ID T0KGU9_COLGC Unreviewed; 841 AA.
AC T0KGU9;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=beta-glucosidase {ECO:0000256|RuleBase:RU361161};
DE EC=3.2.1.21 {ECO:0000256|RuleBase:RU361161};
GN ORFNames=CGLO_05477 {ECO:0000313|EMBL:EQB54657.1};
OS Colletotrichum gloeosporioides (strain Cg-14) (Anthracnose fungus)
OS (Glomerella cingulata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum gloeosporioides species complex.
OX NCBI_TaxID=1237896 {ECO:0000313|EMBL:EQB54657.1, ECO:0000313|Proteomes:UP000015530};
RN [1] {ECO:0000313|EMBL:EQB54657.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Cg-14 {ECO:0000313|EMBL:EQB54657.1};
RA Alkan N., Thon M., Prusky D.;
RT "Global analysis of the Colletotrichum gloeosporioides genome and
RT transcriptome reveals a conserved role for pacC pH regulation in fungi.";
RL Submitted (OCT-2012) 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:EQB54657.1}.
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DR EMBL; AMYD01001081; EQB54657.1; -; Genomic_DNA.
DR AlphaFoldDB; T0KGU9; -.
DR STRING; 1237896.T0KGU9; -.
DR eggNOG; ENOG502SH7D; Eukaryota.
DR HOGENOM; CLU_004542_4_0_1; -.
DR OMA; EVEPYYG; -.
DR OrthoDB; 5486783at2759; -.
DR UniPathway; UPA00696; -.
DR Proteomes; UP000015530; 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 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|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:UP000015530}.
FT DOMAIN 400..553
FT /note="PA14"
FT /evidence="ECO:0000259|PROSITE:PS51820"
SQ SEQUENCE 841 AA; 92705 MW; E15BD463B9358E5E CRC64;
MATDNIPLDV EGLISQLTLE EKIDLLAGQG SFRTTGLPHR GIPALITSDG PHGIRGRRAF
HRNPSPMLPS ATGMGATFNK ELLHKVGNLL GEEARARGVH VLLAPTICLQ RSPLFGRGFE
AFAEDPYLSG ILGAAYINGV QERGVATSVK HYAAHDQSDN SIEDNVCMTQ RTLREVHMMP
FQLVMRDSDP WTFMTSYNKI NGIHVSEDPL LMKQILRDEW GFKGLVMSDW FGTYSTSEAI
NAGLDLEMPG PTQWRGKCLS LAVNSRKVMR TTVDECVRNV LNLTIKVMDT KPEGYFSASN
TPEQQALIRK LVSESIVLLK NDRGVLPIKA SEKKRIALIG DHVKNPALSG GGSAEVEPYY
SVTPYNAIIE EVGKENVAYA LGCHSFRFSP LLKNLKPLNA EGFGWSVEVF GENPDENPNA
EVLLSATAEK ELIDVPESFH ATLPKKFYAR ARAVYTPEIT GPFRLGFSTS GKGKVRLNGK
EVIDLWTEQP PKTGPTPCFN RLSMEKFCDT TLTEGKAINI EVVQVNEDLA GGVGTALTLA
GRVGGFEIID EDLAIKEAAV LAKSVDVPIV VTGLSSDFEY EGADRKHLRL PGRVDDLIQA
VLAANPNAII VTQSGCPIEM PWESQAATLV HAWFGGQETG HGLADVLFGK ANPSGRLSQT
FPESVKHTPA YLNFSKTDYD IVYGEGVFIG HRYYEVVDRD PLFYFGHGLS YSTFEYSKLQ
VPSTFEASEG HKMKISVDVT NKGPYGGDEV VQIYIHDPES TLQRPVRELK AFTKVYLATD
ETKTVELVLD KYSLSYWSQE RSKWLAEAGE YVVIVASSSN PKDEIQRASF HLPETFFWEG
V
//
