ID A0A1C7MG99_GRIFR Unreviewed; 825 AA.
AC A0A1C7MG99;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=bglK {ECO:0000313|EMBL:OBZ75489.1};
GN ORFNames=A0H81_04702 {ECO:0000313|EMBL:OBZ75489.1};
OS Grifola frondosa (Maitake) (Polyporus frondosus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Grifolaceae; Grifola.
OX NCBI_TaxID=5627 {ECO:0000313|EMBL:OBZ75489.1, ECO:0000313|Proteomes:UP000092993};
RN [1] {ECO:0000313|EMBL:OBZ75489.1, ECO:0000313|Proteomes:UP000092993}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=9006-11 {ECO:0000313|EMBL:OBZ75489.1,
RC ECO:0000313|Proteomes:UP000092993};
RA Min B., Park H., Kim J.-G., Cho H., Oh Y.-L., Kong W.-S., Choi I.-G.;
RT "Whole genome sequencing of Grifola frondosa 9006-11.";
RL Submitted (MAR-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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OBZ75489.1}.
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DR EMBL; LUGG01000004; OBZ75489.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C7MG99; -.
DR STRING; 5627.A0A1C7MG99; -.
DR OMA; QIHYRED; -.
DR OrthoDB; 5486783at2759; -.
DR UniPathway; UPA00696; -.
DR Proteomes; UP000092993; 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; 2.
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 InterPro; IPR011658; PA14_dom.
DR PANTHER; PTHR42715; BETA-GLUCOSIDASE; 1.
DR PANTHER; PTHR42715:SF26; BETA-GLUCOSIDASE; 1.
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; (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:UP000092993}.
FT DOMAIN 383..544
FT /note="PA14"
FT /evidence="ECO:0000259|PROSITE:PS51820"
SQ SEQUENCE 825 AA; 90277 MW; F37A2B16AAAF2DA2 CRC64;
MSRSFLDASI PDLVKSLSTD EKISLLGAPN WWNTNTVERL AIPAVRMSDG PNGVRGSSHF
VSTPAQCLPC ATSMASTFDP ELIHKRNPLG GRAFESFSED PHLSGTLAAA YVNGLQSKGV
ASAIKHFVAN DQEHERTAAE SVMSDRALRE VYLYPFMLAQ KHAHPWAFMT SYGRIGGVHC
AENPMLLQDI LRNEWGFDGI VMSDWFGTYS VDLAINAGLD LEMPGPPRWR TPVLVTHMLS
SQKVLPSTLD KRVGNVLSFV QHQARRNPDV VYGDGKERTR DTEEGRRFCR KLATEGMVVL
RNEHSVLPIK PAGKVKRVAL IGPNLKERVI SGGGSAALKA GYIVTPYEGI ISNAPDGLEF
SYEVGCYAHK YTPTLENLLK TPEGEPGWTC TFYNHDADGI PTGDPVAEYV LLDTRVKLND
FLPQGLTPTW TIKLRGSLTV EKTAEYELGL TVAGRAKLWV GGKPTVDNWT TQRPGDFFYG
QGTVEEIGLA HLVAGQPVEI LVEYTNTKPP EGPEADKSQP ALMRGVRLGG CEKIDPDKAI
LSAVELATAS DVVILVAGLS PDWESEGFDR PTLDMPGRTN ELIARVAQAN QNTVVCIQAG
SAVSMPWVND VNGLIQAWYS GNEGGNALAD VIYGRVNPSG RLPLTLPVRE QDIPAYLNTR
SENGKIHYRE DLFVGYKFYQ ARGIAPLFPF GFGLSYTSFS FSGLFLKEVN VSGPSFALDI
SLDVKNTGSV AGSEVVQLYV ALPDIGLTTP RLQLRGFAKT YILAPGELQC ITIKLDKYAV
SFWDAPDRMW RAKAGRYSVF VGKSSADILL EGFFLLSEEF TWSGL
//
