ID   AGDC_NEOFI              Reviewed;         881 AA.
AC   A1D1E6;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   27-MAR-2024, entry version 86.
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=NFIA_009180;
OS   Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS   / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=331117;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 /
RC   NRRL 181 / WB 181;
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; DS027688; EAW22239.1; -; Genomic_DNA.
DR   RefSeq; XP_001264136.1; XM_001264135.1.
DR   AlphaFoldDB; A1D1E6; -.
DR   SMR; A1D1E6; -.
DR   STRING; 331117.A1D1E6; -.
DR   GlyCosmos; A1D1E6; 7 sites, No reported glycans.
DR   EnsemblFungi; EAW22239; EAW22239; NFIA_009180.
DR   GeneID; 4591952; -.
DR   KEGG; nfi:NFIA_009180; -.
DR   VEuPathDB; FungiDB:NFIA_009180; -.
DR   eggNOG; KOG1065; Eukaryota.
DR   HOGENOM; CLU_000631_11_0_1; -.
DR   OMA; YKGAVWP; -.
DR   OrthoDB; 5480935at2759; -.
DR   Proteomes; UP000006702; 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; Reference proteome;
KW   Secreted; Signal.
FT   SIGNAL          1..14
FT                   /evidence="ECO:0000255"
FT   CHAIN           15..881
FT                   /note="Probable alpha/beta-glucosidase agdC"
FT                   /id="PRO_0000394920"
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;  99054 MW;  8311042A49FCA1D0 CRC64;
     MLRSLLLLAP LVGAAVLGVR DNSQECPGYK ATNIREGRNS LTADLTLAGT PCNTYGTDLK
     NLKLLVEYQT DKRLHVKIYD ADEEVYQVPE SVLPRVDGKG GSGKKSALKF DYQANPFSFK
     VKRGGEVLFD TSGSNLIFQS QYLNLRTWLP EDPNLYGLGE HTDSLRLETT NYTRTLWNRD
     AYAIPEKTNL YGTHPVYYDH RGQDGTHGVF LLNSNGMDIK IDKTEDGKQY LEYNTLGGVF
     DFYFFTGATP KDASIEYAKV VGLPAMQSYW TFGFHQCRYG YRDVFEVAEV VYNYTQAKIP
     LETMWTDIDY MDRRRVFTLD PERFPLEKLR ELVTYLHNHN QRYIVMVDPA VSVSDNVGYN
     DGMEQGIFLQ TQNGSLYKGA VWPGVTAYPD WFHPDIQKYW NDQFAKFFDR KTGVDIDGLW
     IDMNEAANFC PYPCSDPEGY SRDNDLPPAA PPVRPSNPRP LPGFPGDFQP SSSSKRSTKG
     SKVGLPNRDL INPPYMIRNE AGSLSNKTIN TDIIHAGEGY AEYDTHNLYG TMMSSASRNA
     MQHRRPEVRP LVITRSTYAG AGAHVGHWLG DNISEWSKYR VSIAQMLAFA SMFQVPMIGS
     DVCGFGGNTT EELCARWARL GAFYTFFRNH NEITGIPQEF YRWPTVAESA RKAIDIRYRL
     LDYIYTAFHR QTQTGEPFLQ PMFYLYPKDK NTFSNQLQFF YGDAILVSPV TDGSQTSVDA
     YFPDDIFYDW HTGAALRGRG ANVTLGNIDV TEIPIHIRGG SIIPIRSESA MTTTELRKKG
     FELIIAPGLD GTASGSLYLD DGDSIEQRAT LELEFTYRKG RLRVKGKFGF RTDVKINAVT
     LLGQSAPASK SGSVASFDSG RQAVTIKTSL DLTGPSEIDL N
//