ID E3QNX1_COLGM Unreviewed; 955 AA.
AC E3QNX1;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=beta-glucosidase {ECO:0000256|RuleBase:RU361161};
DE EC=3.2.1.21 {ECO:0000256|RuleBase:RU361161};
GN ORFNames=GLRG_07573 {ECO:0000313|EMBL:EFQ32559.1};
OS Colletotrichum graminicola (strain M1.001 / M2 / FGSC 10212) (Maize
OS anthracnose fungus) (Glomerella graminicola).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum graminicola species complex.
OX NCBI_TaxID=645133 {ECO:0000313|Proteomes:UP000008782};
RN [1] {ECO:0000313|Proteomes:UP000008782}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M1.001 / M2 / FGSC 10212 {ECO:0000313|Proteomes:UP000008782};
RX PubMed=22885923; DOI=10.1038/ng.2372;
RA O'Connell R.J., Thon M.R., Hacquard S., Amyotte S.G., Kleemann J.,
RA Torres M.F., Damm U., Buiate E.A., Epstein L., Alkan N., Altmueller J.,
RA Alvarado-Balderrama L., Bauser C.A., Becker C., Birren B.W., Chen Z.,
RA Choi J., Crouch J.A., Duvick J.P., Farman M.A., Gan P., Heiman D.,
RA Henrissat B., Howard R.J., Kabbage M., Koch C., Kracher B., Kubo Y.,
RA Law A.D., Lebrun M.-H., Lee Y.-H., Miyara I., Moore N., Neumann U.,
RA Nordstroem K., Panaccione D.G., Panstruga R., Place M., Proctor R.H.,
RA Prusky D., Rech G., Reinhardt R., Rollins J.A., Rounsley S., Schardl C.L.,
RA Schwartz D.C., Shenoy N., Shirasu K., Sikhakolli U.R., Stueber K.,
RA Sukno S.A., Sweigard J.A., Takano Y., Takahara H., Trail F.,
RA van der Does H.C., Voll L.M., Will I., Young S., Zeng Q., Zhang J.,
RA Zhou S., Dickman M.B., Schulze-Lefert P., Ver Loren van Themaat E.,
RA Ma L.-J., Vaillancourt L.J.;
RT "Lifestyle transitions in plant pathogenic Colletotrichum fungi deciphered
RT by genome and transcriptome analyses.";
RL Nat. Genet. 44:1060-1065(2012).
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}.
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DR EMBL; GG697363; EFQ32559.1; -; Genomic_DNA.
DR RefSeq; XP_008096579.1; XM_008098388.1.
DR AlphaFoldDB; E3QNX1; -.
DR STRING; 645133.E3QNX1; -.
DR EnsemblFungi; EFQ32559; EFQ32559; GLRG_07573.
DR GeneID; 24412938; -.
DR VEuPathDB; FungiDB:GLRG_07573; -.
DR eggNOG; ENOG502QR4D; Eukaryota.
DR HOGENOM; CLU_004542_2_0_1; -.
DR OrthoDB; 5486783at2759; -.
DR UniPathway; UPA00696; -.
DR Proteomes; UP000008782; 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:UP000008782};
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 70..93
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 873..946
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..41
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 955 AA; 104361 MW; 680A219416D3B4E6 CRC64;
MDPSNQGLLD KSRGSYDRDS EDGSDIDVTD YLPRNDQKEE SSFPKPAFLS NRFPGCLAAL
KRACHGRSRL CLLVTALAVI MWIIISAGGA VMYKKFKSAP PTGQSPPWYP TPKGGISKNW
AESYKIAAEM VSRMTLPEKV NITTGTGWMM GLAVGTTGPA VHVGFPQLQL QDGPLGIRFA
DNATAFPAGV TVGATWNREL MYERGKAHGQ EARGKGINVL LGPCIGPLGR LPAGGRNWEG
FAADPYLQGI AAAETIKGIQ DQGVMATIKH FVANEQEHFR QSWEWGLPNA MSSNVGDRAM
HELYAWPFLN AVKAGVASVM CSYNMVNNSY ACGNSKLLNG ILKDEMGFQG FVMSDWLAQR
SGVDSALAGL DMTMPGDGLF WSDGKSLWGP ELTKAVLNGS VPVDRLNDMV VRIVASWYQL
GQDDKKLFPN ELPNFSSWTD DKMGTLAPGS KTPQVEFEVN KYVNVQSDHS DVARRVAAEG
TVLLKNENVL PISKDGFIDA KRKRHEGKLK IGIYGEDAGP GNGPNYCKDR GCNQGTLGSG
WGSGAVEFPY LVAPVEALKK AFKSEKVELS EFLTNSPPFK KDPSILHDQD VCIVFANADS
GEGFLSWGGI SGDRNDLKLQ KGGDDLILQV ADNCGKGDGN PVGGDTIVVI HSVGPVEMER
WIEHPGVKAV LYANLPGQES GNALADVILG DVNPSGKLPY TIPKSLKDFG PGGQILYLPN
GIVPQQDFSE GLYIDYRHFD KQEIEPRFEF GFGLSYTTFD FSNVVVEGVK PKSPLPAARP
PPAAEPPKFS DKIPEKKEVL FPEGFRKLEK YVYPYLDTVD DISTEPYPYP EGYDVEQPLS
EAGGEEGGNP DLWEIYVTVK ADVTNTGAVA GKVVPQLYLT YPKDVHGVDF PVKVLRGFDK
FNLEKGEKKT VTFNLTRRDL SYWDVHRQNW VMVTSGEYSF LVGESSRQLS RVGSW
//
