ID A0A0D0CCB6_9AGAR Unreviewed; 741 AA.
AC A0A0D0CCB6;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN ORFNames=GYMLUDRAFT_251201 {ECO:0000313|EMBL:KIK52498.1};
OS Collybiopsis luxurians FD-317 M1.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Omphalotaceae; Collybiopsis;
OC Collybiopsis luxurians.
OX NCBI_TaxID=944289 {ECO:0000313|EMBL:KIK52498.1, ECO:0000313|Proteomes:UP000053593};
RN [1] {ECO:0000313|EMBL:KIK52498.1, ECO:0000313|Proteomes:UP000053593}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FD-317 M1 {ECO:0000313|EMBL:KIK52498.1,
RC ECO:0000313|Proteomes:UP000053593};
RG DOE Joint Genome Institute;
RG Mycorrhizal Genomics Consortium;
RA Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL Submitted (APR-2014) 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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family.
CC {ECO:0000256|ARBA:ARBA00005336}.
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DR EMBL; KN834842; KIK52498.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D0CCB6; -.
DR HOGENOM; CLU_004542_2_1_1; -.
DR OrthoDB; 5486783at2759; -.
DR Proteomes; UP000053593; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
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; 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 PANTHER; PTHR42715; BETA-GLUCOSIDASE; 1.
DR PANTHER; PTHR42715:SF14; BETA-GLUCOSIDASE D-RELATED; 1.
DR Pfam; PF14310; Fn3-like; 1.
DR Pfam; PF00933; Glyco_hydro_3; 1.
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.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:KIK52498.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000053593};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..741
FT /note="beta-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002207836"
FT TRANSMEM 709..730
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 647..717
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
FT REGION 19..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 741 AA; 79853 MW; 0FFCCFB3421C96C5 CRC64;
MLQTAFLILL VLGATAAPSD STDQTLDSPS FFPPSAPSLR STPSYNETAI LSSGYLDLGE
WQDAYNQASA FVSTLTNEEK VLLITRQDIP DKFTALNILD STVAPNTYYF VSTFPGSEAL
AMTWDKDLIY NVGHAIGSEH YNLGLNALNG PVTTPMGRSP WGGRNDKSLG PDAYLNGAGF
GRMVAGISSS GSITIGQHII LYEQETNRTG GVTTFVPNTP LTGSYKVVVD DKAFHETYLR
PWYDGVKNGL GGAMCAMNAF NGTRSCENAE LMNNYLKTEI GFLASYSEMS SYNAAISGMD
YSATTYWSND TILAGINNGS ISQARLDDMA VRGIMAWYKH GQNSGTPTYV SFTAYSNVRA
NHSAIIRDAA AKSIVLLKNN GVLPLGDDTS TMVLFGAHAG SALGGPNFQF SVLGSNDTYQ
GHLAAAGGSG TGSMSYIITP HHVLTNVAEK NGIMLFWIMN NTWTSEEING GVGSFAFYTS
STVAPITYAS YAGQAEVSIV FINAWSGEGA DRSELRNDEQ DELVATVAAN CNNTIVVVNT
VGPRILDAWI DHENVTAVLY AGMLGQQSGN SIVDVLYGRN ISPRYEFGYG LSYTTFAYGE
FSVQKQSDLA PGFFTGAHAV GGRADLWDEA ATVTFTITNT GTVAGTEIAQ LYMTYPSVAE
QPIRQLRGFE KVAIEPGESE TVTLRLLKRD FAFWNVTVTV ARSFLRYKLL IIVFKSCVFS
IQGISVTLAW SKIAMTFMIV G
//