ID A1DFB9_NEOFI Unreviewed; 780 AA.
AC A1DFB9;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN ORFNames=NFIA_080180 {ECO:0000313|EMBL:EAW18076.1};
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 {ECO:0000313|EMBL:EAW18076.1, ECO:0000313|Proteomes:UP000006702};
RN [1] {ECO:0000313|Proteomes:UP000006702}
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 {ECO:0000313|Proteomes:UP000006702};
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 -!- 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 Evidence={ECO:0000256|ARBA:ARBA00000448};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family.
CC {ECO:0000256|ARBA:ARBA00005336}.
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DR EMBL; DS027696; EAW18076.1; -; Genomic_DNA.
DR RefSeq; XP_001259973.1; XM_001259972.1.
DR AlphaFoldDB; A1DFB9; -.
DR STRING; 331117.A1DFB9; -.
DR EnsemblFungi; EAW18076; EAW18076; NFIA_080180.
DR GeneID; 4586529; -.
DR KEGG; nfi:NFIA_080180; -.
DR VEuPathDB; FungiDB:NFIA_080180; -.
DR eggNOG; ENOG502QQ55; Eukaryota.
DR HOGENOM; CLU_004542_5_1_1; -.
DR OMA; MSAYHSY; -.
DR OrthoDB; 5486783at2759; -.
DR Proteomes; UP000006702; Unassembled WGS sequence.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1700; Glycoside hydrolase family 3 C-terminal domain; 1.
DR Gene3D; 3.20.20.300; Glycoside hydrolase, family 3, N-terminal domain; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR026891; Fn3-like.
DR InterPro; IPR002772; Glyco_hydro_3_C.
DR InterPro; IPR036881; Glyco_hydro_3_C_sf.
DR InterPro; IPR001764; Glyco_hydro_3_N.
DR InterPro; IPR036962; Glyco_hydro_3_N_sf.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR PANTHER; PTHR30620:SF16; LYSOSOMAL BETA GLUCOSIDASE; 1.
DR PANTHER; PTHR30620; PERIPLASMIC BETA-GLUCOSIDASE-RELATED; 1.
DR Pfam; PF14310; Fn3-like; 1.
DR Pfam; PF00933; Glyco_hydro_3; 1.
DR Pfam; PF01915; Glyco_hydro_3_C; 1.
DR PRINTS; PR00133; GLHYDRLASE3.
DR SMART; SM01217; Fn3_like; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Reference proteome {ECO:0000313|Proteomes:UP000006702};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..780
FT /note="beta-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002633963"
FT DOMAIN 699..768
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 780 AA; 85347 MW; 758660A0299736EC CRC64;
MVGTFLSKSL LLLQLVSALS TGQAASMPLY KDPSAPVEDR VSDLLGRMTI DDKMAQLMQG
DITNWMNSTS GAFNYTGLVE NMKMKAGSFY VGYPVSWDWI ATNVKRAQDY LMQNTTLGIP
ALVQTEGIHG FLTGNATIFN SPIAYGCSFN RELVQEMAKY VAQEARTLGV TQIFAPVVDL
ARELRFGRVE ETFGEDPYLS GEMGYSYVKG LQSLNVSSMV KHFIGFSQPE QGINTAPVHG
GERYLRTTWF PSFKRAIIDA GAWSIMSAYH SYDGIPAVSD YHTLTEILRG EWGYDFFVMS
DAGGTDRLCS AFKLCRSNPI DMEAVTLQVL PAGNDVEMGG GSFNFRKIPE LIKAGKLDIK
TVDTAVSRVL RAKFEMGLFE NPYPAAPKSQ WNKLIHSKEA VKLARQLDKE SIVLLENHNN
TLPLKKKGDI AVIGPMAHGF MNYGDYVVYK SQYRGVTPLD GIKAAVGKKA NIHYAKGCER
WSNDQSGFAE AVEAAKKSDV AIVVVGTWSR DQMELWQGLN ATTGEHVDVN DLSLVGAQAP
LIKAIVDTGV PTIVVLSSGK PVTETWLSNS TAALVQQFYP SEEGGNALAD VLFGDYNPSG
KLSVSFPSYV GDLPIYYDYL NSARSIGDSG YELPNGTLVF GHQYVFGSPL PWYPFGYGKS
YSTFEYGPVT VDKANVTASD TVTVSVDVTN THKSMDGTEV VQVYIQDEIS SVVVPNRQLK
GFEKVVIPAK KTKTVKIKIK VQDLGLWNSA MKYVVEPGAF TALVGSSSAD IRGNATFYVQ
//
