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Q2UQV7

- AGDC_ASPOR

UniProt

Q2UQV7 - AGDC_ASPOR

Protein

Probable alpha/beta-glucosidase agdC

Gene

agdC

Organism
Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 48 (01 Oct 2014)
      Sequence version 1 (24 Jan 2006)
      Previous versions | rss
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    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 sitei573 – 5731Proton 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:AO090005001084
    OrganismiAspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
    Taxonomic identifieri510516 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
    ProteomesiUP000006564: 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 – 877863Probable alpha/beta-glucosidase agdCPRO_0000394917Add
    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
    Glycosylationi508 – 5081N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi574 – 5741N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi610 – 6101N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi744 – 7441N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Interactioni

    Protein-protein interaction databases

    STRINGi5062.CADAORAP00002956.

    Structurei

    3D structure databases

    ProteinModelPortaliQ2UQV7.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 31 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG1501.
    HOGENOMiHOG000041175.
    KOiK01187.
    OMAiSGQYLEY.
    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.

    Q2UQV7-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLGSLLLLAP LAGAAVIGSR ADTQQCPGYK ASNVQENDRS LTADLTLAGK    50
    PCNTYGTDLH NLKLLVEYQT DERLHVKIYD AEERVYQVPE KVTPRVDSGD 100
    GSSKDSALKF EYEEEPFSFT VKRDDEVLFD SSAENLIFQS QYLKLRTWLP 150
    ENPYLYGLGE HTDPLRLSTT NYTRTFWNRD AYGTSANSNL YGTHPVYYDH 200
    RGESGTHGVF LLNSNGMDVF IDKTADGKQY LEYNALGGIF DFYFFTGSNP 250
    KEASIEYSKI VGLPAMQSYW TFGLHQCRYG YRDVYQVAEV VYNYTKAGIP 300
    LETMWTDIDY MDRRRVFSLD PDRFPLEKMR ELVGYLHDHD QHYIVMVDPA 350
    VSVSDNGAFN RGLEQDVFLK TQNGSLYKGA VWPGVTAYPD WFHPDIQDYW 400
    NSEFSTFFNA ETGVDIDGLW IDMNEASNFC PDPCTDPERY SSENNLPPAP 450
    PPVRSSSPRP LPGFPADFQP SSASRSQKRI VKAKVGLEGR DLLNPPYKIR 500
    NEAGSLSNKT INTGIVHAGE GYAEYDTHNL YGTMMSSSSR EAMQYRRPEV 550
    RPLVITRSTY AGAGRDVGHW LGDNFSKWEH YRISIAEGLA FASMFQVPMV 600
    GADVCGFAGN TTEELCARWA SLGAFFTFYR NHNEIGNIGQ EFYVWPTVAE 650
    SARKAIDIRY RLLDYIYTSF YKQSQTGEPF LQPVFYLYPE DENTFSIDLQ 700
    FFYGDAILVS PVPDKGLTSV DAYFPDDIFY DWYTGTPVRG HGANITLSNI 750
    DITHIPLHIR GGSIIPIRSS SAMTTTELRE KSFQLIIAPG LDGTASGSLY 800
    LDDGDSLEQK ATLEVEFEYR KGVLHIDGKF ELHASLVESV TLLGQGKGGS 850
    RARREDGTKK TIQTNLELSK PTEIKLE 877
    Length:877
    Mass (Da):98,791
    Last modified:January 24, 2006 - v1
    Checksum:i7AECADB4113F457F
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AP007151 Genomic DNA. Translation: BAE56058.1.
    RefSeqiXP_001818060.1. XM_001818008.2.

    Genome annotation databases

    EnsemblFungiiCADAORAT00003003; CADAORAP00002956; CADAORAG00003003.
    GeneIDi5990005.
    KEGGiaor:AOR_1_1888174.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AP007151 Genomic DNA. Translation: BAE56058.1 .
    RefSeqi XP_001818060.1. XM_001818008.2.

    3D structure databases

    ProteinModelPortali Q2UQV7.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 5062.CADAORAP00002956.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii CADAORAT00003003 ; CADAORAP00002956 ; CADAORAG00003003 .
    GeneIDi 5990005.
    KEGGi aor:AOR_1_1888174.

    Phylogenomic databases

    eggNOGi COG1501.
    HOGENOMi HOG000041175.
    KOi K01187.
    OMAi SGQYLEY.
    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. "Genome sequencing and analysis of Aspergillus oryzae."
      Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K., Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H., Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.
      , Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D., Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A., Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y., Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H., Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T., Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O., Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y., Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N., Kikuchi H.
      Nature 438:1157-1161(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 42149 / RIB 40.

    Entry informationi

    Entry nameiAGDC_ASPOR
    AccessioniPrimary (citable) accession number: Q2UQV7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 15, 2010
    Last sequence update: January 24, 2006
    Last modified: October 1, 2014
    This is version 48 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