ID A0A1B7NT05_9EURO Unreviewed; 837 AA.
AC A0A1B7NT05;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=beta-glucosidase {ECO:0000256|RuleBase:RU361161};
DE EC=3.2.1.21 {ECO:0000256|RuleBase:RU361161};
GN ORFNames=ACJ72_05751 {ECO:0000313|EMBL:OAX79924.1};
OS Emergomyces africanus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Emergomyces.
OX NCBI_TaxID=1955775 {ECO:0000313|EMBL:OAX79924.1, ECO:0000313|Proteomes:UP000091918};
RN [1] {ECO:0000313|EMBL:OAX79924.1, ECO:0000313|Proteomes:UP000091918}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 136260 {ECO:0000313|EMBL:OAX79924.1,
RC ECO:0000313|Proteomes:UP000091918};
RA Cuomo C.A., Schwartz I.S., Kenyon C., de Hoog G.S., Govender N.P.,
RA Botha A., Moreno L., de Vries M., Munoz J.F., Stielow J.B.;
RT "Emmonsia species relationships and genome sequence.";
RL Submitted (JUL-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:OAX79924.1}.
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DR EMBL; LGUA01000849; OAX79924.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1B7NT05; -.
DR STRING; 1658172.A0A1B7NT05; -.
DR OrthoDB; 5486783at2759; -.
DR UniPathway; UPA00696; -.
DR Proteomes; UP000091918; 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:SF28; 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 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 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:UP000091918}.
FT DOMAIN 395..555
FT /note="PA14"
FT /evidence="ECO:0000259|PROSITE:PS51820"
SQ SEQUENCE 837 AA; 91221 MW; F55DA8FD23D8DB9E CRC64;
MATLDVEKVI SELTTDEKVA LTAGVDFWHT AAVHRLGIPS LRFSDGPNGV RGTQFFNSVP
SACFPCATAL GATWDTELLH QVGKLLGEEC KAKGAHVLLG PTINIQRSPL GGRGFESYSE
DGVLSGTLAG HYCAGVIEEN VIPTPKHFVC NDQEHERMGV DSIVTQRALR EIYLKPFQIA
LKMAQPGAIM TAYNKINGIH VSEDKRIIDD ILRKEWKWNG LIMSDWFGVY STSESINAGL
DLEMPGPTRW RGSILKHAAE CHKVAPHVLD ERVRNLLKLA NLASKSGIPE NAEEKELNRS
QDQALLRHAA AQSIVLMKNE NNVLPFDKNK SVAVIGPNSK ITTYCGGGSA TVRPYYLVSP
FQGVSAKCTS EVAFAQGVYG HKVIPDLGPL LKTTDGNPGY RFRAYNDPPG VEGREIADEL
RLVNSSALLA DYRSPQIKSS TFYVDMEGTF TPNESGMYDF SVTVIGSGKL FIDGELVVDN
SKNQKLGTAF FGMATIEVFG SKELNGGQTY EVLFQFGSAP TSDIASGTPE LFGPGAFRFG
GCKRLDREAS IASAVDLASK HDQVVIFAGL NNDWESEGHD RESMDLPPGS DELITRILAA
NPKTVVVIQS GTPVTMPWAD NAQALLQAWY GGNETGNGIA DVLFGDVNPS GKLPLSFPIR
LQDNPSYLNF RSERGRVLYG EDVYVGYRYY DKTQTPVLFP FGHGLSYTTF KRSGLQIASE
GDTLTVSLTV TNSGDRAGAE VVQLYVNPSP TNSINRPPRE LKGFKKIHLE AGKSADVKIE
VSKREVTSFW DEIRNAWISE KGVYGVSIEG TSNGGNDEEA ALKGNFEVTE TLYWTGL
//
