AGDC_ASPFC
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 25-MAY-2022, entry version 53.
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 Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus
OS fumigatus).
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=CEA10 / CBS 144.89 / FGSC A1163;
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DS499594; EDP56838.1; -; Genomic_DNA.
DR AlphaFoldDB; B0XNL6; -.
DR SMR; B0XNL6; -.
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 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; 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
