ID A0A100INA6_ASPNG Unreviewed; 416 AA.
AC A0A100INA6;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=glucan 1,3-beta-glucosidase {ECO:0000256|ARBA:ARBA00038929};
DE EC=3.2.1.58 {ECO:0000256|ARBA:ARBA00038929};
DE AltName: Full=Exo-1,3-beta-glucanase 1 {ECO:0000256|ARBA:ARBA00041265};
DE AltName: Full=Exo-1,3-beta-glucanase A {ECO:0000256|ARBA:ARBA00041261};
GN ORFNames=ABL_07001 {ECO:0000313|EMBL:GAQ44340.1};
OS Aspergillus niger.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=5061 {ECO:0000313|EMBL:GAQ44340.1, ECO:0000313|Proteomes:UP000068243};
RN [1] {ECO:0000313|Proteomes:UP000068243}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=An76 {ECO:0000313|Proteomes:UP000068243};
RX PubMed=26893421; DOI=10.1128/genomeA.01700-15;
RA Gong W., Cheng Z., Zhang H., Liu L., Gao P., Wang L.;
RT "Draft genome sequence of Aspergillus niger strain An76.";
RL Genome Announc. 4:E0170015-E0170015(2016).
CC -!- FUNCTION: Beta-glucanases participate in the metabolism of beta-glucan,
CC the main structural component of the cell wall. It could also function
CC biosynthetically as a transglycosylase.
CC {ECO:0000256|ARBA:ARBA00037254}.
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 -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC {ECO:0000256|ARBA:ARBA00005641, ECO:0000256|RuleBase:RU361153}.
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:GAQ44340.1}.
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DR EMBL; BCMY01000012; GAQ44340.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A100INA6; -.
DR PaxDb; 5061-CADANGAP00013786; -.
DR VEuPathDB; FungiDB:An18g04100; -.
DR VEuPathDB; FungiDB:ASPNIDRAFT2_1179270; -.
DR VEuPathDB; FungiDB:ATCC64974_108530; -.
DR VEuPathDB; FungiDB:M747DRAFT_89902; -.
DR OMA; GWDMQDL; -.
DR Proteomes; UP000068243; Unassembled WGS sequence.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProt.
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 Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361153};
KW Hydrolase {ECO:0000256|RuleBase:RU361153};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..416
FT /note="glucan 1,3-beta-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007087594"
FT DOMAIN 86..315
FT /note="Glycoside hydrolase family 5"
FT /evidence="ECO:0000259|Pfam:PF00150"
SQ SEQUENCE 416 AA; 45472 MW; 1D9BCE7EBC64D439 CRC64;
MFVEGVKKAL LALSLLAASA QAVPRVRRQS NASSFDYKSQ IVRGVNLGGW LVTEPWITPS
LYDSTGGGAV DEWTLCQTLG QDEAKAKLSS HWSSFVTQSD FDRMAQAGLN HVRIPIGYWA
VAPIDGEPYV SGQIDYLDQA VTWARAAGLK VLVDLHGAPG SQNGFDNSGH RGPIQWQQGN
TVNQTMTAFD ALARRYAQSD TVTAIEAINE PNIPGGVNEG GLKNYYYGAL ADVQRLNPST
TLFMSDGFQP VESWNGFMQG SNVVMDTHHY QVFDTGLLSM SIDDHVKTAC SLATQHTMQS
DKPVVVGEWT GALTDCAKYL NGVGNAARYD GTYMSTTKYG DCTGKSTGSV ADLSAEEKAN
TRRYIEAQLE AYEMKSGWLF WTWKTEGAPG WDLQDLLANQ LFPTSPTDRQ YPHQCS
//
