GenomeNet

Database: UniProt
Entry: A0A1E3Q6U6_LIPST
LinkDB: A0A1E3Q6U6_LIPST
Original site: A0A1E3Q6U6_LIPST 
ID   A0A1E3Q6U6_LIPST        Unreviewed;       824 AA.
AC   A0A1E3Q6U6;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
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=LIPSTDRAFT_3714 {ECO:0000313|EMBL:ODQ73391.1};
OS   Lipomyces starkeyi NRRL Y-11557.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Lipomycetaceae; Lipomyces.
OX   NCBI_TaxID=675824 {ECO:0000313|EMBL:ODQ73391.1, ECO:0000313|Proteomes:UP000094385};
RN   [1] {ECO:0000313|EMBL:ODQ73391.1, ECO:0000313|Proteomes:UP000094385}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL Y-11557 {ECO:0000313|EMBL:ODQ73391.1,
RC   ECO:0000313|Proteomes:UP000094385};
RX   PubMed=27535936; DOI=10.1073/pnas.1603941113;
RA   Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goeker M.,
RA   Salamov A.A., Wisecaver J.H., Long T.M., Calvey C.H., Aerts A.L.,
RA   Barry K.W., Choi C., Clum A., Coughlan A.Y., Deshpande S., Douglass A.P.,
RA   Hanson S.J., Klenk H.-P., LaButti K.M., Lapidus A., Lindquist E.A.,
RA   Lipzen A.M., Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J.L.,
RA   Peng Y., Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C.,
RA   Stielow J.B., Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V.,
RA   Jeffries T.W.;
RT   "Comparative genomics of biotechnologically important yeasts.";
RL   Proc. Natl. Acad. Sci. U.S.A. 113:9882-9887(2016).
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; KV454294; ODQ73391.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1E3Q6U6; -.
DR   STRING; 675824.A0A1E3Q6U6; -.
DR   OrthoDB; 5486783at2759; -.
DR   UniPathway; UPA00696; -.
DR   Proteomes; UP000094385; 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|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:UP000094385}.
FT   DOMAIN          393..552
FT                   /note="PA14"
FT                   /evidence="ECO:0000259|PROSITE:PS51820"
SQ   SEQUENCE   824 AA;  90681 MW;  7F4973F70437BC01 CRC64;
     MDVERIIRDA NLREKVSLLA GLDFWHTTPL DRFDVPSIRC SDGPNGVRGT KFFNNVPAIC
     IPCGTGLGAT WNKELIFHAG ILLSSECMAK GAHAWLGPTI NMLRSPLNGR GFESFSEDPF
     LSGILAASII NGVQSNGTLA VLKHFVANDQ ETEKISVDVL VSDRALREIY LKPFQLALRH
     SSPASVMASY SKVQGVHCSE SKQLLTNILR DEWGFHGLIM SDWFGTYSLE AALEAGLDLE
     MPGPARFRTP LTLSAVTSGK LKEDAINTSC RNLLNFVNKA SQNVSKHEEE KDTPEDRLLN
     YRLACESIVL LKNDNNILPI PADCGELAII GPNAKLGAAC GGGSASLRPY YTSSILEGIE
     RQVAPGTQIH YEVGTYGHIL QPLLDKSAVC NMDGRPGVTI EFFNEPSRIA GRKAFDRIEV
     PDAAYQLMDY THPDAKEVFY ISMSMYFTPQ KSGRYEFGLA VYGTANLYIN DQLIIENTTS
     QRPGGLFFGR GSAEEKATWE MEAQVCYLLR VECGSAATST LAGQFPVTLP GGACRLGGCL
     QIDPEESVQQ AVDLARKCKY TIVVVGLNSD YEKEGTDRQN MDLPAGVEEL VKAVLSVQRD
     AVIVTQSGTP VSMSFSRQAS TMIHSWYGGN EGGNAVGAVL FGKFNPCGKL PMTFPKRLED
     NPSFLSFGTD NGKLHYSEDV FVGYRWYDAR KIEPEFRFGH GLSYTTFLIS DITFGNDGVD
     VVVENSGRRE GAEVLQLYVS RLAGSTSAFK HPLKELKGFE KIHLQPQERK TVKFVLDRES
     TSCWDEKRNA WCCEKGTYEV AIMATGQTLK GSFEVAETVW WNGL
//
DBGET integrated database retrieval system