BGLF_EMENI
ID BGLF_EMENI Reviewed; 868 AA.
AC Q5B6C6; C8V6A2;
DT 18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 2.
DT 25-MAY-2022, entry version 92.
DE RecName: Full=Probable beta-glucosidase F;
DE EC=3.2.1.21;
DE AltName: Full=Beta-D-glucoside glucohydrolase F;
DE AltName: Full=Cellobiase F;
DE AltName: Full=Gentiobiase F;
DE Flags: Precursor;
GN Name=bglF; ORFNames=AN10482;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
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=EAA58835.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AACD01000063; EAA58835.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BN001302; CBF75129.1; -; Genomic_DNA.
DR RefSeq; XP_661508.1; XM_656416.1.
DR AlphaFoldDB; Q5B6C6; -.
DR SMR; Q5B6C6; -.
DR STRING; 162425.CADANIAP00004795; -.
DR CAZy; GH3; Glycoside Hydrolase Family 3.
DR EnsemblFungi; CBF75129; CBF75129; ANIA_10482.
DR EnsemblFungi; EAA58835; EAA58835; AN3904.2.
DR GeneID; 2873326; -.
DR KEGG; ani:AN3904.2; -.
DR VEuPathDB; FungiDB:AN10482; -.
DR eggNOG; ENOG502QR4D; Eukaryota.
DR HOGENOM; CLU_007314_0_0_1; -.
DR InParanoid; Q5B6C6; -.
DR OMA; WHNGDKL; -.
DR OrthoDB; 559385at2759; -.
DR UniPathway; UPA00696; -.
DR Proteomes; UP000000560; Chromosome II.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0008422; F:beta-glucosidase activity; IBA:GO_Central.
DR GO; GO:0102483; F:scopolin beta-glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009251; P:glucan catabolic process; IBA:GO_Central.
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 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.
DR PROSITE; PS00775; GLYCOSYL_HYDROL_F3; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Cellulose degradation; Glycoprotein; Glycosidase;
KW Hydrolase; Polysaccharide degradation; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..868
FT /note="Probable beta-glucosidase F"
FT /id="PRO_0000394114"
FT REGION 21..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 731..752
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 285
FT /evidence="ECO:0000250"
FT CARBOHYD 65
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 73
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 257
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 328
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 360
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 395
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 421
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 726
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 868 AA; 93918 MW; 2CBEC9AF65A2E6F2 CRC64;
MAHRWLILAL VAAAAPRALA SPGPSLNERQ SDDEPFSPPY YPAPNGGWVS TWAEAYEKAH
SIVSNLTLAE KVNLTTGTGI FMGPCAGQTG SVPRLGIPNL CLHDSPLGVR NTDHNTAFPP
GITVGATFDK SLMYERGVGL GEEARGKGVN VLLGPSVGPL GRKPRGGRNW EGFGFDPVLQ
GIGGAETIKG MQSTGLIACI KHFVGNEQEM HRMSSVVTQG YSSNIDDRTL HELYIWPFAE
GVRAEVGSVM IAYNDVNKSS CSQNSKLING VLKDELGFQG FVVTDWLAHY GGVSSALAGL
DMDMPGDGAV PLFGNSYWGP ELSRSILNGT VPVERLNDMV TRILATWYKM GQDQDYPLPN
FSSNTEDEKG LLYPGAVISP IGVVNQYVNV QGNHNITARA IARDAITLLK NEGDLLPLRR
NDSLKVFGTD AGPDPQGLNS CADKGCNRGV LTMGWGSGTS KLPYLITPQE AIANITPTAE
FFITDSFPSS VDANDEDIAI VFINSDSGEN YITVDGNPGD RKTSGLHAWH NGDELVKAAA
ERFSQVVVVI HTVGPIILEE WIDLDSVKAV LIAHLPGQEA GYSLTDVLFG DYSPSGHLPY
TIPYQESNYP SSVGLLQQPF GQIQDYYTEG LYIDYRHFLK EDITPRYAFG HGLSYTTFEF
SEPALSVVTP LDSAYPPSRP AKGPTPTYPN TIPPASEAAW PAKFNRIWRY IYPYLNNPQA
DAAVANSSKT YPYPDGYSTD PQPPPRAGGA EGGNPALWDV AFSVQVTVTN TGQHSGRAVA
QLYVELPDSL GLDTPSRQLR QFEKTKVLET GQSETLTLEV TRKDVSVWDV EVQDWKTVVG
GEGVKIHIGE SVLDIRTECE VGGRCVTL
