ID A0A367XN59_9ASCO Unreviewed; 835 AA.
AC A0A367XN59;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 13.
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 Name=bglI_1 {ECO:0000313|EMBL:RCK54988.1};
GN ORFNames=Cantr_04668 {ECO:0000313|EMBL:RCK54988.1};
OS Candida viswanathii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=5486 {ECO:0000313|EMBL:RCK54988.1, ECO:0000313|Proteomes:UP000253472};
RN [1] {ECO:0000313|EMBL:RCK54988.1, ECO:0000313|Proteomes:UP000253472}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 20962 {ECO:0000313|EMBL:RCK54988.1,
RC ECO:0000313|Proteomes:UP000253472};
RA Ahn J.;
RT "Whole genome sequencing of Candida tropicalis (genome annotated by CSBL at
RT Korea University).";
RL Submitted (JUN-2018) 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|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:RCK54988.1}.
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DR EMBL; QLNQ01000030; RCK54988.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A367XN59; -.
DR STRING; 5486.A0A367XN59; -.
DR UniPathway; UPA00696; -.
DR Proteomes; UP000253472; 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|RuleBase:RU361161};
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|RuleBase:RU361161};
KW Reference proteome {ECO:0000313|Proteomes:UP000253472}.
FT DOMAIN 400..559
FT /note="PA14"
FT /evidence="ECO:0000259|PROSITE:PS51820"
SQ SEQUENCE 835 AA; 91639 MW; 6A4A7D5F5B1ABBF9 CRC64;
MATTFDVDKV LSELSLEDKI ALTAGKDFWH TNAVPSQSIP SLRFSDGPNG IRGTKFFNSV
PLACFPCGTG LAATFDTQLL ESAGELMATE AKHKGAHVIL GPTMNIQRGP LGGRGFESFS
EDPYLTGRAA SHIVQGIEKH GVGATPKHFV CNDLEDQRMS SDSVLTQRAL REIYLEPFRI
LFKDVSPSCL MTAYNKVNGV HASQNKELLD GVVRGEWGWN GLIMSDWFGT FTSKEALVGG
LDLEMPGPAV FRKVEEVGHM IKTKELNIKV LNERVKNVLR LIKRGIEDSG VPENASEDTK
NNTESTRALL RKLAQDSVVL LKNEDGVLPL KKDESVAVIG PNAKSAVYCG GGSASLRAYY
TTTPFDSISQ KLSTAPEYTV GCYAHKFLPG LGNQVKNPRT GDKGYTMKFY LEPKSASNRT
LIDDYDIDLS SFHLVDYYND KVPDGLYYVD FEAEFTPEET AEYAFGVTVV GTAQLFIDGE
LVVDNKTKQT KGESFFNCGT VEERGTRKLT KGKTYKITVE FGSAPTYTLG GRGAEYFGGG
INLGMAKVIN DKDEIAHAVE IAKSVDKVVL CIGLNGEWES ESYDRPHMKL EGLQDELITA
VIAANPNTVI VNQSGTPVEF PELDKYKSLI QCWYGGNEAG NAIADVLFGD VNPSGKLSLT
FPKRGIDNPT YLNFKTERGR VLYGEDIFVG YRFYEKMQRE VAFPFGHGLS YTTFDFKDLK
VSVAGEDVKV SVVVTNTGAV AGAEVVQAYV GKVESDVIRP VKELKGFAKV ELKPKESKTV
EITLPIKYSA AFFDEYADEW SVQSGEYKVL VGNSSDNTPL TGSFVVEKDY FWTGL
//
