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Database: UniProt
Entry: A0A175WBX1_9PEZI
LinkDB: A0A175WBX1_9PEZI
Original site: A0A175WBX1_9PEZI 
ID   A0A175WBX1_9PEZI        Unreviewed;       854 AA.
AC   A0A175WBX1;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   24-JAN-2024, entry version 22.
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=MMYC01_203815 {ECO:0000313|EMBL:KXX80730.1};
OS   Madurella mycetomatis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariales incertae sedis; Madurella.
OX   NCBI_TaxID=100816 {ECO:0000313|EMBL:KXX80730.1, ECO:0000313|Proteomes:UP000078237};
RN   [1] {ECO:0000313|Proteomes:UP000078237}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=mm55 {ECO:0000313|Proteomes:UP000078237};
RA   van de Sande W.W.J.;
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KXX80730.1, ECO:0000313|Proteomes:UP000078237}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=mm55 {ECO:0000313|Proteomes:UP000078237};
RA   Van De Sande W.;
RT   "Madurella mycetomatis genome sequencing.";
RL   Submitted (JAN-2016) 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|ARBA:ARBA00004987, 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:KXX80730.1}.
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DR   EMBL; LCTW02000052; KXX80730.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A175WBX1; -.
DR   STRING; 100816.A0A175WBX1; -.
DR   VEuPathDB; FungiDB:MMYC01_203815; -.
DR   OrthoDB; 5486783at2759; -.
DR   UniPathway; UPA00696; -.
DR   Proteomes; UP000078237; 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; 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   PANTHER; PTHR42715; BETA-GLUCOSIDASE; 1.
DR   PANTHER; PTHR42715:SF12; BETA-GLUCOSIDASE A-RELATED; 1.
DR   Pfam; PF14310; Fn3-like; 1.
DR   Pfam; PF00933; Glyco_hydro_3; 1.
DR   Pfam; PF01915; Glyco_hydro_3_C; 1.
DR   PRINTS; PR00133; GLHYDRLASE3.
DR   SMART; SM01217; Fn3_like; 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.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW   ECO:0000256|RuleBase:RU361161};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
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|ARBA:ARBA00023326,
KW   ECO:0000256|RuleBase:RU361161};
KW   Reference proteome {ECO:0000313|Proteomes:UP000078237};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..854
FT                   /note="beta-glucosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5008043879"
FT   DOMAIN          766..834
FT                   /note="Fibronectin type III-like"
FT                   /evidence="ECO:0000259|SMART:SM01217"
SQ   SEQUENCE   854 AA;  91868 MW;  E69EF7372D2681E0 CRC64;
     MANLVLALLL FLSALTSAAT DTPFLGYPSP WATNITDPTW AAAYAQAIAF VANLTLTEKV
     NLTTGTGWEA DRCIGATGGI PRLGFRPFCL MDGPLGVRYT DHNSAFPAGV NTAATFSRRL
     MRLRGEAMGA EFRGKGIDVM LGPVAGALGR VPQGGRNWEG FSPDPYLTGV AMAETIQGIQ
     SRGVVACAKH YILNEQEHFR GSIDVRIDDR TMHELYLWPF ADAVRAGVGS VMCSYNKING
     TYACENEWTT NYLLKNELGF QGFVLSDWGA QHNTLGSALG GLDMAMPGDG GPPPYRAWWG
     GALTEAVLRG DVPQWRLDDM AVRIMAAYFR VHTGNYTSRP DINFSAWTNS TVGPLYPAAN
     QSYTVVNEFV DVQSDHASLI REIGAKSVVL LKNAYDLLPL RQPGPPIIAV IGDDAQDHPL
     GPNACPERGC LNGTLAMGYG SGTANFPYLV SPLTALTEQA RADNTTLLYA PSNWDLDAAI
     TTARNASIAI VFAAATSGEN FITVDGNAGD RNNLTLWANG DALIKAVASI NPNTIVVLHT
     PGPVILDYAE EHPNISAILW AGLPGQESGN ALVDVLYGKV NPQGRSPFTW GDSVEEYGAQ
     LMFEAENPRA PVQSFDEGVF IDYRKFSTFG GKLTYPFGFG LSYTKFRYSG LSVVRKEEVE
     GRFEPAEGLT GPAPTFGVVE AELGVHTAPE GFTRISPYVY PWLNNSESLV TGNSTGASEF
     PAAARNGSAQ PVLPASGAPG GNPGLYEVLY TITASIENVG EVAGTEIPQL YVQLGGEENP
     FGVLRGFDEV ELEPGETKNV TFELTRRDVS NWNTSTQNWE ITDREKVVFV GSSVRDIRLN
     ASLPAPVGMA WRHG
//
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