AGDC_ASPOR
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 25-MAY-2022, entry version 85.
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 EnsemblFungi; BAE56058; BAE56058; AO090005001084.
DR GeneID; 5990005; -.
DR KEGG; aor:AO090005001084; -.
DR VEuPathDB; FungiDB:AO090005001084; -.
DR HOGENOM; CLU_000631_11_0_1; -.
DR OMA; DAYFPDD; -.
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 Gene3D; 2.60.40.1180; -; 2.
DR InterPro; IPR031727; Gal_mutarotase_N.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR000322; Glyco_hydro_31.
DR InterPro; IPR030458; Glyco_hydro_31_AS.
DR InterPro; IPR025887; Glyco_hydro_31_N_dom.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF13802; Gal_mutarotas_2; 1.
DR Pfam; PF01055; Glyco_hydro_31; 1.
DR Pfam; PF16863; NtCtMGAM_N; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF74650; SSF74650; 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
