ID A0A074W591_9PEZI Unreviewed; 778 AA.
AC A0A074W591;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN ORFNames=M437DRAFT_38316 {ECO:0000313|EMBL:KEQ68028.1};
OS Aureobasidium melanogenum CBS 110374.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX NCBI_TaxID=1043003 {ECO:0000313|EMBL:KEQ68028.1, ECO:0000313|Proteomes:UP000030672};
RN [1] {ECO:0000313|EMBL:KEQ68028.1, ECO:0000313|Proteomes:UP000030672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 110374 {ECO:0000313|EMBL:KEQ68028.1,
RC ECO:0000313|Proteomes:UP000030672};
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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family.
CC {ECO:0000256|ARBA:ARBA00005336}.
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DR EMBL; KL584824; KEQ68028.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A074W591; -.
DR STRING; 1043003.A0A074W591; -.
DR HOGENOM; CLU_004542_5_1_1; -.
DR OrthoDB; 5486783at2759; -.
DR Proteomes; UP000030672; Unassembled WGS sequence.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
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; PTHR30620:SF16; LYSOSOMAL BETA GLUCOSIDASE; 1.
DR PANTHER; PTHR30620; PERIPLASMIC BETA-GLUCOSIDASE-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 Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Reference proteome {ECO:0000313|Proteomes:UP000030672};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..778
FT /note="beta-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001701147"
FT DOMAIN 697..766
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 778 AA; 83965 MW; 489CD488E46D2C0A CRC64;
MVRLCVTGLA LASLSLAQAQ SNTSLANAIY KDASQSVDAR VENLLSLMTL EEKMAQLMQG
DISNWLNTTS GAYNQTGLEF NFANRSGMFY VGYPISWDWL AEGIKVGQDY AVNSTRLGIP
AIVQTEGIHG FLIENATIFN SPIAQACSFN RELQRQMGEQ IALEAAALGV TQLFAPLADL
ARELRYGRVE ETYGEDGYLA GEMAYNYVVG CQGQNVSAMV KHFAAYSEPE GGLNTAPVHG
GERELRTTWL PSFHRAIVDG GAYAIMSAYH AYDGIPAVAD YHMLTEILRD EWGYPYFVSS
DAGATDRLFK NFLTCGVNDF GCVTEQCLTA GNDVEMGGGS FNFRSIPDLV SNNTLDISVV
NEAVARVLRT KFQMGLFENP NPAAPKEQWN SIINNAAAKK LARDLDAESI VLLQNPNKTL
PLSKTDKIAV IGPMASGFMN YGDYVVYESQ YRGVQYLEGI RNAVGPSANA TVTYALGCER
WSTDESGIPE AVETAKNADV AVVIVGTWSR DQKELWAGLN ATTGEHIDES DLGLVGAQRA
LVKAVIDTGK PTVVVFSSGK PLTEDWISNT TASLAQQFYP GEEGGNALAD ILFGSVNPSG
KLSVSFPHDI GTLPAYYDFL NSGRPTYPGF VGADGNLYFG SSYILNTPVP WFPFGYGLSY
TTFDYGNVTL SSSQVSPTDN ITATISVTNN GTFDGAEVVQ LYVKDQVASV AVPNIQLKGF
EKVFIKAGET ATVSIPLNVA DIGLWNKSMK YVVEPGNFTI FVGSSSADFR ANATLTVV
//
