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Database: UniProt
Entry: A0A1E3QCU7_LIPST
LinkDB: A0A1E3QCU7_LIPST
Original site: A0A1E3QCU7_LIPST 
ID   A0A1E3QCU7_LIPST        Unreviewed;       833 AA.
AC   A0A1E3QCU7;
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_69491 {ECO:0000313|EMBL:ODQ75284.1};
OS   Lipomyces starkeyi NRRL Y-11557.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Lipomycetaceae; Lipomyces.
OX   NCBI_TaxID=675824 {ECO:0000313|EMBL:ODQ75284.1, ECO:0000313|Proteomes:UP000094385};
RN   [1] {ECO:0000313|EMBL:ODQ75284.1, ECO:0000313|Proteomes:UP000094385}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL Y-11557 {ECO:0000313|EMBL:ODQ75284.1,
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}.
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DR   EMBL; KV454291; ODQ75284.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1E3QCU7; -.
DR   STRING; 675824.A0A1E3QCU7; -.
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: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:UP000094385}.
FT   DOMAIN          401..559
FT                   /note="PA14"
FT                   /evidence="ECO:0000259|PROSITE:PS51820"
SQ   SEQUENCE   833 AA;  90906 MW;  4FB55A680D15744B CRC64;
     MAPHEQLDIE ATLAELTARE KISLLAGTDF WHTQGIPRLS IPALRMSDGP NGIRGIRFFS
     GVPAACFPCG TALGATWDRP LLEKAGKVMG DEAIAKGAVI ILGPTVNIQR SPLGGRGFES
     FSEDPYLSGS LAAAEIRGIQ NGTGVAATIK HFVANDQEHE RSAVNSIVSD RAMREIYLLP
     FQLAVRDAKP AAIMTAYNKL NGTHCSEHQG LLKGILRGEW GWKGLVMSDW FGTYSTSASI
     NAGVDLEMPG PTRFRGTNLG HAMFSKKVNS YVLDERVKNV LELVNRVAPL GMPENAKEET
     RNTPKTAALL RKIAADSIVL LKNENNVLPF DKNKKIAIVG PNAKVATYCG GGSASLAPYY
     AITPFEGISA KYSNPASISY SVGAYSHELL PLLDGQLKTE DGSIGWMFRV FPSQDAASTG
     SADPIDEVFL RSTNTFLGDY KHPQGAGTFY ATFEGYFTPQ VDGIYDFGIA TAGTAYLYVD
     NKVLVDNATN QRKGEYFFGH GTVEVSNSIK LKAGTTYHLK VLWGTMSTSK IYDGSSENGA
     LRLGGALRID EDYEIERAKE IAKTVDQVVL CVGLNHDWES EGYDRQFMDL PGRQDELITA
     VAEVNPNIVV VNQSGTPVTM PWLSKVGGLL QAWYGGNETG NAIADVLFGD VVPSGKLPLS
     FPVLNEDNPA FLNYRSERGR VLYGEDVYVG YRFYDKTKKK VNFPFGYGLS YTTFELSDII
     ADIAGDTLTV RVTVSNVGKV NGSEVVQIYI SQHAPSINRP PKELKGYKKI AVPSGDSELV
     EIAIPVKYAF SFWDEERDAW ICEKDNYTIT ASNGTMTLKT DVNVEETMWW NGI
//
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