9XEI3

- Q9XEI3_HORVD

UniProt

Q9XEI3 - Q9XEI3_HORVD

Protein
Submitted name:

Beta-D-glucan exohydrolase isoenzyme ExoI

Gene
N/A
Organism
Hordeum vulgare var. distichum (Two-rowed barley)
Status
Unreviewed - Annotation score: 1 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 63 (01 Oct 2014)
      Sequence version 1 (01 Nov 1999)
      Previous versions | rss
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    Functioni

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei120 – 1201GlucoseImported
    Binding sitei183 – 1831GlucoseImported
    Active sitei310 – 3101Proton donor/acceptor
    Binding sitei310 – 3101GlucoseImported
    Binding sitei512 – 5121MannoseImported
    Active sitei516 – 5161Proton donor/acceptor
    Binding sitei591 – 5911Beta-D-mannoseImported

    GO - Molecular functioni

    1. hydrolase activity, hydrolyzing O-glycosyl compounds Source: InterPro

    GO - Biological processi

    1. carbohydrate metabolic process Source: InterPro

    Keywords - Molecular functioni

    HydrolaseSAAS annotationImported

    Protein family/group databases

    CAZyiGH3. Glycoside Hydrolase Family 3.

    Names & Taxonomyi

    Protein namesi
    Submitted name:
    Beta-D-glucan exohydrolase isoenzyme ExoIImported
    OrganismiHordeum vulgare var. distichum (Two-rowed barley)Imported
    Taxonomic identifieri112509 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBEP cladePooideaeTriticeaeHordeum

    Organism-specific databases

    GrameneiQ9XEI3.

    PTM / Processingi

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi246 – 2461N-linked (GlcNAc...)Imported
    Glycosylationi523 – 5231N-linked (GlcNAc...)Imported
    Glycosylationi625 – 6251N-linked (GlcNAc...)Imported

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1EX1X-ray2.20A26-630[»]
    1IEQX-ray2.70A26-630[»]
    1IEVX-ray2.80A26-630[»]
    1IEWX-ray2.55A26-630[»]
    1IEXX-ray2.20A26-630[»]
    1J8VX-ray2.40A26-630[»]
    1LQ2X-ray2.70A26-627[»]
    1X38X-ray1.70A26-627[»]
    1X39X-ray1.80A26-627[»]
    ProteinModelPortaliQ9XEI3.
    SMRiQ9XEI3. Positions 26-628.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9XEI3.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni231 – 2322Glucose bindingImported

    Family and domain databases

    Gene3Di3.20.20.300. 1 hit.
    3.40.50.1700. 1 hit.
    InterProiIPR026892. Glyco_hydro_3.
    IPR002772. Glyco_hydro_3_C.
    IPR001764. Glyco_hydro_3_N.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PANTHERiPTHR30620. PTHR30620. 1 hit.
    PfamiPF00933. Glyco_hydro_3. 1 hit.
    PF01915. Glyco_hydro_3_C. 1 hit.
    [Graphical view]
    PRINTSiPR00133. GLHYDRLASE3.
    SUPFAMiSSF51445. SSF51445. 1 hit.
    SSF52279. SSF52279. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q9XEI3-1 [UniParc]FASTAAdd to Basket

    « Hide

    MALLTAPAVF AALLLFWAVL GGTDADYVLY KDATKPVEDR VADLLGRMTL    50
    AEKIGQMTQI ERLVATPDVL RDNFIGSLLS GGGSVPRKGA TAKEWQDMVD 100
    GFQKACMSTR LGIPMIYGID AVHGQNNVYG ATIFPHNVGL GATRDPYLVK 150
    RIGEATALEV RATGIQYAFA PCIAVCRDPR WGRCYESYSE DRRIVQSMTE 200
    LIPGLQGDVP KDFTSGMPFV AGKNKVAACA KHFVGDGGTV DGINENNTII 250
    NREGLMNIHM PAYKNAMDKG VSTVMISYSS WNGVKMHANQ DLVTGYLKDT 300
    LKFKGFVISD WEGIDRITTP AGSDYSYSVK ASILAGLDMI MVPNNYQQFI 350
    SILTGHVNGG VIPMSRIDDA VTRILRVKFT MGLFENPYAD PAMAEQLGKQ 400
    EHRDLAREAA RKSLVLLKNG KTSTDAPLLP LPKKAPKILV AGSHADNLGY 450
    QCGGWTIEWQ GDTGRTTVGT TILEAVKAAV DPSTVVVFAE NPDAEFVKSG 500
    GFSYAIVAVG EHPYTETKGD NLNLTIPEPG LSTVQAVCGG VRCATVLISG 550
    RPVVVQPLLA ASDALVAAWL PGSEGQGVTD ALFGDFGFTG RLPRTWFKSV 600
    DQLPMNVGDA HYDPLFRLGY GLTTNATKKY 630
    Length:630
    Mass (Da):67,906
    Last modified:November 1, 1999 - v1
    Checksum:iE55B2970655DB9AF
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF102868 mRNA. Translation: AAD23382.1.
    PIRiT51281.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF102868 mRNA. Translation: AAD23382.1 .
    PIRi T51281.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1EX1 X-ray 2.20 A 26-630 [» ]
    1IEQ X-ray 2.70 A 26-630 [» ]
    1IEV X-ray 2.80 A 26-630 [» ]
    1IEW X-ray 2.55 A 26-630 [» ]
    1IEX X-ray 2.20 A 26-630 [» ]
    1J8V X-ray 2.40 A 26-630 [» ]
    1LQ2 X-ray 2.70 A 26-627 [» ]
    1X38 X-ray 1.70 A 26-627 [» ]
    1X39 X-ray 1.80 A 26-627 [» ]
    ProteinModelPortali Q9XEI3.
    SMRi Q9XEI3. Positions 26-628.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi GH3. Glycoside Hydrolase Family 3.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Organism-specific databases

