BGLI_ASPOR
ID BGLI_ASPOR Reviewed; 839 AA.
AC Q2U8Y5;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 25-MAY-2022, entry version 88.
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=AO090701000244;
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(2005).
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; AP007164; BAE61980.1; -; Genomic_DNA.
DR RefSeq; XP_001823113.1; XM_001823061.2.
DR AlphaFoldDB; Q2U8Y5; -.
DR SMR; Q2U8Y5; -.
DR STRING; 510516.Q2U8Y5; -.
DR CAZy; GH3; Glycoside Hydrolase Family 3.
DR EnsemblFungi; BAE61980; BAE61980; AO090701000244.
DR GeneID; 5995170; -.
DR KEGG; aor:AO090701000244; -.
DR VEuPathDB; FungiDB:AO090701000244; -.
DR HOGENOM; CLU_004542_4_0_1; -.
DR OMA; GPTINTQ; -.
DR UniPathway; UPA00696; -.
DR Proteomes; UP000006564; Chromosome 5.
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; Reference proteome; Secreted.
FT CHAIN 1..839
FT /note="Probable beta-glucosidase I"
FT /id="PRO_0000394888"
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; 92142 MW; 0A3230F3AC56079F 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 SLDAYYTVTP
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 EYEVLVTGTG EGVLKSSFKV EKTRYWLGL
