Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q876J3

- EXG_SACU7

UniProt

Q876J3 - EXG_SACU7

Protein

Glucan 1,3-beta-glucosidase

Gene

EXG1

Organism
Saccharomyces uvarum (strain ATCC 76518 / CBS 7001 / CLIB 283 / NBRC 10550 / MCYC 623 / NCYC 2669 / NRRL Y-11845) (Yeast) (Saccharomyces bayanus var. uvarum)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 53 (01 Oct 2014)
      Sequence version 1 (01 Jun 2003)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Beta-glucanases participate in the metabolism of beta-glucan, the main structural component of the cell wall. It could also function biosynthetically as a transglycosylase By similarity.By similarity

    Catalytic activityi

    Successive hydrolysis of beta-D-glucose units from the non-reducing ends of (1->3)-beta-D-glucans, releasing alpha-glucose.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei232 – 2321Proton donorBy similarity
    Active sitei334 – 3341NucleophileBy similarity

    GO - Molecular functioni

    1. glucan exo-1,3-beta-glucosidase activity Source: UniProtKB-EC

    GO - Biological processi

    1. carbohydrate metabolic process Source: InterPro

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Cell wall biogenesis/degradation

    Protein family/group databases

    CAZyiGH5. Glycoside Hydrolase Family 5.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glucan 1,3-beta-glucosidase (EC:3.2.1.58)
    Alternative name(s):
    Exo-1,3-beta-glucanase
    Gene namesi
    Name:EXG1
    OrganismiSaccharomyces uvarum (strain ATCC 76518 / CBS 7001 / CLIB 283 / NBRC 10550 / MCYC 623 / NCYC 2669 / NRRL Y-11845) (Yeast) (Saccharomyces bayanus var. uvarum)
    Taxonomic identifieri226127 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

    Subcellular locationi

    Secreted Curated

    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 – 1919Sequence AnalysisAdd
    BLAST
    Propeptidei20 – 4021Sequence AnalysisPRO_0000007890Add
    BLAST
    Chaini41 – 448408Glucan 1,3-beta-glucosidasePRO_0000007889Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi317 ↔ 443By similarity
    Disulfide bondi342 ↔ 372By similarity

    Keywords - PTMi

    Disulfide bond, Zymogen

    Structurei

    3D structure databases

    ProteinModelPortaliQ876J3.
    SMRiQ876J3. Positions 41-448.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Family and domain databases

    Gene3Di3.20.20.80. 1 hit.
    InterProiIPR001547. Glyco_hydro_5.
    IPR018087. Glyco_hydro_5_CS.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PfamiPF00150. Cellulase. 1 hit.
    [Graphical view]
    SUPFAMiSSF51445. SSF51445. 1 hit.
    PROSITEiPS00659. GLYCOSYL_HYDROL_F5. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q876J3-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLSLKTLLCT LLTVSSVIAN PVPARDPSSI QFVHEENKKR YYDYDNGALG    50
    EPIRGVNIGG WLVLEPYITP SLFEAFRTND NNDDGIPVDE YHYCQYLGND 100
    LAKSRLQSHW STFYQEQDFA NIASQGFNLV RIPIGYWAFA TLDNDPYVTG 150
    LQESYLDQAI GWARNNSLKV WVDLHGAAGS QNGFDNSGLR DSYEFLEDSN 200
    LAVTTKALNY ILKKYSAEEY LDTVIGIELI NEPLGPVLDM DKMKNDYLLP 250
    AYEYLRNTIE SNQIIIMHDA FQQFNYWDDF MTETDGYWGV TIDHHHYQVF 300
    DSSQLESSMD EHIQVACQWG TGVLDEAHWT VCGEFAAALT DCTKWVNSVG 350
    FGARYDGSWV NGDETSTYIG SCANNDDITS WSDQRKENTR RYVEAQLDAF 400
    EMRGGWIIWC YKTESSLEWD VQRLMYNGLF PQPLTDRQYP NQCNTTSS 448
    Length:448
    Mass (Da):51,229
    Last modified:June 1, 2003 - v1
    Checksum:i80AAF86129D16F1C
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY144818 Genomic DNA. Translation: AAO32382.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY144818 Genomic DNA. Translation: AAO32382.1 .

    3D structure databases

    ProteinModelPortali Q876J3.
    SMRi Q876J3. Positions 41-448.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi GH5. Glycoside Hydrolase Family 5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    Gene3Di 3.20.20.80. 1 hit.
    InterProi IPR001547. Glyco_hydro_5.
    IPR018087. Glyco_hydro_5_CS.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view ]
    Pfami PF00150. Cellulase. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51445. SSF51445. 1 hit.
    PROSITEi PS00659. GLYCOSYL_HYDROL_F5. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Yeast genome duplication was followed by asynchronous differentiation of duplicated genes."
      Langkjaer R.B., Cliften P.F., Johnston M., Piskur J.
      Nature 421:848-852(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 623-6C / CBS 9787 / CLIB 533.

    Entry informationi

    Entry nameiEXG_SACU7
    AccessioniPrimary (citable) accession number: Q876J3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 13, 2004
    Last sequence update: June 1, 2003
    Last modified: October 1, 2014
    This is version 53 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    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