ID   AGDC_ASPOR              Reviewed;         877 AA.
AC   Q2UQV7;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   27-MAR-2024, entry version 90.
DE   RecName: Full=Probable alpha/beta-glucosidase agdC;
DE            EC=3.2.1.20;
DE            EC=3.2.1.21;
DE   Flags: Precursor;
GN   Name=agdC; ORFNames=AO090005001084;
OS   Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=510516;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42149 / RIB 40;
RX   PubMed=16372010; DOI=10.1038/nature04300;
RA   Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA   Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA   Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA   Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA   Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA   Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA   Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA   Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA   Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA   Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA   Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA   Kikuchi H.;
RT   "Genome sequencing and analysis of Aspergillus oryzae.";
RL   Nature 438:1157-1161(2005).
CC   -!- FUNCTION: Glucosidase involved in the degradation of cellulosic
CC       biomass. Has both alpha- and beta-glucosidase activity (By similarity).
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal, non-reducing (1->4)-linked alpha-D-
CC         glucose residues with release of alpha-D-glucose.; EC=3.2.1.20;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal, non-reducing beta-D-glucosyl residues
CC         with release of beta-D-glucose.; EC=3.2.1.21;
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 31 family. {ECO:0000305}.
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DR   EMBL; AP007151; BAE56058.1; -; Genomic_DNA.
DR   RefSeq; XP_001818060.1; XM_001818008.2.
DR   AlphaFoldDB; Q2UQV7; -.
DR   SMR; Q2UQV7; -.
DR   STRING; 510516.Q2UQV7; -.
DR   CAZy; GH31; Glycoside Hydrolase Family 31.
DR   GlyCosmos; Q2UQV7; 7 sites, No reported glycans.
DR   EnsemblFungi; BAE56058; BAE56058; AO090005001084.
DR   GeneID; 5990005; -.
DR   KEGG; aor:AO090005001084; -.
DR   VEuPathDB; FungiDB:AO090005001084; -.
DR   HOGENOM; CLU_000631_11_0_1; -.
DR   OMA; YKGAVWP; -.
DR   OrthoDB; 5480935at2759; -.
DR   Proteomes; UP000006564; Chromosome 1.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008422; F:beta-glucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0032450; F:maltose alpha-glucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0102483; F:scopolin beta-glucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR   CDD; cd06602; GH31_MGAM_SI_GAA; 1.
DR   CDD; cd14752; GH31_N; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.1760; glycosyl hydrolase (family 31); 1.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 2.
DR   InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR   InterPro; IPR030458; Glyco_hydro_31_AS.
DR   InterPro; IPR048395; Glyco_hydro_31_C.
DR   InterPro; IPR025887; Glyco_hydro_31_N_dom.
DR   InterPro; IPR000322; Glyco_hydro_31_TIM.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR22762; ALPHA-GLUCOSIDASE; 1.
DR   PANTHER; PTHR22762:SF67; ALPHA_BETA-GLUCOSIDASE AGDC-RELATED; 1.
DR   Pfam; PF13802; Gal_mutarotas_2; 1.
DR   Pfam; PF01055; Glyco_hydro_31_2nd; 1.
DR   Pfam; PF21365; Glyco_hydro_31_3rd; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
DR   PROSITE; PS00129; GLYCOSYL_HYDROL_F31_1; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Cell wall biogenesis/degradation; Glycoprotein;
KW   Glycosidase; Hydrolase; Polysaccharide degradation; Reference proteome;
KW   Secreted; Signal.
FT   SIGNAL          1..14
FT                   /evidence="ECO:0000255"
FT   CHAIN           15..877
FT                   /note="Probable alpha/beta-glucosidase agdC"
FT                   /id="PRO_0000394917"
FT   REGION          432..476
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        444..465
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        422
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10066"
FT   ACT_SITE        425
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        573
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        171
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        293
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        373
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        508
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        574
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        610
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        744
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   877 AA;  98791 MW;  7AECADB4113F457F CRC64;
     MLGSLLLLAP LAGAAVIGSR ADTQQCPGYK ASNVQENDRS LTADLTLAGK PCNTYGTDLH
     NLKLLVEYQT DERLHVKIYD AEERVYQVPE KVTPRVDSGD GSSKDSALKF EYEEEPFSFT
     VKRDDEVLFD SSAENLIFQS QYLKLRTWLP ENPYLYGLGE HTDPLRLSTT NYTRTFWNRD
     AYGTSANSNL YGTHPVYYDH RGESGTHGVF LLNSNGMDVF IDKTADGKQY LEYNALGGIF
     DFYFFTGSNP KEASIEYSKI VGLPAMQSYW TFGLHQCRYG YRDVYQVAEV VYNYTKAGIP
     LETMWTDIDY MDRRRVFSLD PDRFPLEKMR ELVGYLHDHD QHYIVMVDPA VSVSDNGAFN
     RGLEQDVFLK TQNGSLYKGA VWPGVTAYPD WFHPDIQDYW NSEFSTFFNA ETGVDIDGLW
     IDMNEASNFC PDPCTDPERY SSENNLPPAP PPVRSSSPRP LPGFPADFQP SSASRSQKRI
     VKAKVGLEGR DLLNPPYKIR NEAGSLSNKT INTGIVHAGE GYAEYDTHNL YGTMMSSSSR
     EAMQYRRPEV RPLVITRSTY AGAGRDVGHW LGDNFSKWEH YRISIAEGLA FASMFQVPMV
     GADVCGFAGN TTEELCARWA SLGAFFTFYR NHNEIGNIGQ EFYVWPTVAE SARKAIDIRY
     RLLDYIYTSF YKQSQTGEPF LQPVFYLYPE DENTFSIDLQ FFYGDAILVS PVPDKGLTSV
     DAYFPDDIFY DWYTGTPVRG HGANITLSNI DITHIPLHIR GGSIIPIRSS SAMTTTELRE
     KSFQLIIAPG LDGTASGSLY LDDGDSLEQK ATLEVEFEYR KGVLHIDGKF ELHASLVESV
     TLLGQGKGGS RARREDGTKK TIQTNLELSK PTEIKLE
//