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Q2TZQ9

- EXGB_ASPOR

UniProt

Q2TZQ9 - EXGB_ASPOR

Protein

Probable glucan endo-1,6-beta-glucosidase B

Gene

exgB

Organism
Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 46 (01 Oct 2014)
      Sequence version 1 (24 Jan 2006)
      Previous versions | rss
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    Functioni

    Beta-glucanases participate in the metabolism of beta-glucan, the main structural component of the cell wall. Acts on lutean, pustulan and 1,6-oligo-beta-D-glucosides By similarity.By similarity

    Catalytic activityi

    Random hydrolysis of (1->6)-linkages in (1->6)-beta-D-glucans.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei220 – 2201Proton donorBy similarity
    Active sitei322 – 3221NucleophileBy similarity

    GO - Molecular functioni

    1. glucan endo-1,6-beta-glucosidase activity Source: UniProtKB-EC

    GO - Biological processi

    1. polysaccharide catabolic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism, Cell wall biogenesis/degradation, Polysaccharide degradation

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Probable glucan endo-1,6-beta-glucosidase B (EC:3.2.1.75)
    Alternative name(s):
    Beta-1,6-glucanase B
    Endo-1,6-beta-D-glucanase B
    Endo-1,6-beta-glucanase B
    Gene namesi
    Name:exgB
    ORF Names:AO090011000757
    OrganismiAspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
    Taxonomic identifieri510516 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
    ProteomesiUP000006564: Chromosome 7

    Subcellular locationi

    Secreted By similarity

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1818Sequence AnalysisAdd
    BLAST
    Chaini19 – 406388Probable glucan endo-1,6-beta-glucosidase BPRO_0000394708Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi31 – 311N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Structurei

    3D structure databases

    ProteinModelPortaliQ2TZQ9.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG2730.
    HOGENOMiHOG000217590.
    OMAiSEHFPQG.
    OrthoDBiEOG776T0C.

    Family and domain databases

    Gene3Di3.20.20.80. 1 hit.
    InterProiIPR001547. Glyco_hydro_5.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PfamiPF00150. Cellulase. 1 hit.
    [Graphical view]
    SUPFAMiSSF51445. SSF51445. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    Q2TZQ9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKVTRLAVLN TLATLTVAWL PTTDKTITSS NGTDLFKASH GKIRGVNLGS    50
    QFVFEPWIAT KAWSELGCEG QESEFDCVMK LGQDAANKAF AKHWDSWITK 100
    EDIKEIRSYG LNTIRIPVGY WMNEDLIYHD SEYFPHGGFA YLEKLCGWAS 150
    DAGLYIIIDL HGAPGAQVAK NAFTGQFADT PGFYVDFQYQ RALEFLEWMT 200
    IKVHTLHNFR NVGMLEVVNE PVQNPQVTTT LRSNYYPNAF HSIRKVEGAL 250
    SIDRKDYLHI QMMDGAWGAG DPHEHLTDDY YAAYDNHRYL KWDPRVEVSK 300
    DSYIKTSCND NVATNWPAII GEWSLGVPDN VQETADWKPY SNLDFYQKWF 350
    AAQVQNYEQH QGWIFWTWKT QLDEYRWSYR DGVKAGVIPT DLNAVFREDV 400
    CKGRSS 406
    Length:406
    Mass (Da):46,614
    Last modified:January 24, 2006 - v1
    Checksum:i9A8781C383B12BA6
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AP007171 Genomic DNA. Translation: BAE65206.1.
    RefSeqiXP_001826339.1. XM_001826287.2.

    Genome annotation databases

    EnsemblFungiiCADAORAT00005465; CADAORAP00005364; CADAORAG00005465.
    GeneIDi5998442.
    KEGGiaor:AOR_1_1278054.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AP007171 Genomic DNA. Translation: BAE65206.1 .
    RefSeqi XP_001826339.1. XM_001826287.2.

    3D structure databases

    ProteinModelPortali Q2TZQ9.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii CADAORAT00005465 ; CADAORAP00005364 ; CADAORAG00005465 .
    GeneIDi 5998442.
    KEGGi aor:AOR_1_1278054.

    Phylogenomic databases

    eggNOGi COG2730.
    HOGENOMi HOG000217590.
    OMAi SEHFPQG.
    OrthoDBi EOG776T0C.

    Family and domain databases

    Gene3Di 3.20.20.80. 1 hit.
    InterProi IPR001547. Glyco_hydro_5.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view ]
    Pfami PF00150. Cellulase. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51445. SSF51445. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Genome sequencing and analysis of Aspergillus oryzae."
      Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K., Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H., Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.
      , Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D., Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A., Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y., Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H., Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T., Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O., Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y., Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N., Kikuchi H.
      Nature 438:1157-1161(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 42149 / RIB 40.

    Entry informationi

    Entry nameiEXGB_ASPOR
    AccessioniPrimary (citable) accession number: Q2TZQ9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 15, 2010
    Last sequence update: January 24, 2006
    Last modified: October 1, 2014
    This is version 46 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3