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Q4WU49

- BGLI_ASPFU

UniProt

Q4WU49 - BGLI_ASPFU

Protein

Probable beta-glucosidase I

Gene

bglI

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 58 (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 sitei225 – 2251By 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 I (EC:3.2.1.21)
    Alternative name(s):
    Beta-D-glucoside glucohydrolase I
    Cellobiase I
    Gentiobiase I
    Gene namesi
    Name:bglI
    ORF Names:AFUA_5G07190
    OrganismiNeosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
    Taxonomic identifieri330879 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
    ProteomesiUP000002530: Chromosome 5

    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 – 838838Probable beta-glucosidase IPRO_0000394886Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi197 – 1971N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi493 – 4931N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Interactioni

    Protein-protein interaction databases

    STRINGi5085.CADAFUAP00006281.

    Structurei

    3D structure databases

    ProteinModelPortaliQ4WU49.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini396 – 542147PA14Add
    BLAST

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG1472.
    HOGENOMiHOG000031215.
    KOiK05349.
    OMAiKTRWRGD.
    OrthoDBiEOG7H799Q.

    Family and domain databases

    Gene3Di3.20.20.300. 1 hit.
    3.40.50.1700. 2 hits.
    InterProiIPR026891. Fn3-like.
    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]
    PANTHERiPTHR30620. PTHR30620. 1 hit.
    PfamiPF14310. Fn3-like. 1 hit.
    PF00933. 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.

    Q4WU49-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVQLDVEKTI EELTLGEKVA LTAGIDFWHT AAVPRLNIPS LRMSDGPNGV    50
    RGTRFFNGVP AACFPCATAL GATWDTKLLY EVGRLMGEES IAKGAHVVLG 100
    PTINTQRSPL GGRGFESFAE DGVLSGILAG HYCKGLQETG VAATLKHFVC 150
    NDQEHERLAV DSIVTMRAMR EIYLLPFQLA MRICKTACVM TAYNKVNGTH 200
    VSENKQIITD ILRKEWGWDG LVMSDWFGTY STCDAINAGL DLEMPGPTRW 250
    RGTALAHAVS SNKAFEFVMD ERVRNILNLH NFVEPLGIPE NAPEKALNRP 300
    EDQALLRRAA AESVVLIKNQ DNILPLKKEK PILVIGPNAK TAAYCGGGSA 350
    SLDAYYTVTP FEGVAAQSQG EVTFSQGVYS YKELPLLGPL LKTDDGKKGF 400
    KFRVYNEPPS EPNRQLIDEL HLESSSGFLM DYKHPKIKTF TFYVDMEGYF 450
    TPEEDGIYDF GVTVVGTGKL FVDDELVVDN SKNQRQGTAM FGNATVEEKG 500
    SKELKAGQTY KVVLQFGTAP TSDLDMRGVV IFGPGGFRFG AARRVSQEEL 550
    ISKAAELASQ TSQVVIFAGL TSEWETEGYD RDHMDLPPGS DEMISRVLDA 600
    NPDTVVVIQS GTPVTMPWAH KAKALLQAWF GGNECGNGIA DVLYGNVNPA 650
    AKLPLSFPVR LQDNPSYLNF RSERGRVLYG EDIYVGYRYY EKVDLAPLFP 700
    FGHGLSYTTF SRSDLSLATT PEKPQLEDGE PITVTVSVTN TGSVAGAEIV 750
    QLWVAPPPTG VNRPVRELKG FTKVFLQPGE TKKVEIVVEK KLATSWWDEQ 800
    REKWASEKGT YEVLVTGTGD EVLKSSFEVE KTRYWLGL 838
    Length:838
    Mass (Da):92,208
    Last modified:July 5, 2005 - v1
    Checksum:i778CBDF5A0B2C14B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AAHF01000003 Genomic DNA. Translation: EAL91877.1.
    RefSeqiXP_753915.1. XM_748822.1.

    Genome annotation databases

    EnsemblFungiiCADAFUAT00006281; CADAFUAP00006281; CADAFUAG00006281.
    GeneIDi3511295.
    KEGGiafm:AFUA_5G07190.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AAHF01000003 Genomic DNA. Translation: EAL91877.1 .
    RefSeqi XP_753915.1. XM_748822.1.

    3D structure databases

    ProteinModelPortali Q4WU49.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 5085.CADAFUAP00006281.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii CADAFUAT00006281 ; CADAFUAP00006281 ; CADAFUAG00006281 .
    GeneIDi 3511295.
    KEGGi afm:AFUA_5G07190.

    Phylogenomic databases

    eggNOGi COG1472.
    HOGENOMi HOG000031215.
    KOi K05349.
    OMAi KTRWRGD.
    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 IPR026891. Fn3-like.
    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 PF14310. Fn3-like. 1 hit.
    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 nameiBGLI_ASPFU
    AccessioniPrimary (citable) accession number: Q4WU49
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 15, 2010
    Last sequence update: July 5, 2005
    Last modified: October 1, 2014
    This is version 58 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