BGLE_ASPOR
ID BGLE_ASPOR Reviewed; 1048 AA.
AC Q2UTX5;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 2.
DT 25-MAY-2022, entry version 75.
DE RecName: Full=Probable beta-glucosidase E;
DE EC=3.2.1.21;
DE AltName: Full=Beta-D-glucoside glucohydrolase E;
DE AltName: Full=Cellobiase E;
DE AltName: Full=Gentiobiase E;
GN Name=bglE; ORFNames=AO090009000554;
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: Cell membrane {ECO:0000250}; Single-pass type II
CC membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE54990.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AP007150; BAE54990.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001816992.2; XM_001816940.2.
DR AlphaFoldDB; Q2UTX5; -.
DR SMR; Q2UTX5; -.
DR STRING; 510516.Q2UTX5; -.
DR CAZy; GH3; Glycoside Hydrolase Family 3.
DR EnsemblFungi; BAE54990; BAE54990; AO090009000554.
DR UniPathway; UPA00696; -.
DR Proteomes; UP000006564; Chromosome 1.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; 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 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; SSF51445; 1.
DR SUPFAM; SSF52279; SSF52279; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Cell membrane; Cellulose degradation;
KW Glycoprotein; Glycosidase; Hydrolase; Membrane; Polysaccharide degradation;
KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..1048
FT /note="Probable beta-glucosidase E"
FT /id="PRO_0000394873"
FT TOPO_DOM 1..150
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 151..171
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 172..1048
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 1..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 508..527
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 438
FT /evidence="ECO:0000250"
FT CARBOHYD 216
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 224
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 410
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 481
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 520
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 578
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 895
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 991
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1048 AA; 114456 MW; C11B8431841623DE CRC64;
MPPPPFRDAP SSAKSSQRYT PLHESIPEEL NDKQYSSDAD SLPLSDPSDG EDDSEIRLRR
VDRNGTRSNQ ATAYVPVVRK SGDVEAYFDS IAEAELELLS ASRQYDGVDD DDDDSDGYGV
GVKRGQRQGL LKRTHDGRTG WRTVYYSKYW WRALIGVVVV LVLLVLVFLG LARSKQVGDE
LDYSMIPAES WFPSPRGGAL KEWAADYQKA ALLVGNMTLI EKVNITTGTG WQMGLCVGNT
GPAESVHFPS LCLQDGPMGI RYADHISAFP PGLTTGATWN RDLIRERGIA MGLEARLKGV
NVLLGPSMGP LGMMPAGGRN WEAFGSDPVL QGVAAAETIK GIQSNGVMAT AKHFVMNEQE
HFRQPFEWGI PTALSSNVGD RALHEVFAWP FAESIRADVA SVMCAYQMVN NSHACENSKL
LNGILKDELG FQGFVQSDWL AQRSGINSAL GGLDMSMPGD GLHWADGKSL WGSELTRAVL
NTSIPMERLN DMVTRIVAAW YHLGQDQWER PPPDGEGGPN FSSWTDDQTG WWQQASVEAG
DQDGGWGIVN KYVDAGAGHG DIARKVAAEG IVLVKNNNNT LPLSRSPPSP YRIGIYGDDA
GPALGPNACP DRGCSQGTLA SGWGSGTVEF PFLVSPLEAL QGAWETEVEI TPYLQNMVMP
VSVQDKDLCL VFANANSGEG YIHAGGIHGD RNDLFLQKGG DTLIQAVANN CAGPTVVVVH
AVGPVVVESW IDLPGVDAVL FAHLPGQESG NALVDVLFGD VDASGRLPYT VGKSLEDYGP
GAQVLYENNA PVPQVDFLDA LYIDYRYFDK FNITPRYEFG FGLSYTSFEL SKLYIKSMQW
KSRLPKSRPQ DQVSPPEYDT RPPVNENVLF PEGFHALSKY VYSYLPSLDG TAAANYTEYP
DGYDLPRQPS EAGGDLGGNP SLYEEMAKVQ VQVANTGARA GQTVVQAYVS FPSDVVEEGD
LVEVPVDEKG ETVTFVPSKE QVEFPDRVLR NFTKIALEPG EKKTVEMTLS RKDLSYWSAR
QQNWVMPDGD FQIWVGQSSR DLPLHGKY