    Gramenei Q9XEI3.

    Miscellaneous databases

    EvolutionaryTracei Q9XEI3.

    Family and domain databases

    Gene3Di 3.20.20.300. 1 hit.
    3.40.50.1700. 1 hit.
    InterProi IPR026892. Glyco_hydro_3.
    IPR002772. Glyco_hydro_3_C.
    IPR001764. Glyco_hydro_3_N.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view ]
    PANTHERi PTHR30620. PTHR30620. 1 hit.
    Pfami PF00933. Glyco_hydro_3. 1 hit.
    PF01915. Glyco_hydro_3_C. 1 hit.
    [Graphical view ]
    PRINTSi PR00133. GLHYDRLASE3.
    SUPFAMi SSF51445. SSF51445. 1 hit.
    SSF52279. SSF52279. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Three-dimensional structure of a barley beta-D-glucan exohydrolase, a family 3 glycosyl hydrolase."
      Varghese J.N., Hrmova M., Fincher G.B.
      Structure 7:179-190(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 26-630 IN COMPLEX WITH GLUCOSE AND MANNOSE, ACTIVE SITE, GLYCOSYLATION AT ASN-246 AND ASN-523.
    2. "Regulation of genes encoding beta-D-glucan glucohydrolases in barley (Hordeum vulgare)."
      Harvey A.J., Hrmova M., Fincher G.B.
      Physiol. Plantarum 113:108-120(2001)
      Cited for: NUCLEOTIDE SEQUENCE.
    3. "Catalytic mechanisms and reaction intermediates along the hydrolytic pathway of a plant beta-D-glucan glucohydrolase."
      Hrmova M., Varghese J.N., De Gori R., Smith B.J., Driguez H., Fincher G.B.
      Structure 9:1005-1016(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 26-630 IN COMPLEX WITH MANNOSE, GLYCOSYLATION AT ASN-246; ASN-523 AND ASN-625.
    4. "Structural basis for broad substrate specificity in higher plant beta-D-glucan glucohydrolases."
      Hrmova M., De Gori R., Smith B.J., Fairweather J.K., Driguez H., Varghese J.N., Fincher G.B.
      Plant Cell 14:1033-1052(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 26-630 IN COMPLEX WITH MANNOSE, GLYCOSYLATION AT ASN-246; ASN-523 AND ASN-625.
    5. "Three-dimensional structure of the barley beta-D-glucan glucohydrolase in complex with a transition state mimic."
      Hrmova M., De Gori R., Smith B.J., Vasella A., Varghese J.N., Fincher G.B.
      J. Biol. Chem. 279:4970-4980(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 26-627 IN COMPLEX WITH BETA-D-MANNOSE AND MANNOSE, GLYCOSYLATION AT ASN-246; ASN-523 AND ASN-625.
    6. "Structural rationale for low-nanomolar binding of transition state mimics to a family GH3 beta-D-glucan glucohydrolase from barley."
      Hrmova M., Streltsov V.A., Smith B.J., Vasella A., Varghese J.N., Fincher G.B.
      Biochemistry 44:16529-16539(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 26-627 IN COMPLEX WITH MANNOSE, GLYCOSYLATION AT ASN-246; ASN-523 AND ASN-625.

    Entry informationi

    Entry nameiQ9XEI3_HORVD
    AccessioniPrimary (citable) accession number: Q9XEI3
    Entry historyi
    Integrated into UniProtKB/TrEMBL: November 1, 1999
    Last sequence update: November 1, 1999
    Last modified: October 1, 2014
    This is version 63 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiUnreviewed (UniProtKB/TrEMBL)

    Miscellaneousi

    Keywords - Technical termi

    3D-structureImported

    External Data

    Dasty 3