ID R9AF64_WALI9 Unreviewed; 842 AA.
AC R9AF64;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
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=J056_004676 {ECO:0000313|EMBL:EOR00864.1};
OS Wallemia ichthyophaga (strain EXF-994 / CBS 113033).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Wallemiomycotina;
OC Wallemiomycetes; Wallemiales; Wallemiaceae; Wallemia.
OX NCBI_TaxID=1299270 {ECO:0000313|EMBL:EOR00864.1, ECO:0000313|Proteomes:UP000014064};
RN [1] {ECO:0000313|Proteomes:UP000014064}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EXF-994 / CBS 113033 {ECO:0000313|Proteomes:UP000014064};
RX PubMed=24034603; DOI=10.1186/1471-2164-14-617;
RA Zajc J., Liu Y., Dai W., Yang Z., Hu J., Gostincar C., Gunde-Cimerman N.;
RT "Genome and transcriptome sequencing of the halophilic fungus Wallemia
RT ichthyophaga: haloadaptations present and absent.";
RL BMC Genomics 14:617-617(2013).
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; KE007232; EOR00864.1; -; Genomic_DNA.
DR RefSeq; XP_009268141.1; XM_009269866.1.
DR AlphaFoldDB; R9AF64; -.
DR STRING; 1299270.R9AF64; -.
DR GeneID; 20377628; -.
DR KEGG; wic:J056_004676; -.
DR eggNOG; ENOG502QR4D; Eukaryota.
DR HOGENOM; CLU_004542_4_0_1; -.
DR OMA; TYYVDME; -.
DR OrthoDB; 5486783at2759; -.
DR UniPathway; UPA00696; -.
DR Proteomes; UP000014064; 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; SSF56988; Anthrax protective antigen; 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:UP000014064}.
FT DOMAIN 403..564
FT /note="PA14"
FT /evidence="ECO:0000259|PROSITE:PS51820"
SQ SEQUENCE 842 AA; 91751 MW; 46BCFE1589D75F4E CRC64;
MTLPELNVEE LLQQLTVKEK IELLAGKDMW HTVNNTRLGI PSIRTSDGPN GVRGINFFEG
TPSSCFPGAT ALGASFDNQL LERVGSALAD ECIAKGVHVL LAPTINIQRS PLGGRGFESY
SEDPELSGTL AKYFVKGLQD KGVAATIKHY VGNDQEFERM SMSSEISERA LREIYLRAFE
IPLRESEHKP WSVMTAYNRV NGLHCSEDPR LLGDILRGEW GWNGMTMSDW FGTYSAGEST
HAGLDLEMPG PSVVRGAALQ RALTAKKVFI EDIDARVKNV LELINKVRKS GIDEATPEKV
HDTPELRQTL REAAANGVVL LKNEENVMPI KKGTTKISVI GPNAESAIIS GGGSAALRAS
YAVSPLDAIR EQAKEIGAEV VYSRGGNAHK LTPLFGPELK TADGRAGVDV KFYGSDPAAG
KAKPLHELYA HSSHLFFNDN LPGPETVPLT CWAEASGIFT PNKTDNYEIG IAGAGQTDLF
VDGERVVDNS TNPQPGTLWF NSGSQERTVV KKLEEGKQYS IMARLYYSSE GAQAAGTLSP
HSRGGIRFGI SPSKSQDEFL QEALDACKGA DLVLCFVGLN NDFESEGFDR PDMKLPDSAN
AFMNAISSAH SNTVAIVQSG TPVELPWVDK VKGVYQAFYG GNEVGNGLAD ILFGRLNPSA
KLPLTMPVEL RDSPSHLNFG GENGRVVYAE GVFVGYRHFA TTGKKPLFPF GKGLSYTSFD
VTNARVDQTS DSHDVLIRMK VTNTGSVAGR EIIQLYVNDV ESRLARPFLE LKAYAKTNLI
LPGESEEVTL MLGKRAFSYF DDFKSRWVIE AGEFKLFVAT SSAVEDIKHT LSYYVDKTSE
FI
//
