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Q4WA69

- BGLK_ASPFU

UniProt

Q4WA69 - BGLK_ASPFU

Protein

Probable beta-glucosidase K

Gene

bglK

Organism
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 56 (01 Oct 2014)
      Sequence version 1 (05 Jul 2005)
      Previous versions | rss
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    Functioni

    Beta-glucosidases are one of a number of cellulolytic enzymes involved in the degradation of cellulosic biomass. Catalyzes the last step releasing glucose from the inhibitory cellobiose By similarity.By similarity

    Catalytic activityi

    Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei232 – 2321By similarity

    GO - Molecular functioni

    1. beta-glucosidase activity Source: UniProtKB-EC

    GO - Biological processi

    1. cellulose catabolic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism, Cellulose degradation, Polysaccharide degradation

    Enzyme and pathway databases

    UniPathwayiUPA00696.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Probable beta-glucosidase K (EC:3.2.1.21)
    Alternative name(s):
    Beta-D-glucoside glucohydrolase K
    Cellobiase K
    Gentiobiase K
    Gene namesi
    Name:bglK
    ORF Names:AFUA_7G00240
    OrganismiNeosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
    Taxonomic identifieri330879 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
    ProteomesiUP000002530: 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
    Chaini1 – 767767Probable beta-glucosidase KPRO_0000394897Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi19 – 191N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi324 – 3241N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi477 – 4771N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi749 – 7491N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Structurei

    3D structure databases

    ProteinModelPortaliQ4WA69.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini406 – 541136PA14Add
    BLAST

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 3 family.Curated
    Contains 1 PA14 domain.Curated

    Phylogenomic databases

    eggNOGiCOG1472.
    HOGENOMiHOG000031215.
    KOiK01238.
    OMAiQRGGTFF.
    OrthoDBiEOG7H799Q.

    Family and domain databases

    Gene3Di3.20.20.300. 1 hit.
    3.40.50.1700. 2 hits.
    InterProiIPR026892. Glyco_hydro_3.
    IPR019800. Glyco_hydro_3_AS.
    IPR002772. Glyco_hydro_3_C.
    IPR001764. Glyco_hydro_3_N.
    IPR017853. Glycoside_hydrolase_SF.
    IPR011658. PA14.
    [Graphical view]
    PANTHERiPTHR30620. PTHR30620. 1 hit.
    PfamiPF00933. Glyco_hydro_3. 1 hit.
    PF01915. Glyco_hydro_3_C. 1 hit.
    PF07691. PA14. 1 hit.
    [Graphical view]
    PRINTSiPR00133. GLHYDRLASE3.
    SMARTiSM00758. PA14. 1 hit.
    [Graphical view]
    SUPFAMiSSF51445. SSF51445. 1 hit.
    SSF52279. SSF52279. 2 hits.
    PROSITEiPS00775. GLYCOSYL_HYDROL_F3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q4WA69-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGEICPRRED FDIDYILKNA SLLEKVSLLA GYDFWHTAPL PRFNVPSVRV    50
    SDGPNGVRGT KFFDGVRAAC LPCGTGLAAT WDQSLLYDAG VLIGQECLAK 100
    GAHCWLVPTV CIQRSPLGGR GFESFAEDPY ATGKLAAAYI RGAQSTGVIS 150
    TIKHFAANDQ EHERISVNAV MSERALREVH LLPFQIAIAD SAPGAVMTCY 200
    NKVNGQHLSE SKEMLDGLLR REWGWKGLIM SDWFGTYSTA EALNAGLGLE 250
    MPGTTRLRGP LLELAISSRK VSRATLDERA RTVLEFVQRA RKAEVSAVES 300
    TRDFPEDRRL NRKLAADSIV LLKNESGLLP LNPQTLTSVA LIGPNMKTAA 350
    FCGGGSASLQ PYYSTSPYQG ITSQLPPGVE VLYETGATSY AFIPELEASE 400
    VRTPEGQPGL RMRFYRDPPS VQERRVLMGF SNPELDRLFY ADIEAELIAP 450
    ATGPFQFGLA VYGSASLFLN DQLIIDNTTV QRGGTFFFGK GTLEETATVD 500
    LVQGQSYQIK VQFASGPSSK LVKPGVVNFG GGAGRLGMVQ VVDPERAIAR 550
    AVEAAKRADI TILGVGLTRD HESEGFDRSH MDLPPAVASL VTAVLDVAPD 600
    AILLTQSGTP FSMLPWADLV KTHLHAWFGG NELGNGIADV LFGVVNPSGK 650
    LPLSFPRRIE DTPTYLNFGS ERGQVTYGEG IYVGYKLLRK SPTSCALSIR 700
    ARFVVHLLCV LRFDGRHRVR YTECSKLGRR GRSGSSPAVY RGRSNNVVNR 750
    TSHQGAQRIS KGGFAAR 767
    Length:767
    Mass (Da):83,358
    Last modified:July 5, 2005 - v1
    Checksum:iBF4924E3FE58BC4E
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AAHF01000015 Genomic DNA. Translation: EAL84867.1.
    RefSeqiXP_746905.1. XM_741812.1.

    Genome annotation databases

    EnsemblFungiiCADAFUAT00001243; CADAFUAP00001243; CADAFUAG00001243.
    GeneIDi3504260.
    KEGGiafm:AFUA_7G00240.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AAHF01000015 Genomic DNA. Translation: EAL84867.1 .
    RefSeqi XP_746905.1. XM_741812.1.

    3D structure databases

    ProteinModelPortali Q4WA69.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii CADAFUAT00001243 ; CADAFUAP00001243 ; CADAFUAG00001243 .
    GeneIDi 3504260.
    KEGGi afm:AFUA_7G00240.

    Phylogenomic databases

    eggNOGi COG1472.
    HOGENOMi HOG000031215.
    KOi K01238.
    OMAi QRGGTFF.
    OrthoDBi EOG7H799Q.

    Enzyme and pathway databases

    UniPathwayi UPA00696 .

    Family and domain databases

    Gene3Di 3.20.20.300. 1 hit.
    3.40.50.1700. 2 hits.
    InterProi IPR026892. Glyco_hydro_3.
    IPR019800. Glyco_hydro_3_AS.
    IPR002772. Glyco_hydro_3_C.
    IPR001764. Glyco_hydro_3_N.
    IPR017853. Glycoside_hydrolase_SF.
    IPR011658. PA14.
    [Graphical view ]
    PANTHERi PTHR30620. PTHR30620. 1 hit.
    Pfami PF00933. Glyco_hydro_3. 1 hit.
    PF01915. Glyco_hydro_3_C. 1 hit.
    PF07691. PA14. 1 hit.
    [Graphical view ]
    PRINTSi PR00133. GLHYDRLASE3.
    SMARTi SM00758. PA14. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51445. SSF51445. 1 hit.
    SSF52279. SSF52279. 2 hits.
    PROSITEi PS00775. GLYCOSYL_HYDROL_F3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Genomic sequence of the pathogenic and allergenic filamentous fungus Aspergillus fumigatus."
      Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J., Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P., Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.
      , Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N., Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K., Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E., Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A., Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D., O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R., Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.G., Denning D.W.
      Nature 438:1151-1156(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100.

    Entry informationi

    Entry nameiBGLK_ASPFU
    AccessioniPrimary (citable) accession number: Q4WA69
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 15, 2010
    Last sequence update: July 5, 2005
    Last modified: October 1, 2014
    This is version 56 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3