ID   EXGB_ASPFC              Reviewed;         396 AA.
AC   B0XRX9;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 52.
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=AFUB_025210;
OS   Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus
OS   fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=451804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CEA10 / CBS 144.89 / FGSC A1163;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
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; DS499595; EDP54465.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0XRX9; -.
DR   SMR; B0XRX9; -.
DR   EnsemblFungi; EDP54465; EDP54465; AFUB_025210.
DR   VEuPathDB; FungiDB:AFUB_025210; -.
DR   HOGENOM; CLU_004624_7_0_1; -.
DR   PhylomeDB; B0XRX9; -.
DR   Proteomes; UP000001699; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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   InterPro; IPR001547; Glyco_hydro_5.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   Pfam; PF00150; Cellulase; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Cell wall biogenesis/degradation; Glycoprotein;
KW   Glycosidase; Hydrolase; Polysaccharide degradation; Secreted; Signal.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..396
FT                   /note="Probable glucan endo-1,6-beta-glucosidase B"
FT                   /id="PRO_0000394705"
FT   ACT_SITE        219
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        320
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        30
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        272
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   396 AA;  44894 MW;  2ECFAB9C6F6BEF38 CRC64;
     MIRRLAAFSA LSGLATAWLP EVNKKITSTN GTNLFTSSNG KIRGVNLGSQ FVFEPWIAEK
     AWSDMGCGGQ KSEFDCVSRL GQANANSAFA SHWGSWITQD DIAEMVSYGL NTIRVPVGYW
     MREDLVYSDS EHFPQGGLQY LENLCEWASD AGLYIIIDLH GAPGAQTPQN PFTGQYAPIA
     GFYQDYQFER ALKFLEWMTT NIHQNDKFRN VGMLEVVNEP VQDAGKVGSM RSSYYPNAFK
     RIRAAEQSLN IDRNNYLHIQ MMDRLWGSGD PNESLTDTYY AAYDDHRYLK WASVAVSKDS
     YISTSCSDQL NSNTPTIVGE WSLSVPDNVQ WNSDWSPDSN KDFYKKWFAA QVTAYERQQG
     WIFWTWKAQL GDYRWSYQGG LLLTRPGIGD QQVLTL