BGLJ_NEOFI
ID BGLJ_NEOFI Reviewed; 864 AA.
AC A1DNN8;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 84.
DE RecName: Full=Probable beta-glucosidase J;
DE EC=3.2.1.21;
DE AltName: Full=Beta-D-glucoside glucohydrolase J;
DE AltName: Full=Cellobiase J;
DE AltName: Full=Gentiobiase J;
GN Name=bglJ; ORFNames=NFIA_057590;
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 / NRRL 181
RC / 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: Beta-glucosidases are one of a number of cellulolytic enzymes
CC involved in the degradation of cellulosic biomass. Catalyzes the last
CC step releasing glucose from the inhibitory cellobiose (By similarity).
CC {ECO:0000250}.
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 -!- PATHWAY: Glycan metabolism; cellulose degradation.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family. {ECO:0000305}.
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DR EMBL; DS027698; EAW16409.1; -; Genomic_DNA.
DR RefSeq; XP_001258306.1; XM_001258305.1.
DR AlphaFoldDB; A1DNN8; -.
DR SMR; A1DNN8; -.
DR STRING; 36630.CADNFIAP00004470; -.
DR EnsemblFungi; EAW16409; EAW16409; NFIA_057590.
DR GeneID; 4584822; -.
DR KEGG; nfi:NFIA_057590; -.
DR VEuPathDB; FungiDB:NFIA_057590; -.
DR eggNOG; ENOG502QR4D; Eukaryota.
DR HOGENOM; CLU_004542_4_0_1; -.
DR OMA; WHTFAIP; -.
DR OrthoDB; 175854at2759; -.
DR UniPathway; UPA00696; -.
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:0102483; F:scopolin beta-glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 3.20.20.300; -; 1.
DR Gene3D; 3.40.50.1700; -; 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 InterPro; IPR037524; PA14/GLEYA.
DR InterPro; IPR011658; PA14_dom.
DR Pfam; PF14310; Fn3-like; 1.
DR Pfam; PF00933; Glyco_hydro_3; 1.
DR Pfam; PF01915; Glyco_hydro_3_C; 1.
DR Pfam; PF07691; PA14; 1.
DR PRINTS; PR00133; GLHYDRLASE3.
DR SMART; SM01217; Fn3_like; 1.
DR SMART; SM00758; PA14; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF52279; SSF52279; 1.
DR PROSITE; PS51820; PA14; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Cellulose degradation; Glycoprotein; Glycosidase;
KW Hydrolase; Polysaccharide degradation; Reference proteome; Secreted.
FT CHAIN 1..864
FT /note="Probable beta-glucosidase J"
FT /id="PRO_0000394895"
FT DOMAIN 411..578
FT /note="PA14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01164"
FT ACT_SITE 233
FT /evidence="ECO:0000250"
FT CARBOHYD 434
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 447
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 503
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 864 AA; 93160 MW; B620FB8B941D14A6 CRC64;
MGSLDTVDMG QRAIDQIISE LSLNEKVSLL SGVDAWHTFA IPRLGIPSIR TTDGPNGARG
TRYFNGVPSA CLPCGTALGA TFDKDLIFSL GQLLAAECKA KGAHVLLGPT INIQRGPLGG
RGFESFSEDP VLSGLAAASY CSGVQDGGVV PTLKHLVCND QEHERVAVSA LVTPRALREI
YLLPFQLAIR GARPGAVMTS YNKVNGLHAS ESPGLIRDIL RGEWGYEGAV ISDWFGTYSV
ADAVNAGLDL EMPGPTRFRG PALMHALTSN KVSEKTLNER VRKVLELVQL ASRSRVPEYA
PERKLNRPED RALLRRAAGE SVVLLKNDKN DNNNSPILPL DREKKTLVIG PNADIAAYCG
GGSASLLAYY TVTPRQGIAD KCGADQVVFS QGCYGHKELP LLGEHLRTIE TGEPGYTFRV
YTEPPAASGS FKGNGSRKPV DELHMTNSSA FLMDYSHPQI SGDTYYATLE GTLEPPESGV
YEFGLTVAGT GLLYIDGVLV VDNKTVQRAG TSFFGIGTVE ERGERYLEAG KKHHVFVEFG
TAPTSNLQHH GVVSFGPGGL RLGGCRKLDT DAAIQQAVQS AAQTDQVVVC VGLSGDWESE
GFDRPHMDLP PGTDELVNAV LEVQPNAVIV VQSGTPVTMP WADKAKALLQ AWYGGNEAGN
GIADVLFGDV NPSAKLPLTF PRELSQNPSY LSYRSERGRV LYSEDIYVGY RYYDKARQPP
LFRFGHGLSY TTFHLSDLAV RETAPYAANI KESSLRVSVT VSNTGARPGA EVVLVYVRPP
PATCSVGRPV RELKGYEKVM LQPGETREVS IAIPVGYATS FWDEGCDAWL SEKGLYFVEA
VGTGECNTLV APLSVQVSRM WNGL
