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O13990

- BGL2_SCHPO

UniProt

O13990 - BGL2_SCHPO

Protein

Glucan 1,3-beta-glucosidase

Gene

bgl2

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 89 (01 Oct 2014)
      Sequence version 4 (01 Feb 2005)
      Previous versions | rss
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    Functioni

    Glucanases possibly play a role in cell expansion during growth, in cell-cell fusion during mating, and in spore release during sporulation. This enzyme may be involved in beta-glucan degradation and also function biosynthetically as a transglycosylase.

    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 sitei244 – 2441NucleophileBy similarity
    Active sitei300 – 3001Proton donorBy similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. fungal-type cell wall beta-glucan metabolic process Source: PomBase

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Protein family/group databases

    CAZyiGH17. Glycoside Hydrolase Family 17.

    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:bgl2
    ORF Names:SPAC26H5.08c
    OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
    Taxonomic identifieri284812 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
    ProteomesiUP000002485: Chromosome I

    Organism-specific databases

    PomBaseiSPAC26H5.08c.

    Subcellular locationi

    Secretedcell wall By similarity
    Note: Tightly bound to cell wall.By similarity

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-KW
    2. fungal-type cell wall Source: PomBase

    Keywords - Cellular componenti

    Cell wall, Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2121Sequence AnalysisAdd
    BLAST
    Chaini22 – 321300Glucan 1,3-beta-glucosidasePRO_0000011895Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi39 – 391N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi99 – 991N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi210 – 2101N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi213 – 2131N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi237 – 2371N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi309 – 3091N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi317 – 3171N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    MaxQBiO13990.

    Interactioni

    Protein-protein interaction databases

    BioGridi279153. 18 interactions.
    STRINGi4896.SPAC26H5.08c-1.

    Structurei

    3D structure databases

    ProteinModelPortaliO13990.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 17 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG5309.
    HOGENOMiHOG000207150.
    KOiK01210.
    OMAiSDCNTLQ.
    OrthoDBiEOG7WMCVT.
    PhylomeDBiO13990.

    Family and domain databases

    Gene3Di3.20.20.80. 1 hit.
    InterProiIPR000490. Glyco_hydro_17.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PfamiPF00332. Glyco_hydro_17. 1 hit.
    [Graphical view]
    SUPFAMiSSF51445. SSF51445. 1 hit.
    PROSITEiPS00587. GLYCOSYL_HYDROL_F17. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    O13990-1 [UniParc]FASTAAdd to Basket

    « Hide

    MQFLSSFVFA ALALLPLSAM AVDEAASEIA SSTKPASTNG TLSFCLGVKH    50
    ADGTCKYTDD YLADFEVLAP YTNMIRTYAT SDCNTLEYLL PALAQSPYNF 100
    SAILGVWPTD DAHYDLEKQA LMQYLPQYGV DHVRAITVGS EVLYRNDLPA 150
    DVLAERIYDV RGLVQQKLGF DVPVGTADSW NLWAGGSGDV VITASDFIMS 200
    NDFPYWQGQN TSNMTNTFIS DTLAALERVQ SVKGTNNVTF WVGETGWPTD 250
    GPSYGEADAT VDIASEFFQE ALCNIRRKGI DIFFFEAFDE DWKGDSSSVE 300
    PYFGAMYSNR TLKYNLNCTS E 321
    Length:321
    Mass (Da):35,412
    Last modified:February 1, 2005 - v4
    Checksum:i10094466592006CA
    GO

    Sequence cautioni

    The sequence BAA19145.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti281 – 2811D → N in BAA19145. (PubMed:9501991)Curated
    Sequence conflicti303 – 3031F → L in BAA19145. (PubMed:9501991)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CU329670 Genomic DNA. Translation: CAB16200.1.
    AB000539 mRNA. Translation: BAA19145.1. Different initiation.
    PIRiT38427.
    RefSeqiNP_594455.1. NM_001019884.2.

    Genome annotation databases

    EnsemblFungiiSPAC26H5.08c.1; SPAC26H5.08c.1:pep; SPAC26H5.08c.
    GeneIDi2542700.
    KEGGispo:SPAC26H5.08c.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CU329670 Genomic DNA. Translation: CAB16200.1 .
    AB000539 mRNA. Translation: BAA19145.1 . Different initiation.
    PIRi T38427.
    RefSeqi NP_594455.1. NM_001019884.2.

    3D structure databases

    ProteinModelPortali O13990.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 279153. 18 interactions.
    STRINGi 4896.SPAC26H5.08c-1.

    Protein family/group databases

    CAZyi GH17. Glycoside Hydrolase Family 17.

    Proteomic databases

    MaxQBi O13990.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii SPAC26H5.08c.1 ; SPAC26H5.08c.1:pep ; SPAC26H5.08c .
    GeneIDi 2542700.
    KEGGi spo:SPAC26H5.08c.

    Organism-specific databases

    PomBasei SPAC26H5.08c.

    Phylogenomic databases

    eggNOGi COG5309.
    HOGENOMi HOG000207150.
    KOi K01210.
    OMAi SDCNTLQ.
    OrthoDBi EOG7WMCVT.
    PhylomeDBi O13990.

    Miscellaneous databases

    NextBioi 20803748.

    Family and domain databases

    Gene3Di 3.20.20.80. 1 hit.
    InterProi IPR000490. Glyco_hydro_17.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view ]
    Pfami PF00332. Glyco_hydro_17. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51445. SSF51445. 1 hit.
    PROSITEi PS00587. GLYCOSYL_HYDROL_F17. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The genome sequence of Schizosaccharomyces pombe."
      Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
      , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
      Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 972 / ATCC 24843.
    2. "Identification of open reading frames in Schizosaccharomyces pombe cDNAs."
      Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.
      DNA Res. 4:363-369(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 11-321.
      Strain: PR745.

    Entry informationi

    Entry nameiBGL2_SCHPO
    AccessioniPrimary (citable) accession number: O13990
    Secondary accession number(s): P79062
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 2005
    Last sequence update: February 1, 2005
    Last modified: October 1, 2014
    This is version 89 of the entry and version 4 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. Schizosaccharomyces pombe
      Schizosaccharomyces pombe: entries and gene names
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3