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Q5AWI5

- AGDC_EMENI

UniProt

Q5AWI5 - AGDC_EMENI

Protein

Alpha/beta-glucosidase agdC

Gene

agdC

Organism
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 55 (01 Oct 2014)
      Sequence version 2 (15 Jun 2010)
      Previous versions | rss
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    Functioni

    Glucosidase involved in the degradation of cellulosic biomass. Has both alpha- and beta-glucosidase activity.1 Publication

    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 sitei429 – 4291NucleophileBy similarity
    Active sitei432 – 4321By similarity
    Active sitei600 – 6001Proton donorBy similarity

    GO - Molecular functioni

    1. alpha-1,4-glucosidase activity Source: UniProtKB
    2. beta-glucosidase activity Source: UniProtKB
    3. carbohydrate binding Source: InterPro
    4. glucosidase activity Source: ASPGD
    5. hydrolase activity, hydrolyzing O-glycosyl compounds Source: ASPGD
    6. maltose alpha-glucosidase activity Source: UniProtKB-EC
    7. transferase activity, transferring glycosyl groups Source: ASPGD

    GO - Biological processi

    1. cellular carbohydrate catabolic process Source: ASPGD
    2. glucan catabolic process Source: UniProtKB
    3. maltose metabolic process Source: ASPGD
    4. starch metabolic process Source: ASPGD
    5. xyloglucan metabolic process Source: ASPGD

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism, Cell wall biogenesis/degradation, Polysaccharide degradation

    Protein family/group databases

    CAZyiGH31. Glycoside Hydrolase Family 31.
    mycoCLAPiAGL31C_EMENI.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Alpha/beta-glucosidase agdC (EC:3.2.1.20, EC:3.2.1.21)
    Gene namesi
    Name:agdC
    Synonyms:agdD
    ORF Names:AN7345
    OrganismiEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
    Taxonomic identifieri227321 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
    ProteomesiUP000000560: Chromosome IV

    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 – 2121Sequence AnalysisAdd
    BLAST
    Chaini22 – 894873Alpha/beta-glucosidase agdCPRO_0000394919Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi137 – 1371N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi178 – 1781N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi300 – 3001N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi402 – 4021N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi482 – 4821N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi483 – 4831N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi536 – 5361N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi601 – 6011N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi637 – 6371N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi802 – 8021N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Interactioni

    Protein-protein interaction databases

    STRINGi162425.CADANIAP00000088.

    Structurei

    3D structure databases

    ProteinModelPortaliQ5AWI5.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 31 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG1501.
    HOGENOMiHOG000041175.
    KOiK01187.
    OMAiMMSTATH.
    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.

    Sequencei

    Sequence statusi: Complete.

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

    Q5AWI5-1 [UniParc]FASTAAdd to Basket

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    MAGTLLSWTP LALALMARAL SQLPLTDCPG YRVINVEERP RGLTADLTLA    50
    GTPCNVYGVD IENLRLETDY DTNQRLHVKI YDADENVYQV PDSVFPRPVV 100
    NDQACADENT PELRFSYAED PFSFAVSRAS NDETLFNTTG HNLIFQSQYV 150
    NLRTSLPQNP NLYGLGEHSD PLRLNTINYT RTLWNRDAYT IPAGTNLYGA 200
    HPMYIDHRGE AGTHGVFLLN SNGMDIKIDK NSDNIQFLEY NILGGVLDFY 250
    FFAGPSPKDV SVQYAEVAGL PAMVPYWGLG FHQCRYGYRD IFEVAAVVHN 300
    YSEARIPLET MWTDIDYMDH RKVFTLDRER FPLDTVRALV QYLHQRDQHY 350
    IVMVDPAVAH SENGAFTRGL EKDVFMRKQD GTLYQGAVWP GATVFPDWFH 400
    PNTSDYWINE FALFFNAESG VDIDALWIDM NEAANFCDWP CTDPVAYAEE 450
    NNLPPEPPAV RPNPSSLPGF PAEFQPVNSN NNNSSRKRET QVVIAARQGF 500
    VKVGNDNGNG RRLGLQGREL IDPPYKIANA AGSLSNKTMN TDIFHANGLA 550
    EYDTHNLYGT MMSSLSRDAM LYRRPEKRPL VITRSTFAGA GSYVGHWLGD 600
    NASTWTKYRI SIAQMLAFAS IFQIPMVGSD ACGFTGNTTE ELCSRWATLA 650
    AFNPFFRNHN EYGMVSQEFY RWNSVAEAAR KAISIRYSLL DYLYTEFHEQ 700
    TVTGEPFLLP LFFVYPNDPN VVGIDSQFFY GDAILVSPVI EEGKTEVHAY 750
    FPGDLFYDWY TGLPLRGNGE VITLTDIGYT DIPLHVRGGK IVPVRTGSAG 800
    MNTTTEVRKS GFRLVIAPGL DGRAAGRLYI DDGESLEQTA MVDVVFTYED 850
    GRVSVDGVFT LQTDLRVEAV TVFGDNVVER TIDLPLSGPG GVEL 894
    Length:894
    Mass (Da):100,075
    Last modified:June 15, 2010 - v2
    Checksum:i6AE3AD13A10C594D
    GO

    Sequence cautioni

    The sequence EAA61716.1 differs from that shown. Reason: Erroneous gene model prediction.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DQ490507 mRNA. Translation: ABF50883.1.
    AACD01000128 Genomic DNA. Translation: EAA61716.1. Sequence problems.
    BN001304 Genomic DNA. Translation: CBF78576.1.
    RefSeqiXP_680614.1. XM_675522.1.

    Genome annotation databases

    EnsemblFungiiCADANIAT00000088; CADANIAP00000088; CADANIAG00000088.
    GeneIDi2869771.
    KEGGiani:AN7345.2.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DQ490507 mRNA. Translation: ABF50883.1 .
    AACD01000128 Genomic DNA. Translation: EAA61716.1 . Sequence problems.
    BN001304 Genomic DNA. Translation: CBF78576.1 .
    RefSeqi XP_680614.1. XM_675522.1.

    3D structure databases

    ProteinModelPortali Q5AWI5.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 162425.CADANIAP00000088.

    Protein family/group databases

    CAZyi GH31. Glycoside Hydrolase Family 31.
    mycoCLAPi AGL31C_EMENI.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii CADANIAT00000088 ; CADANIAP00000088 ; CADANIAG00000088 .
    GeneIDi 2869771.
    KEGGi ani:AN7345.2.

    Phylogenomic databases

    eggNOGi COG1501.
    HOGENOMi HOG000041175.
    KOi K01187.
    OMAi MMSTATH.
    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.
    ProtoNeti Search...

    Publicationsi

    1. "Development and application of a suite of polysaccharide-degrading enzymes for analyzing plant cell walls."
      Bauer S., Vasu P., Persson S., Mort A.J., Somerville C.R.
      Proc. Natl. Acad. Sci. U.S.A. 103:11417-11422(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
      Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
    3. "The 2008 update of the Aspergillus nidulans genome annotation: a community effort."
      Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J., Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M., Estrada C.G.
      , Geysens S., Goldman G., de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B., van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.
      Fungal Genet. Biol. 46:S2-13(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GENOME REANNOTATION.
      Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.

    Entry informationi

    Entry nameiAGDC_EMENI
    AccessioniPrimary (citable) accession number: Q5AWI5
    Secondary accession number(s): C8VCK6, Q1HFR7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 15, 2010
    Last sequence update: June 15, 2010
    Last modified: October 1, 2014
    This is version 55 of the entry and version 2 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