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Database: UniProt
Entry: A0A875S5I4_EENNA
LinkDB: A0A875S5I4_EENNA
Original site: A0A875S5I4_EENNA 
ID   A0A875S5I4_EENNA        Unreviewed;       840 AA.
AC   A0A875S5I4;
DT   19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2022, sequence version 1.
DT   28-JAN-2026, 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   ORFNames=FOA43_002643 {ECO:0000313|EMBL:QPG75292.1};
OS   Eeniella nana (Yeast) (Brettanomyces nanus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Pichiomycetes;
OC   Pichiales; Pichiaceae; Brettanomyces.
OX   NCBI_TaxID=13502 {ECO:0000313|EMBL:QPG75292.1, ECO:0000313|Proteomes:UP000662931};
RN   [1] {ECO:0000313|EMBL:QPG75292.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CBS 1945 {ECO:0000313|EMBL:QPG75292.1};
RA   Roach M.J.R.;
RL   Submitted (OCT-2020) 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}.
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DR   EMBL; CP064814; QPG75292.1; -; Genomic_DNA.
DR   RefSeq; XP_038778857.1; XM_038922929.1.
DR   AlphaFoldDB; A0A875S5I4; -.
DR   GeneID; 62196044; -.
DR   KEGG; bnn:FOA43_002643; -.
DR   OrthoDB; 47059at2759; -.
DR   UniPathway; UPA00696; -.
DR   Proteomes; UP000662931; Chromosome 3.
DR   GO; GO:0008422; F:beta-glucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-UniPathway.
DR   FunFam; 3.20.20.300:FF:000006; Beta-glucosidase H; 1.
DR   FunFam; 2.60.40.10:FF:000495; Periplasmic beta-glucosidase; 1.
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; IPR050288; Cellulose_deg_GH3.
DR   InterPro; IPR026891; Fn3-like.
DR   InterPro; IPR017853; GH.
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; IPR013783; Ig-like_fold.
DR   InterPro; IPR037524; PA14/GLEYA.
DR   InterPro; IPR011658; PA14_dom.
DR   PANTHER; PTHR42715; BETA-GLUCOSIDASE; 1.
DR   PANTHER; PTHR42715:SF27; 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:UP000662931}.
FT   DOMAIN          403..563
FT                   /note="PA14"
FT                   /evidence="ECO:0000259|PROSITE:PS51820"
SQ   SEQUENCE   840 AA;  92913 MW;  AEF21622C2A11421 CRC64;
     MTFDVDNLLE QLTTEEKVSL ISAVDFWHTA KIERLGIPSI RVSDGPNGIR GTKFFDGVPS
     ACFPNGTCLA STFDAELLEK AGELMAREAD HKGAQVILGP TTNIQRGPLG GRGFESFSED
     PYLSGISTAS IVGGIQKTGK VAATVKHFVC NDLEHERFSS NSVVSERALR EIYLEPFRLA
     IKLADPKCIM TSYNKVNGVH CSENYKLTQK ILRGEWKWNG MIMSDWYGTY SSVEAIQHGI
     DIEFPGPTRF RKWDVIKHLL QSKENDLREG DIDDRCRHVL DLVKYVVDSR GEGPYSTLED
     TKNNTPKTSA TLRKIAADGI VLLKNDKNVL PLSKGKSTVV IGPNAVALNT YSGGGSASLN
     PYYVVTPLEG IKNKVDNVDF TIGCHSHKAL GGLFESMTND LDKSKKGVRA RFYTKPIDER
     SSAEKPIDEL VVRNSYVTLF DYSNAAVDTK TKLFYTDFEG VFTPTETADY EFGCQVFGTA
     LIYLNDKLLI DNKTHQTKGT FCFSSGTVEE TAVAHLKAGE NYKIRVEFGS GITSKLASDF
     GAGGLQVGVT KVIDAEKEIQ HAVSLAKSHD NVILCIGLNS EWESEGYDRD DMTLPRKTND
     LVSAVLKANP NTVVVNQSGT PVEMPWLKDC QTLVQAWYGG NELGNAIADV LFGDVVPSGK
     LSLSWPFKNQ DNPAYLNFHT EKGRVLYGED VFVGYRYYEK LQSQVAFPFG YGLSYTTFKY
     DDLKVTVNDT TVTASFTVAN SGDKYTGKEA VQLYVASLNP SVIRPVKELK AFAKTELKPG
     ESQTIKLSLN LKEACSYFDE YENKWCLEAG KYQIQVGSSS DDIHLIGDFE VQKTVYFLEL
//
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