ID A0A1G4BP95_9PEZI Unreviewed; 956 AA.
AC A0A1G4BP95;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=beta-glucosidase {ECO:0000256|RuleBase:RU361161};
DE EC=3.2.1.21 {ECO:0000256|RuleBase:RU361161};
GN ORFNames=CORC01_01335 {ECO:0000313|EMBL:OHF03282.1};
OS Colletotrichum orchidophilum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum.
OX NCBI_TaxID=1209926 {ECO:0000313|EMBL:OHF03282.1, ECO:0000313|Proteomes:UP000176998};
RN [1] {ECO:0000313|EMBL:OHF03282.1, ECO:0000313|Proteomes:UP000176998}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMI 309357 {ECO:0000313|EMBL:OHF03282.1,
RC ECO:0000313|Proteomes:UP000176998};
RA Capua I., De Benedictis P., Joannis T., Lombin L.H., Cattoli G.;
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Beta-glucosidases are one of a number of cellulolytic enzymes
CC involved in the degradation of cellulosic biomass. Catalyzes the last
CC step releasing glucose from the inhibitory cellobiose.
CC {ECO:0000256|ARBA:ARBA00024983}.
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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004401};
CC Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004401}.
CC Membrane {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane
CC protein {ECO:0000256|ARBA:ARBA00004606}.
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:OHF03282.1}.
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DR EMBL; MJBS01000007; OHF03282.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G4BP95; -.
DR STRING; 1209926.A0A1G4BP95; -.
DR OrthoDB; 5486783at2759; -.
DR UniPathway; UPA00696; -.
DR Proteomes; UP000176998; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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:SF20; BETA-GLUCOSIDASE E-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 Cell membrane {ECO:0000256|ARBA:ARBA00022475};
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 Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326,
KW ECO:0000256|RuleBase:RU361161};
KW Reference proteome {ECO:0000313|Proteomes:UP000176998};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 71..94
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 874..947
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 773..792
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 956 AA; 104635 MW; ACF146BF2E5DB4AC CRC64;
MDPSKEGLLG DKSRRSYDGE SDDGSDMDAT EYLERNERKQ ESRLRKPAFL SVKPRGCIAA
FRRLFQGRSK LCLLITAVVF IMWVLISAGG AVMYKKFKGA PPVGLSPPWY PTPKGGISKN
WAESYKKASE MVAKMTLPEK VNITTGTGWM MGLAVGTTGP AVHVGFPQLQ LQDGPLGIRF
ADNATAFPAG VTVGATWNKE LMYQRGKAHG QEARGKGINV LLGPCVGPLG RLPAGGRNWE
GFGADPYLSG IAAAETIKGI QEEGVMATIK HFVANEQEHF RQSWEWGLPN AISSNIDDRA
MHELYAWPFL DAVKAGVASV MCSYNQVNNS YACDNSKLLN GILKDEMGFQ GFVMSDWLAQ
RSGVGSALAG LDMTMPGDGL FWQNGKSLWG PELTRAVLNG SVPVERLDDM AVRIVASWYK
LGQDDKKLYP DELPNFSSWT NDKMGKLAPG SKTPQPELEV NKYVNVQGNH SDIARRVAAE
GTVLLKNKDV LPISRDGFID AKRKRHEGKL KIGIFGEDAG PGNGPNYCAD RGCNQGTLGS
GWGSGAVEFP YLVTPVEALK KGFKSEKVEL SEYLTNSPPF QKDPSILHNQ DVCIVFANAD
SGEGFLAWGG IGGDRNDLKL QNGGDDLILL VADNCGKGEG NLAGGDTIVV IHSVGPVEME
RWIEHPGVKV VLYANLPGEE SGNALADVIF GDVNPSGKLP YTIPKSLKDF GPAGQILYLP
NGVVPQQDFS EGLYIDYRHF DKNNIEPRFE FGFGLSYTSF EFSNVVVEGL KEKTALPPPR
PSPGAEPPKF SEKIPDKKVA LFPEGFRKLE KYVYPYLDTV DDISSDPYPY PDGYEVKQPL
SQAGGEEGGN PDLWETYVTV KADVTNTGAV SGKVVPQLYM SYPKNVHGVD FPVKVLRGFD
KFNLDKGEKK TVTFNLTRRD LSYWDVRQQN WAMITFGEYS FLVGESSRQL TQVGSW
//
