ID BGLN_EMENI Reviewed; 670 AA.
AC Q5B681; C8V626;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 27-MAR-2024, entry version 90.
DE RecName: Full=Probable beta-glucosidase N;
DE EC=3.2.1.21;
DE AltName: Full=Beta-D-glucoside glucohydrolase N;
DE AltName: Full=Cellobiase N;
DE AltName: Full=Gentiobiase N;
DE Flags: Precursor;
GN Name=bglN; ORFNames=AN3949;
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}.
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DR EMBL; AACD01000064; EAA59258.1; -; Genomic_DNA.
DR EMBL; BN001302; CBF75028.1; -; Genomic_DNA.
DR RefSeq; XP_661553.1; XM_656461.1.
DR AlphaFoldDB; Q5B681; -.
DR SMR; Q5B681; -.
DR STRING; 227321.Q5B681; -.
DR CAZy; GH3; Glycoside Hydrolase Family 3.
DR GlyCosmos; Q5B681; 6 sites, No reported glycans.
DR EnsemblFungi; CBF75028; CBF75028; ANIA_03949.
DR GeneID; 2873370; -.
DR KEGG; ani:AN3949.2; -.
DR eggNOG; ENOG502QR4D; Eukaryota.
DR HOGENOM; CLU_004542_2_1_1; -.
DR InParanoid; Q5B681; -.
DR OMA; CENDHIM; -.
DR OrthoDB; 2281617at2759; -.
DR UniPathway; UPA00696; -.
DR Proteomes; UP000000560; Chromosome II.
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; 3.40.50.1700; Glycoside hydrolase family 3 C-terminal domain; 1.
DR Gene3D; 3.20.20.300; Glycoside hydrolase, family 3, N-terminal domain; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR026891; Fn3-like.
DR InterPro; IPR002772; Glyco_hydro_3_C.
DR InterPro; IPR036881; Glyco_hydro_3_C_sf.
DR InterPro; IPR036962; Glyco_hydro_3_N_sf.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR PANTHER; PTHR42715; BETA-GLUCOSIDASE; 1.
DR PANTHER; PTHR42715:SF20; BETA-GLUCOSIDASE E-RELATED; 1.
DR Pfam; PF14310; Fn3-like; 1.
DR Pfam; PF01915; Glyco_hydro_3_C; 2.
DR SMART; SM01217; Fn3_like; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 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..21
FT /evidence="ECO:0000255"
FT CHAIN 22..670
FT /note="Probable beta-glucosidase N"
FT /id="PRO_0000394911"
FT REGION 65..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 152
FT /evidence="ECO:0000250"
FT CARBOHYD 51
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 141
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 184
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 248
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 330
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 417
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 670 AA; 72928 MW; 3E9B3263827188EC CRC64;
MHSNILPVLT SVATLLGLVQ GQSQQPYRDW AKAYEAAETL VLPWTLEQQA NISVRDGTAP
GFVPFEPSDG VRSVQGSGKD YDNPAMRTSS NLDDRTLHEL YLWPWIDGVA NGLGSVMCVM
NRVNGIIGCE NDHIMNGILK NETGFRGFIV PDVTAPVDKA AGLLGGLGWN SGYSVSEIMA
AVKNGSIPES VMTEHALRIV ATQLNLLQPP EEYAFPVETA DLNVRDPSSK DFIRRAGSES
IVLLKNKNNT LPLRSPMSLG IFGKDAANLA TGPTPQSDFS NFAGDTYDGH LITGGGSYSP
APYVVSPLDA LTARAADGQG FGYKYILSDN WTVTPSESTG EGFFQTSGVS VSQYARESEH
CLVFINAFGK EGSDRRTLAD ETGDKLVNDV ADYCGSTIVI INNAGVRLVD AWIEHENVTV
FTDLIPCSNQ VHTNMFCFPG CPERRRSRQE SGHAIVDVLF GDVNPSAKLV YTIAKSKDDY
NGQICECCEC DYTEGLYIDY RHFDQAGIEP RFEFGFGLCF KSDGRANIAA YTTFTHSDLT
INPSTDITTL QPYATGPITE GGPSDLFEQI LTISASISNT GGVAGAEVAQ LYLSFPDAAK
APVRQLRGFE KVYLEPGETK FVSFPIQRRD LSIWDEQTSK WKIVGGKYGV VLGRSSRDFT
VEETLELLTI
//
