BGLH_ASPCL
ID BGLH_ASPCL Reviewed; 829 AA.
AC A1CUR8;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 72.
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=ACLA_087610;
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
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; DS027060; EAW07055.1; -; Genomic_DNA.
DR RefSeq; XP_001268481.1; XM_001268480.1.
DR AlphaFoldDB; A1CUR8; -.
DR SMR; A1CUR8; -.
DR STRING; 5057.CADACLAP00007648; -.
DR EnsemblFungi; EAW07055; EAW07055; ACLA_087610.
DR GeneID; 4699856; -.
DR KEGG; act:ACLA_087610; -.
DR VEuPathDB; FungiDB:ACLA_087610; -.
DR eggNOG; ENOG502SMPY; Eukaryota.
DR HOGENOM; CLU_004542_4_0_1; -.
DR OMA; CESTGVI; -.
DR OrthoDB; 175854at2759; -.
DR UniPathway; UPA00696; -.
DR Proteomes; UP000006701; 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_0000394876"
FT DOMAIN 389..548
FT /note="PA14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01164"
FT ACT_SITE 225
FT /evidence="ECO:0000250"
FT CARBOHYD 416
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 431
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"
SQ SEQUENCE 829 AA; 90774 MW; F6CD19443ADAD23C CRC64;
MTAKFDVDHV LNSISEDDKI ALLSGTDFWH TYSIPEHNVP PIRTTDGPNG VRGTKFFAGV
PAACLPCGTA LGATWDRDLL HKAGVLLGQE CLAKGAHCWL GPTINMQRSP LGGRGFESFA
EDPHLSGTMA KSIILGCEST GVISAVKHYV GNDQEHERRA VDVMVTPRAL REIYLRPFQI
VARDAHSGAL MTSYNKINGK HVVENPAMYD IIRKEWKWDP LIMSDWLGTY TTIDSLNAGL
DLEMPGPSRY RGKYIESAVQ ARLVKQSTID QRARKVLEFA ARASQAPASA VESGRDYPED
RALNREICGN SIVLLKNEDT LLPLPKKIKK IALIGSHVKT PAISGGGSAS LQPYYAVSLY
DAIIEVLPDT EIIYETGAYA HKMLPVIDRM LSNAVIRFYN EPADKERTLL STEPVNNTAF
QLMDYNTPGL NRTLFWATLD GEFTPDVSGL WDFGLTVFGT ATLYIDDEMV IDNTTQQTRG
TAFFGKGTIQ EVGAKELTAG RTYKIRIEFG SANTSPIKAI GVVHFGGGAA HLGAFLHMDP
EQMVRDAVKA ASEADYTILC TGLNRDWESE GFDRPDMDLP PRIDALISAV LDVAGDKTII
VNQSGTPVMM PWSDRARAII QAWYGGNETG HGIADVLFGD VNPCAKLPLS WPADVRHNPA
YLNSLSVGGR MLYGEDIYVG YRFYEKIGQV TLFPFGHGLS YTLFEVSPKV TVSPTAFTVE
TPLSATVRIK NTGPVAGAQI LQLYVAAPTS ATPRPVKELQ GFSKVFLQSG EEKTVVISVD
KYATSFWDGI EDMWKSEAGV YQVLIGTSSQ DIVARGEFTV DETTFWTGV
