ID   AGDC_ASPFC              Reviewed;         881 AA.
AC   B0XNL6;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   27-MAR-2024, entry version 58.
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=AFUB_015590;
OS   Aspergillus fumigatus (strain CBS 144.89 / FGSC A1163 / CEA10) (Neosartorya
OS   fumigata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=451804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 144.89 / FGSC A1163 / CEA10;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
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; DS499594; EDP56838.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0XNL6; -.
DR   SMR; B0XNL6; -.
DR   GlyCosmos; B0XNL6; 7 sites, No reported glycans.
DR   EnsemblFungi; EDP56838; EDP56838; AFUB_015590.
DR   VEuPathDB; FungiDB:AFUB_015590; -.
DR   HOGENOM; CLU_000631_11_0_1; -.
DR   PhylomeDB; B0XNL6; -.
DR   Proteomes; UP000001699; Unassembled WGS sequence.
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; Secreted; Signal.
FT   SIGNAL          1..14
FT                   /evidence="ECO:0000255"
FT   CHAIN           15..881
FT                   /note="Probable alpha/beta-glucosidase agdC"
FT                   /id="PRO_0000394914"
FT   REGION          440..485
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        448..465
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        467..481
FT                   /note="Polar 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        571
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        506
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        572
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        608
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        742
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   881 AA;  98888 MW;  15EE1FAA6A1FDAD3 CRC64;
     MLRSLLLLAP LVGAAVIGAR DHSQECPGYK ATNIREGRDS LTADLTLAGK PCNTYGTDLK
     NLKLLVEYQT DKRLHVKIYD ADEEVYQVPE SVLPRVDGKG GSSKKSALKF DYQANPFSFK
     VKRGGEVLFD TSGSNLIFQS QYLSLRTWLP EDPNLYGLGE HTDSLRLETT NYTRTLWNRD
     AYAIPEKTNL YGTHPVYYDH RGQHGTHGVF LLNSNGMDIK IDKTKDGKQY LEYNTLGGVF
     DFYFFTGATP KDASIEYAKV VGLPAMQSYW TFGFHQCRYG YRDVFEVAEV VYNYSQAKIP
     LETMWTDIDY MDRRRVFTLD PERFPLEKMR ELVSYLHNHN QHYIVMVDPA VSVSDNVGYN
     DGMEQGIFLQ TQNGSLYKGA VWPGVTAYPD WFHPDIQKYW NDQFAKFFDP KTGVDIDGLW
     IDMNEAANFC PYPCSDPEGY ARDNDLPPAA PPVRPSNPRP LPGFPGDFQP SSSSKRSTKG
     SKVGLPNRDL INPPYMIRNE AGSLSNKTIN TDIIHAGEGY AEYDTHNLYG TMMSSASRNA
     MQHRRPGVRP LVITRSTYAG AGAHVGHWLG DNISEWSKYR ISISQMLAFA SMFQVPMIGS
     DVCGFGGNTT EELCARWARL GAFYTFFRNH NEITGIPQEF YRWPTVAESA RKAIDIRYRL
     LDYIYTAFHR QTQTGEPFLQ PMFYLYPKDK NTFSNQLQFF YGDAILVSPV TDGSQTSVDA
     YFPDDIFYDW HTGAALRGRG ANVTLSNIDV TEIPIHIRGG SIIPVRSESA MTTTELRKKG
     FELIIAPGLD GTASGSLYLD DGDSIEPRAT LELEFTYRKG HLQVKGKFGF RTEVKINAVT
     LLGQSAPASK SADVASLDSG RQAVTIKTSL DLTGPSEIDL S
//