ID A0A2X0L545_9BASI Unreviewed; 632 AA.
AC A0A2X0L545;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=glucan 1,3-beta-glucosidase {ECO:0000256|ARBA:ARBA00038929};
DE EC=3.2.1.58 {ECO:0000256|ARBA:ARBA00038929};
GN ORFNames=BZ3500_MVSOF-1268-A1-R1_CHR8-2G10094
GN {ECO:0000313|EMBL:SCZ96287.1};
OS Microbotryum saponariae.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Microbotryales; Microbotryaceae; Microbotryum.
OX NCBI_TaxID=289078 {ECO:0000313|EMBL:SCZ96287.1, ECO:0000313|Proteomes:UP000249723};
RN [1] {ECO:0000313|Proteomes:UP000249723}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Jeantristanb JTB J.-T., Ricardo R.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Successive hydrolysis of beta-D-glucose units from the non-
CC reducing ends of (1->3)-beta-D-glucans, releasing alpha-glucose.;
CC EC=3.2.1.58; Evidence={ECO:0000256|ARBA:ARBA00036824};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC {ECO:0000256|ARBA:ARBA00005641, ECO:0000256|RuleBase:RU361153}.
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DR EMBL; FMWP01000088; SCZ96287.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2X0L545; -.
DR STRING; 289078.A0A2X0L545; -.
DR Proteomes; UP000249723; Unassembled WGS sequence.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0071704; P:organic substance metabolic process; IEA:InterPro.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR001547; Glyco_hydro_5.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR31297:SF1; GLUCAN 1,3-BETA-GLUCOSIDASE I_II-RELATED; 1.
DR PANTHER; PTHR31297; GLUCAN ENDO-1,6-BETA-GLUCOSIDASE B; 1.
DR Pfam; PF00150; Cellulase; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361153};
KW Hydrolase {ECO:0000256|RuleBase:RU361153};
KW Reference proteome {ECO:0000313|Proteomes:UP000249723};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..632
FT /note="glucan 1,3-beta-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5030060152"
FT DOMAIN 191..436
FT /note="Glycoside hydrolase family 5"
FT /evidence="ECO:0000259|Pfam:PF00150"
FT REGION 33..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 81..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..121
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 632 AA; 70785 MW; 57FC05F894749001 CRC64;
MLGSNNIAAA ALCVVAGLCI VPTTDAALRL ERDPAARRSA SPSEALGSSS ASPYQRQLGL
DRSELVKAGY VEDAASAYTS LHRRKRSGRR AAVRSARGPA RSDALKGSLS RRKRVASRAT
PTESDAEETS PTLLRPFDYA NDKIRGVSLG GWLVTEPFIK ASLYLEPNRA DWRIQDEWTF
CQYQDREVAA TALRDHWDSW MTELDIEEIA EAGLNHIRVP VGYWAVDIDT AAGEPYIPGS
LYYLDAAIKW AKKAGLRVLI DLYVSSVGRR GSIEWNKNAT NLVRTRNVLK VLADEFSKPE
YHNVVTAIQP INEPWGHEPG VLAAAEDYYY DGFQLAKLDG TDPSRSLLYV IHDAFRGVSH
WKADVIPPHR QDFMRNSTYE GKVMIDTHIY SIFDEQEIRF SEAQRIEHYC EYGQYLSQIT
AGGLRPVVGE WSTAPTDCNQ AFPGANYSRP EQQIGWPSRY DGSWPGTRAM GRCRDISGNG
EKFAMDYREQ LGRLWEVQVS TYEQGSGWIM WTWKTETTAD FSYQAGLDHG WIPKDVTQRT
WQDLCKVSPP QRLQLGTIED SGEADELPTD FLAVGEKVPS SIELKEDDTT DEPVAVYIAN
THGRFDALYD TASTVLLLFA DAIDVLFLYI GF
//
