AGDC_ASPCL
ID AGDC_ASPCL Reviewed; 887 AA.
AC A1CNK4;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 69.
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=ACLA_019300;
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
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; DS027059; EAW07225.1; -; Genomic_DNA.
DR RefSeq; XP_001268651.1; XM_001268650.1.
DR AlphaFoldDB; A1CNK4; -.
DR SMR; A1CNK4; -.
DR STRING; 5057.CADACLAP00003050; -.
DR EnsemblFungi; EAW07225; EAW07225; ACLA_019300.
DR GeneID; 4700931; -.
DR KEGG; act:ACLA_019300; -.
DR VEuPathDB; FungiDB:ACLA_019300; -.
DR eggNOG; KOG1065; Eukaryota.
DR HOGENOM; CLU_000631_11_0_1; -.
DR OMA; DAYFPDD; -.
DR OrthoDB; 151244at2759; -.
DR Proteomes; UP000006701; 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; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..887
FT /note="Probable alpha/beta-glucosidase agdC"
FT /id="PRO_0000394913"
FT REGION 457..483
FT /note="Disordered"
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 747
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 879
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 887 AA; 99904 MW; DAA2C23C3A28E665 CRC64;
MLRSLLLLAP MVGAAVAATE PNSPACPGYR ATNVREGHNS LTADLTLAGK PCNTYGTDLK
NLKLLVEYQT DERLHVKIYD ANEQVYQVPE SVVPRVDGKG GSRKKSVLKF NFKANPFSFQ
VKRGREVLFD TSGSNLVFQD QYLNLRTSLP RDPNLYGLGE HTDPLRLTTT NYTRTLWNRD
SYGIPENSNL YGSHPVYYDH RGEDGTHGVF LLNSNGMDIK IDKTKDGKQF LEYNALGGIF
DFYFFNGDTP KDASIEYAKV AGLPAMQSYW SFGFHQCRYG YRDAFEVAEV VQNYTQAKIP
LETMWTDIDY MDRRRVFTLD PDRFPLEKVR ELVSYLHKHD QKYIVMVDPA VSVSDNKGFN
DGMEQGVFMK HQNGSLYKGA VWPGVTAYPD WFHPDIQKYW DGQFNDFFSP EKGVDIDGLW
IDMNEAANFC TYPCLDPEGY SIENNLPPAA PPVRPNPRPL PGFPDDFQPP AASKRSVAKG
SKVGLPGRDL LNPRYQIRND AGLISSKTIN TDLIHAGEGY AEYDTHNLYG TMMSSASRQS
MAQRRPAVRP LIITRSTFAG AGTHVGHWLG DNLADWKHYR ISIAQMLSFA SMFQVPMVGS
DICGFGGDTN EELCARWARL GAFYPFFRNH NEITSIPQEF YRWESVAESA RKAIEVRYKL
LDYVYTAFHR QTQTGEPFLQ PMFYMYPEDK NTFSNDMQFF YGDSILVSPV HDVSQTSVEA
YFPKDIFYDW NTGDVLRGRG AKVTLSNISV TDIPIHIRGG SIVPIRSESA MTTVELRKKG
FELLIAPGQD GTASGTLYLD DGDSLKQSAS LELEFKYRKG NLQIKGKFGM HTDLKINAIT
LLGQTSVPRQ VTLSRAGKAD SKFDPARQSV TIKTDLSLNE SSEIDIN
