ID A0A5N6FP46_PETAA Unreviewed; 821 AA.
AC A0A5N6FP46;
DT 22-APR-2020, integrated into UniProtKB/TrEMBL.
DT 22-APR-2020, sequence version 1.
DT 27-MAR-2024, entry version 11.
DE RecName: Full=beta-glucosidase {ECO:0000256|RuleBase:RU361161};
DE EC=3.2.1.21 {ECO:0000256|RuleBase:RU361161};
GN ORFNames=BDW43DRAFT_301595 {ECO:0000313|EMBL:KAB8231658.1};
OS Petromyces alliaceus (Aspergillus alliaceus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=209559 {ECO:0000313|EMBL:KAB8231658.1, ECO:0000313|Proteomes:UP000326931};
RN [1] {ECO:0000313|EMBL:KAB8231658.1, ECO:0000313|Proteomes:UP000326931}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 536.65 {ECO:0000313|EMBL:KAB8231658.1,
RC ECO:0000313|Proteomes:UP000326931};
RG DOE Joint Genome Institute;
RA Kjaerbolling I., Vesth T., Frisvad J.C., Nybo J.L., Theobald S.,
RA Kildgaard S., Isbrandt T., Kuo A., Sato A., Lyhne E.K., Kogle M.E.,
RA Wiebenga A., Kun R.S., Lubbers R.J., Makela M.R., Barry K., Chovatia M.,
RA Clum A., Daum C., Haridas S., He G., LaButti K., Lipzen A., Mondo S.,
RA Riley R., Salamov A., Simmons B.A., Magnuson J.K., Henrissat B.,
RA Mortensen U.H., Larsen T.O., Devries R.P., Grigoriev I.V., Machida M.,
RA Baker S.E., Andersen M.R.;
RT "Friends and foes A comparative genomics study of 23 Aspergillus species
RT from section Flavi.";
RL Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Beta-glucosidases are one of a number of cellulolytic enzymes
CC involved in the degradation of cellulosic biomass. Catalyzes the last
CC step releasing glucose from the inhibitory cellobiose.
CC {ECO:0000256|ARBA:ARBA00024983}.
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; ML733092; KAB8231658.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5N6FP46; -.
DR OMA; WASAYEQ; -.
DR OrthoDB; 5486783at2759; -.
DR UniPathway; UPA00696; -.
DR Proteomes; UP000326931; Unassembled WGS sequence.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
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:SF5; BETA-GLUCOSIDASE M-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 Cellulose degradation {ECO:0000256|ARBA:ARBA00023001};
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:UP000326931};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..821
FT /note="beta-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5024808285"
FT DOMAIN 738..805
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 821 AA; 89270 MW; 56AC94D420A6B009 CRC64;
MALFLRLLSA YGLALTVCGQ TFNNETTGEL QAVLTNLERH WSYGRSPPVY PSPAGNGAGD
WASAYEQAKA LVAQMTNDEK NNVTYGFPSA SNGCSGNSGA VPRLEFPGLC LQDAGNGVRG
LDMVNAYASG LHVGAAWNPD LAYKRGQYMG AEFKRKSINV ALGPVVGPLG RIARGGRNWE
GFSNDPYLCG KLAYETIIGM QESVIASVKH LVGNEQETDR NPSVYLVNAS VSSNIDDRTI
HELYMWPFQD AVKAGVGSVM CSYNRVNNSY ACQNSKSLNG LLKTELGFQG FTLTDWYAQH
TGVASANAGL DMAMPYSPYW GSGNLSLAVA NGSMTQSRLD DMATRIVATW YKFSKLKNPG
AYVPMNLSEP HEIIEARDPA SEHIIFQGAI EGHVLVKNVN SALPLKKPKI LSLFGYDAPA
ATSNSQTAAF SFQQGLGLGN TLSYLGGQLF SYEIMAALMG SFLVNTTGPG VALNGTLITG
GGSGSNTPAY IDAPFNAFQR QAKLDGTYLS WDFYSQDPGV NAASEACIVF VNEQSSEGWD
RPSLTDSYSD TLITNVAAKC NNTMVVIHNA GVRLVDTWIE HPNITAVIFA HVPGQDSGSA
LVEIMYGRQS PSGRLPYTVA KDPRDYGALL DPVYPDNSTM YYTQSNFTEG LYTDYRYFIA
NNITPRFEFG YGLTYSTFDY HNLEVHISGH ALKSYFPPGS EIYTTTEPKP PGGLDSLWDI
VATISCTVTN TGEVDAAEVA QLYVRIPGAG PDRLLRGFLK QTISPRNSLY LQFHLTRRDL
SQWDVLTQQW VLRDGTYEVM VSKSVLDIQL AGNLTITYDA I
//
