BGLH_EMENI
ID BGLH_EMENI Reviewed; 831 AA.
AC Q5B6C7; C8V6A3;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 2.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Probable beta-glucosidase H;
DE EC=3.2.1.21;
DE AltName: Full=Beta-D-glucoside glucohydrolase H;
DE AltName: Full=Cellobiase H;
DE AltName: Full=Gentiobiase H;
GN Name=bglH; ORFNames=AN3903;
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=CBF75131.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=EAA58834.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AACD01000063; EAA58834.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BN001302; CBF75131.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_661507.1; XM_656415.1.
DR AlphaFoldDB; Q5B6C7; -.
DR SMR; Q5B6C7; -.
DR STRING; 162425.CADANIAP00004796; -.
DR CAZy; GH3; Glycoside Hydrolase Family 3.
DR PRIDE; Q5B6C7; -.
DR EnsemblFungi; EAA58834; EAA58834; AN3903.2.
DR GeneID; 2873323; -.
DR KEGG; ani:AN3903.2; -.
DR eggNOG; ENOG502SMPY; Eukaryota.
DR HOGENOM; CLU_004542_4_0_1; -.
DR InParanoid; Q5B6C7; -.
DR OrthoDB; 175854at2759; -.
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; 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; 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..831
FT /note="Probable beta-glucosidase H"
FT /id="PRO_0000394881"
FT DOMAIN 389..549
FT /note="PA14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01164"
FT ACT_SITE 225
FT /evidence="ECO:0000250"
FT CARBOHYD 13
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 474
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 514
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 604
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 629
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 726
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 823
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 831 AA; 91333 MW; 8FD1F0D0767812A6 CRC64;
MTRTFDIDYV LANISDQDKI ALLSGIDFWH THPIPQFNVP SVRVTDGPNG IRGTKFFAGV
PAACLPCGTA LGATWDRDLL RRAGELLGDE CIAKGAHCWL GPTVNMQRSP LGGRGFESFS
EDPYLAGVAA ASMIVGCESK GIIATVKHFV GNDQEHERRA VDVIVTPRAL REIYLRPFQI
VARDARPGAL MTSYNKVNGK HVVEDPKMYD LIRKDWGWDP LVMSDWYGTY TTIDSTNAGL
DLEMPGVSRY RGKYIESAMQ ARLIKSSTLD ARARKVLEFV QRASRTKVSE VEKGRNHPED
RALMRTLCSN SIVLLKNEEN ILPLPKNVKK IALIGSHIKT PAISGGGSAA LKPYYASTLY
DAVREALPNA EVLYETGAHA HNMLPVIDRL LSNAVIHFYN EPMTQPNRKC LGTEPVTTTA
FQFMDYKLAG LNRALFWSTL IGDFTPDQSG IWDFGLSVFG TANLYINDEL IIDNTTKQTK
GTSFFGKGTR EEIGSMKLTA GQTYKIRIEF GSANTTTMKT TGMVNFGGGA ANLGASLRLD
AEEMINRAVK AAEDADYAII CTGLNQDWES EGFDRPHMDL PPVGIDKMIS GVLDIAAHKT
VIVNQSGTPV TMPWASRAKS IVHSWYGGNE TGHGIADILF GDVNPSGKLS LSWPIDVRHN
PAYLNYASVG GRVLYGEDIY VGYRFYEKTG REVLFPFGHG LSYTTFAVSP EALVSPGTFT
PENPSNATVK IKNIGGAAGA QVLQLYVAAP NSPTPRPQKE LQGFEKVFLR PGEEKTVIIR
LDKYATSFWD EIEGMWKSEA GVYEVLIGTS SEDIVARGQF EVNQTRYWSG L
