ID A0A0M8PB04_9EURO Unreviewed; 842 AA.
AC A0A0M8PB04;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=ACN38_g266 {ECO:0000313|EMBL:KOS48788.1};
OS Penicillium nordicum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=229535 {ECO:0000313|EMBL:KOS48788.1, ECO:0000313|Proteomes:UP000037696};
RN [1] {ECO:0000313|EMBL:KOS48788.1, ECO:0000313|Proteomes:UP000037696}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DAOMC 185683 {ECO:0000313|EMBL:KOS48788.1,
RC ECO:0000313|Proteomes:UP000037696};
RA Nguyen H.D., Seifert K.A.;
RT "Genome sequencing of Penicillium nordicum.";
RL Submitted (AUG-2015) 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|ARBA:ARBA00004987, 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:KOS48788.1}.
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DR EMBL; LHQQ01000002; KOS48788.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M8PB04; -.
DR STRING; 229535.A0A0M8PB04; -.
DR OrthoDB; 5486783at2759; -.
DR UniPathway; UPA00696; -.
DR Proteomes; UP000037696; 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; 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 InterPro; IPR037524; PA14/GLEYA.
DR InterPro; IPR011658; PA14_dom.
DR PANTHER; PTHR42715; BETA-GLUCOSIDASE; 1.
DR PANTHER; PTHR42715:SF13; BETA-GLUCOSIDASE K-RELATED; 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|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:UP000037696}.
FT DOMAIN 407..567
FT /note="PA14"
FT /evidence="ECO:0000259|PROSITE:PS51820"
SQ SEQUENCE 842 AA; 92005 MW; AF1D58C1D3D31D9F CRC64;
MESPCSLFDV DKVLREATVA EKVGLISGKD AWHTYDIPRL GVPSIRFTDG SDGARGTRFD
VCLPCGTALG ATWNRELVRQ GGELIGLEVK ASGAQIWLGP TVNIQRSPLG GRNFESFAED
PLLSGKLAGS YIGGAQSKDI VSTLRHFVAN DQEHERMAVD VRITERALRE IYLLPFQIAL
KKSKPGVIIA SCNKVNGLHV SESPALLKDV LRREWGFKGM IMSDWHGTYS TVEAMNAGLD
LEMPGPPRLR GKLAELAVSS RKVSHATLDA RARNVLNLVK SCEKVEGVSS VKSNLYVPAD
GSTNRQLATE SIVLLKNDSG ILPLAYDEVD EIALIGPNLK NGAYCGGSAQ FGSSYVVTNF
EGIVHRLTHN GRYNWRQLED VQINYDIGVH TWGFLPLLGS KITSPDALVK GLRMFFFSEP
PSTPKRKIVD IMDITDSTWD LTKYSHAKLG PEFWVDVEGT FCADETGDYE WGIACCGTAS
LFIDGAMIID NTTTQQPGNS FFGRGSTEKK AVMHIEEGQN YKIKVEFGSL PTSKIHKEGV
VAYGGAGAGR IGAWPVSDSD RTIPRAAALA ARCKYTIVCV GLDEEFESEG YDRPTMDLPE
STDRLITAVL DANPDAIIVT QSGAPINMQP WVSRAKAMVH MWYGGSDMGT GLADVLFGVA
NPSGRLPVTF PKAIEDTPAF LNCESERGRT VYGEGVYVGY RYYEKLKTSV AFPFGHGLSY
TTFALSELSI SPREVTLSVH NTGMFKGATV VQLYISPSPT NTVSRPMKEL KGFTKIFLDS
CQCEEVVMRL DRLSTSFWDE TLGCWLSEKG TYGIHVGRSS ADIVLTGTLE VKETTTWTGL
DF
//
