ID A0A074XM17_9PEZI Unreviewed; 951 AA.
AC A0A074XM17;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 22-FEB-2023, entry version 33.
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 ORFNames=M436DRAFT_71080 {ECO:0000313|EMBL:KEQ75601.1};
OS Aureobasidium namibiae CBS 147.97.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX NCBI_TaxID=1043004 {ECO:0000313|EMBL:KEQ75601.1, ECO:0000313|Proteomes:UP000027730};
RN [1] {ECO:0000313|EMBL:KEQ75601.1, ECO:0000313|Proteomes:UP000027730}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 147.97 {ECO:0000313|EMBL:KEQ75601.1,
RC ECO:0000313|Proteomes:UP000027730};
RX PubMed=24984952;
RA Gostin Ar C., Ohm R.A., Kogej T., Sonjak S., Turk M., Zajc J., Zalar P.,
RA Grube M., Sun H., Han J., Sharma A., Chiniquy J., Ngan C.Y., Lipzen A.,
RA Barry K., Grigoriev I.V., Gunde-Cimerman N.;
RT "Genome sequencing of four Aureobasidium pullulans varieties:
RT biotechnological potential, stress tolerance, and description of new
RT species.";
RL BMC Genomics 15:549-549(2014).
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|ARBA:ARBA00004987, 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; KL584705; KEQ75601.1; -; Genomic_DNA.
DR RefSeq; XP_013429796.1; XM_013574342.1.
DR AlphaFoldDB; A0A074XM17; -.
DR STRING; 1043004.A0A074XM17; -.
DR GeneID; 25414881; -.
DR HOGENOM; CLU_004542_2_0_1; -.
DR OrthoDB; 5486783at2759; -.
DR UniPathway; UPA00696; -.
DR Proteomes; UP000027730; 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; 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 PANTHER; PTHR42715; BETA-GLUCOSIDASE; 1.
DR PANTHER; PTHR42715:SF12; BETA-GLUCOSIDASE A-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.
DR PROSITE; PS00775; GLYCOSYL_HYDROL_F3; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW ECO:0000256|RuleBase:RU361161};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
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|ARBA:ARBA00023326,
KW ECO:0000256|RuleBase:RU361161};
KW Reference proteome {ECO:0000313|Proteomes:UP000027730};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..951
FT /note="beta-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001704000"
FT DOMAIN 808..876
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 951 AA; 102446 MW; 47995419B140143E CRC64;
MSGFKSLALL LAAQLANAQG GYPNPPVAGL PFPGTNYPGS EVPYAVAGAQ FNQTSPPYYP
SPWGTGAGEW ASAYEKAIAF VSQLTLAEKV NLTTVSSWES EKCVGNTGSI PRLGFKSLCL
QDSPLGVRFG DFVSAFSAGV TVAATWDRSL AYTRGNDMGS EHRDKGVDVM LGPVVGPLGR
SPEGGRNWEG FSPDPVLSGI LNAETVKGIQ DAGVIACTKH YILNEQEHFR QGGPNISDAV
SANVDDITLH ELYVWPFADA VRAGTGSVMC SYNQANNSYV CQNSHLLNKV LKSELGFQGF
VVSDWSGQHS GVSSALAGLD MTMPGDVGFD SGTSFWGANL TIAVLNGTVP QYRIDDMAVR
IVAAWYLVDR EDHQVENAPN FSSWTTRTFG YRHYIAQEGY EQLNYHVDVQ EDHRDNIREV
AAKGTVLLKN NGALPLKGTE QLVGVFGEDA ADNQYGPNGC SDRGCDNGTL AMGWGSGTAN
FPYLVAPHSA IENEVRSHGK SVESILDRAA FSQIDVLAQR ADEVNGACIV FANADAGEGY
IIVDGNQGDR NNLTLWQGGE EVISHVAGLC KNTIVVLHTV GPVLINDWYD HENITAILWA
GVPGQESGNA IVDVLYGKVN PSGKLPFTLG KTRESYGTDL LYEYNNGGAA PQTQFEEGVF
IDYRAFDRAG ETPVYEFGYG LSYTNFSYSD ISVSVNTSAP AYVPASGFTE AAPVYGSISN
NSADYVFPAD VRPIEYYIYP YLNSTNLRAS SQDPYYGSNY SFPAGSASSA PQPLLPASGA
PGGNPGLYDI LYTVTATVTN TGSVEGEEVP QLYISLGGPD DPAVVLRQFD KFSIAPGASK
TFTAQITRRD ISNWSPALDD WYVSEYPKTV YVGSSSRKLP LKAALPANGA TSPGTGNVFE
PFVESLFISL YHSRWLQQLD YLHPALWLPL DLVERAGVVK SRRTHDDDIR F
//