ID A0A2X0MD09_9BASI Unreviewed; 894 AA.
AC A0A2X0MD09;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 12.
DE RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744, ECO:0000256|RuleBase:RU361161};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744, ECO:0000256|RuleBase:RU361161};
GN Name=BQ5605_C004g03079 {ECO:0000313|EMBL:SGY69927.1};
GN ORFNames=BQ5605_C004G03079 {ECO:0000313|EMBL:SGY69927.1};
OS Microbotryum silenes-dioicae.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Microbotryales; Microbotryaceae; Microbotryum.
OX NCBI_TaxID=796604 {ECO:0000313|EMBL:SGY69927.1, ECO:0000313|Proteomes:UP000249464};
RN [1] {ECO:0000313|EMBL:SGY69927.1, ECO:0000313|Proteomes:UP000249464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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 Evidence={ECO:0000256|ARBA:ARBA00000448,
CC ECO:0000256|RuleBase:RU361161};
CC -!- PATHWAY: Glycan metabolism; cellulose degradation.
CC {ECO:0000256|RuleBase:RU361161}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family.
CC {ECO:0000256|ARBA:ARBA00005336, ECO:0000256|RuleBase:RU361161}.
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DR EMBL; FQNC01000046; SGY69927.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2X0MD09; -.
DR STRING; 796604.A0A2X0MD09; -.
DR UniPathway; UPA00696; -.
DR Proteomes; UP000249464; Unassembled WGS sequence.
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; 2.60.120.260; Galactose-binding domain-like; 1.
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; 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 InterPro; IPR037524; PA14/GLEYA.
DR PANTHER; PTHR42715; BETA-GLUCOSIDASE; 1.
DR PANTHER; PTHR42715:SF28; BETA-GLUCOSIDASE-RELATED; 1.
DR Pfam; PF14310; Fn3-like; 1.
DR Pfam; PF00933; Glyco_hydro_3; 2.
DR Pfam; PF01915; Glyco_hydro_3_C; 1.
DR PRINTS; PR00133; GLHYDRLASE3.
DR SMART; SM01217; Fn3_like; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 1.
DR PROSITE; PS00775; GLYCOSYL_HYDROL_F3; 1.
DR PROSITE; PS51820; PA14; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|RuleBase:RU361161};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361161};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361161};
KW Polysaccharide degradation {ECO:0000256|RuleBase:RU361161};
KW Reference proteome {ECO:0000313|Proteomes:UP000249464}.
FT DOMAIN 428..590
FT /note="PA14"
FT /evidence="ECO:0000259|PROSITE:PS51820"
SQ SEQUENCE 894 AA; 96758 MW; EFE510A351B8C5C6 CRC64;
MARNYTQLDV DTTLAKLSVT EKTNLLAGKD FWHLNEVQRH GIPSVRVSDG PNGVRGTKFF
NGVKANCFPC STGLGASFDK PLAKKVGAAL GHEAHAKGAH VLLGPTCNMQ RSPLGGRGFE
SFAEDPHLSG MLTANYVEGV QSTGVAACVK HFVANDQEVC SLLFNATPKR CTHVLGEYIT
QFERFSSDSV VGARALREIY LEPFRLAVKH AHPLTFMSSY NRINGIHVSE SKDLLDDILR
KEWGFDGLVM SDWTGTYSTD AAVKAGLDLE MPGPTTMRGA AIGRMLAAGK LTVSDIDARV
RNVLELVNHA IASGIPFNGS ESLIDTPESR ALLREAANSA HVLLKNSDSL LPLKHAKKIA
VIGANAKVPV ASGGGSASLA STYTVSPLEG ITSAAKEIGA KVEFANGCST FRYLPLLDPL
MKNGKLEAWK DDFLDDWYQS KFDDAKAPEP DYQCNIDTSM GILVDDRSVY AKLGATPRTR
ISCTYTPETS GPYLIDLCTL GFGSVLIDGL VVLDNVKTRK SGEIFFGGGS EEESATIQLE
KGREYLIELR HSNNLTSAEA GPFSAMPQAI GFRLGLYPDQ PEEVARQEAV ELAKASDVAI
VVVGTNKDWE SEGFDRKTIA LPGAQDALVQ AVQAANPKTI IVTQSGCPVS MPWIEQASTV
LQAFFGGNEL GNALADIVFG KVNPSGKSPV QEAEQQAFDW NSQGQTGGQP FVRFVRDYFV
YARGSALHRT SIASSPPPPQ GIYMGYRHYD ANNIVTLFPF GFGLSYTTFS LSSLSRTPLS
SQAECTFSMK VRNTGSVPGR SVVQVYVRAV GGARGVDRPK KELIGFTKTS LLQPGEEEVV
KVEVTKEAFS YWDEKKGSWS VEEGEYEFLV GENSGELKLG EKVEVKEAFD WRGL
//
