ID   EXGB_ASPFN              Reviewed;         392 AA.
AC   B8NBJ4;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-MAY-2023, entry version 67.
DE   RecName: Full=Probable glucan endo-1,6-beta-glucosidase B;
DE            EC=3.2.1.75;
DE   AltName: Full=Beta-1,6-glucanase B;
DE   AltName: Full=Endo-1,6-beta-D-glucanase B;
DE   AltName: Full=Endo-1,6-beta-glucanase B;
DE   Flags: Precursor;
GN   Name=exgB; ORFNames=AFLA_045690;
OS   Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS   / JCM 12722 / SRRC 167).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=332952;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 /
RC   SRRC 167;
RX   PubMed=25883274; DOI=10.1128/genomea.00168-15;
RA   Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA   Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT   "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT   aflatoxin contamination of food and feed.";
RL   Genome Announc. 3:E0016815-E0016815(2015).
CC   -!- FUNCTION: Beta-glucanases participate in the metabolism of beta-glucan,
CC       the main structural component of the cell wall. Acts on lutean,
CC       pustulan and 1,6-oligo-beta-D-glucosides (By similarity).
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Random hydrolysis of (1->6)-linkages in (1->6)-beta-D-
CC         glucans.; EC=3.2.1.75;
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC       {ECO:0000305}.
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DR   EMBL; EQ963476; EED52867.1; -; Genomic_DNA.
DR   RefSeq; XP_002378031.1; XM_002377990.1.
DR   AlphaFoldDB; B8NBJ4; -.
DR   SMR; B8NBJ4; -.
DR   GlyCosmos; B8NBJ4; 1 site, No reported glycans.
DR   EnsemblFungi; EED52867; EED52867; AFLA_045690.
DR   VEuPathDB; FungiDB:AFLA_008154; -.
DR   eggNOG; ENOG502RBRB; Eukaryota.
DR   HOGENOM; CLU_004624_7_0_1; -.
DR   OMA; WMLPAEW; -.
DR   Proteomes; UP000001875; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0052859; F:glucan endo-1,4-beta-glucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046557; F:glucan endo-1,6-beta-glucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR001547; Glyco_hydro_5.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR31297; GLUCAN ENDO-1,6-BETA-GLUCOSIDASE B; 1.
DR   PANTHER; PTHR31297:SF39; 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; Cell wall biogenesis/degradation; Glycoprotein;
KW   Glycosidase; Hydrolase; Polysaccharide degradation; Secreted; Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..392
FT                   /note="Probable glucan endo-1,6-beta-glucosidase B"
FT                   /id="PRO_0000394706"
FT   ACT_SITE        220
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        322
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        31
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   392 AA;  45214 MW;  BD96C170AF70A32C CRC64;
     MKVTRLAVLN TLATLTVAWL PTTDKTITSS NGTDLFKASH GKIRGVNLGS QFVFEPWIAT
     KAWSELGCEG QESEFDCVMK LGQDAANKAF AKHWDSWITK EDIKEIRSYG LNTIRIPVGY
     WMNEDLIYHD SEYFPHGGFA YLEKLCGWAS DAGLYIIIDL HGAPGAQVAK NAFTGQFADT
     PGFYVDFQYQ RALEFLEWMT IKVHTLHNFR NVGMLEVVNE PVQNPQVTTT LRSNYYPNAF
     HSIRKVEGAL SIDRKDYLHI QMMDGAWGAG DPHEHLTDDY YAAYDNHRYL KWDPRVEVSK
     DSYIKTSCND NVATNWPAII GEWSLGVPDN VQETADWKPY SNLDFYQKWF AAQVQNYEQH
     QGWIFWTWKT QLDEYRWSYR GTYLSGFWQT SS
//