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)

Q4WRH9

- AGDC_ASPFU

UniProt

Q4WRH9 - AGDC_ASPFU

Protein

Probable alpha/beta-glucosidase agdC

Gene

agdC

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
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 52 (01 Oct 2014)
      Sequence version 1 (05 Jul 2005)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Glucosidase involved in the degradation of cellulosic biomass. Has both alpha- and beta-glucosidase activity By similarity.By similarity

    Catalytic activityi

    Hydrolysis of terminal, non-reducing (1->4)-linked alpha-D-glucose residues with release of alpha-D-glucose.
    Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei422 – 4221NucleophilePROSITE-ProRule annotation
    Active sitei425 – 4251By similarity
    Active sitei571 – 5711Proton donorBy similarity

    GO - Molecular functioni

    1. beta-glucosidase activity Source: UniProtKB-EC
    2. carbohydrate binding Source: InterPro
    3. maltose alpha-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 alpha/beta-glucosidase agdC (EC:3.2.1.20, EC:3.2.1.21)
    Gene namesi
    Name:agdC
    ORF Names:AFUA_1G16250
    OrganismiNeosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
    Taxonomic identifieri330879 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
    ProteomesiUP000002530: Chromosome 1

    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 – 1414Sequence AnalysisAdd
    BLAST
    Chaini15 – 881867Probable alpha/beta-glucosidase agdCPRO_0000394916Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi171 – 1711N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi293 – 2931N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi373 – 3731N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi506 – 5061N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi572 – 5721N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi608 – 6081N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi742 – 7421N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Interactioni

    Protein-protein interaction databases

    STRINGi5085.CADAFUAP00006886.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 31 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG1501.
    HOGENOMiHOG000041175.
    KOiK01187.
    OMAiNEAANFN.
    OrthoDBiEOG77T1CZ.

    Family and domain databases

    InterProiIPR011013. Gal_mutarotase_SF_dom.
    IPR000322. Glyco_hydro_31.
    IPR025887. Glyco_hydro_31_N_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PfamiPF13802. Gal_mutarotas_2. 1 hit.
    PF01055. Glyco_hydro_31. 1 hit.
    [Graphical view]
    SUPFAMiSSF51445. SSF51445. 2 hits.
    SSF74650. SSF74650. 1 hit.
    PROSITEiPS00129. GLYCOSYL_HYDROL_F31_1. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q4WRH9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLRSLLLLAP LVGAAVIGAR DHSQECPGYK ATNIREGRDS LTADLTLAGK    50
    PCNTYGTDLK NLKLLVEYQT DKRLHVKIYD ADEEVYQVPE SVLPRVDGKG 100
    GSSKKSALKF DYQANPFSFK VKRGGEVLFD TSGSNLIFQS QYLSLRTWLP 150
    EDPNLYGLGE HTDSLRLETT NYTRTLWNRD AYAIPEKTNL YGTHPVYYDH 200
    RGQHGTHGVF LLNSNGMDIK IDKTKDGKQY LEYNTLGGVF DFYFFTGATP 250
    KDASIEYAKV VGLPAMQSYW TFGFHQCRYG YRDVFEVAEV VYNYSQAKIP 300
    LETMWTDIDY MDRRRVFTLD PERFPLEKMR ELVSYLHNHN QHYIVMVDPA 350
    VSVSDNVGYN DGMEQGIFLQ TQNGSLYKGA VWPGVTAYPD WFHPDIQKYW 400
    NDQFAKFFDP KTGVDIDGLW IDMNEAANFC PYPCSDPEGY ARDNDLPPAA 450
    PPVRPSNPRP LPGFPGDFQP SSSSKRSTKG SKVGLPNRDL INPPYMIRNE 500
    AGSLSNKTIN TDIIHAGEGY AEYDTHNLYG TMMSSASRNA MQHRRPGVRP 550
    LVITRSTYAG AGAHVGHWLG DNISEWSKYR ISISQMLAFA SMFQVPMIGS 600
    DVCGFGGNTT EELCARWARL GAFYTFFRNH NEITGIPQEF YRWPTVAESA 650
    RKAIDIRYRL LDYIYTAFHR QTQTGEPFLQ PMFYLYPKDK NTFSNQLQFF 700
    YGDAILVSPV TDGSQTSVDA YFPDDIFYDW HTGAALRGRG ANVTLSNIDV 750
    TEIPIHIRGG SIIPVRSESA MTTTELRKKG FELIIAPGLD GTASGSLYLD 800
    DGDSIEPRAT LELEFTYRKG HLQVKGKFGF RTEVKINAVT LLGQSAPASK 850
    SADVASLDSG RQAVTIKTSL DLTGPSEIDL S 881
    Length:881
    Mass (Da):98,888
    Last modified:July 5, 2005 - v1
    Checksum:i15EE1FAA6A1FDAD3
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AAHF01000004 Genomic DNA. Translation: EAL90953.1.
    RefSeqiXP_752991.1. XM_747898.1.

    Genome annotation databases

    EnsemblFungiiCADAFUAT00006886; CADAFUAP00006886; CADAFUAG00006886.
    GeneIDi3510016.
    KEGGiafm:AFUA_1G16250.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AAHF01000004 Genomic DNA. Translation: EAL90953.1 .
    RefSeqi XP_752991.1. XM_747898.1.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 5085.CADAFUAP00006886.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii CADAFUAT00006886 ; CADAFUAP00006886 ; CADAFUAG00006886 .
    GeneIDi 3510016.
    KEGGi afm:AFUA_1G16250.

    Phylogenomic databases

    eggNOGi COG1501.
    HOGENOMi HOG000041175.
    KOi K01187.
    OMAi NEAANFN.
    OrthoDBi EOG77T1CZ.

    Family and domain databases

    InterProi IPR011013. Gal_mutarotase_SF_dom.
    IPR000322. Glyco_hydro_31.
    IPR025887. Glyco_hydro_31_N_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view ]
    Pfami PF13802. Gal_mutarotas_2. 1 hit.
    PF01055. Glyco_hydro_31. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51445. SSF51445. 2 hits.
    SSF74650. SSF74650. 1 hit.
    PROSITEi PS00129. GLYCOSYL_HYDROL_F31_1. 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 nameiAGDC_ASPFU
    AccessioniPrimary (citable) accession number: Q4WRH9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 15, 2010
    Last sequence update: July 5, 2005
    Last modified: October 1, 2014
    This is version 52 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