BGLI_ASPFN
ID BGLI_ASPFN Reviewed; 839 AA.
AC B8NDE2;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 2.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Probable beta-glucosidase I;
DE EC=3.2.1.21;
DE AltName: Full=Beta-D-glucoside glucohydrolase I;
DE AltName: Full=Cellobiase I;
DE AltName: Full=Gentiobiase I;
GN Name=bglI; ORFNames=AFLA_057030;
OS Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS / JCM 12722 / SRRC 167).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=332952;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC
RC 167;
RX PubMed=25883274; DOI=10.1128/genomea.00168-15;
RA Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT aflatoxin contamination of food and feed.";
RL Genome Announc. 3:E0016815-E0016815(2015).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EED51440.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; EQ963477; EED51440.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_002378447.1; XM_002378406.1.
DR AlphaFoldDB; B8NDE2; -.
DR SMR; B8NDE2; -.
DR STRING; 5059.CADAFLAP00006312; -.
DR eggNOG; ENOG502QR4D; Eukaryota.
DR UniPathway; UPA00696; -.
DR Proteomes; UP000001875; 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; IPR019800; Glyco_hydro_3_AS.
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; PS00775; GLYCOSYL_HYDROL_F3; 1.
DR PROSITE; PS51820; PA14; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Cellulose degradation; Glycoprotein; Glycosidase;
KW Hydrolase; Polysaccharide degradation; Secreted.
FT CHAIN 1..839
FT /note="Probable beta-glucosidase I"
FT /id="PRO_0000394885"
FT DOMAIN 395..555
FT /note="PA14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01164"
FT ACT_SITE 225
FT /evidence="ECO:0000250"
FT CARBOHYD 197
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 620
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 839 AA; 92082 MW; E52897D374F30765 CRC64;
MPRLDVEKTI EELSLGEKVA LTAGIDFWHT ASVPRLNIPT LRMSDGPNGV RGTRFFNGVP
AACFPCATAL GATWDTELLH EIGQLMGEES IAKGSHIILG PTINTQRSPL GGRGFESFAE
DGVLSGLLAG YISKGIQEKG VAATLKHFVC NDQEHQRMAV DSIVTQRALR EIYLLPFQLA
MRICRTACVM TAYNKVNGTH VSQNKEIITD ILRKEWGWDG LVMSDWFGTY STSDAINAGL
DLEMPGKTRW RGTALAHAVS SNEVAEFVMD ERVRNVLNLV NFVDGLNIPE NAPEKALNRP
QDQALLRRAA AESVVLMKNE EDILPLKKEK SILVIGPNSK VAAYCGGGSA SLDAYYTVNP
FEGVSAQSKG EVKFSQGVYS HKDLPLLGPL LKTADGKTGF SFKVYNEHPS ESNRELIEQL
HLVSSSGFLM DYVNPKIKSL TYYVDMEGLF TPEEDGVYDF GVTVVGTGQL FIDGELVVDN
TKNQRQGSAF FGSATVEEKG SKELKAGQTY KVLFQFGTAP TSDLDTRGVV VFGPGGFRFG
ASRRVGQEEL ISNAVKLASE AEQVVVFAGL TSEWETEGYD RDHMDLPPGS DEMISRVLDV
NPNAVVVIQS GTPVTMPWAN KTKALLHAWF GGNECGNGIA DVLYGDVNPS GKLPITFPVR
LQDNPSYVNF RSERGRVLYG EDVYVGYRYY EKVDLAPLFP FGHGLSYTTF TRSDLTLTTT
PEKPQYEESG EPITATVTVT NTGKVAGAEI VQLWVAPPAT EVNRPVRELK GFTKVFLQPG
EQKKVEIVVE KKLATSWFDE MREKWASEKG EYGVLVTGTG EGVLKSSFKV EKTRYWLGL