BGLH_NEOFI
ID BGLH_NEOFI Reviewed; 829 AA.
AC A1DPG0;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 78.
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=NFIA_060370;
OS Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=331117;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC / WB 181;
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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; DS027698; EAW16681.1; -; Genomic_DNA.
DR RefSeq; XP_001258578.1; XM_001258577.1.
DR AlphaFoldDB; A1DPG0; -.
DR SMR; A1DPG0; -.
DR STRING; 36630.CADNFIAP00004863; -.
DR EnsemblFungi; EAW16681; EAW16681; NFIA_060370.
DR GeneID; 4585094; -.
DR KEGG; nfi:NFIA_060370; -.
DR VEuPathDB; FungiDB:NFIA_060370; -.
DR eggNOG; ENOG502SMPY; Eukaryota.
DR HOGENOM; CLU_004542_4_0_1; -.
DR OMA; CESTGVI; -.
DR OrthoDB; 175854at2759; -.
DR UniPathway; UPA00696; -.
DR Proteomes; UP000006702; Unassembled WGS sequence.
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; 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..829
FT /note="Probable beta-glucosidase H"
FT /id="PRO_0000394882"
FT DOMAIN 389..548
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 304
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 473
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 602
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 627
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 664
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 829 AA; 90819 MW; 76A219B2EEEF9D68 CRC64;
MTAKFDVDYV LANITEDDKI ALLSGSDFWH THAIPKFNVP PIRTTDGPNG IRGTKFFAGV
PAACLPCGTA LGATWDRDLL HQAGVLLGKE CLAKGAHCWL GPTINMQRSP LGGRGFESFA
EDPHLSGIMA KSIILGCEST GVISTVKHYV GNDQEHERRA VDVLVTPRAL REIYLRPFQI
VARDAHPGAL MTSYNKINGK HVVENPAMLD IVRKDWNWDP LIMSDWLGTY TTIDSMNAGL
DLEMPGPTRY RGKYIESAMQ ARLIKQSTIN KRARKVLEFV QRASRAPVSA DETGRDFPED
RALNRTLCAN SIVLLKNDGN LLPIPKTVKK IALIGSHVKT PAISGGGSAS LEPYYAVSLY
DAVVEALPDA KILYEAGAYA HKMLPVIDRM LSNAVIHFYN EPPEKERTLL ATEPVVNTAF
QLMDYNAPGL NRGLFWATLI GEFTPDVSGL WDFGLTVFGT ATLFVDDEMV IDNTTRQTRG
TAFFGKGTVQ EVGQKQLTAG QTYKIRIEFG SANTSPMKAI GVVHFGGGAA HLGACLHMDP
EQMVANAVKV AAEADYTIVC TGLNRDWESE GFDRPDMDLP PGIDALISSV LDLAADRTVI
VNQSGTPVTL PWADRARGVV QAWYGGNETG HGIADVLFGD VNPCGKLPLS WPVDVKHNPA
YLNNMSVGGR MLYGEDVYMG YRFYEKVGRE VLFPFGHGLS YTTFSVSPEA TVSPSVFSSD
SPPTARVLVK NTGPVAGAQI LQLYIAAPNS ATPRPVKELH GFTKVFLQPG EERTVAIHID
KYATSFWDEI EDMWKSEEGV YQVLIGTSSQ EIVSRGEFRV EQTRYWRGV
