ID   EXGB_NEOFI              Reviewed;         400 AA.
AC   A1DGM6;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   03-MAY-2023, entry version 78.
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=NFIA_084850;
OS   Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS   / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=331117;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 /
RC   NRRL 181 / WB 181;
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; DS027696; EAW18533.1; -; Genomic_DNA.
DR   RefSeq; XP_001260430.1; XM_001260429.1.
DR   AlphaFoldDB; A1DGM6; -.
DR   SMR; A1DGM6; -.
DR   GlyCosmos; A1DGM6; 2 sites, No reported glycans.
DR   EnsemblFungi; EAW18533; EAW18533; NFIA_084850.
DR   GeneID; 4586988; -.
DR   KEGG; nfi:NFIA_084850; -.
DR   VEuPathDB; FungiDB:NFIA_084850; -.
DR   eggNOG; ENOG502RBRB; Eukaryota.
DR   HOGENOM; CLU_004624_7_0_1; -.
DR   OMA; WMLPAEW; -.
DR   OrthoDB; 1431012at2759; -.
DR   Proteomes; UP000006702; 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; Reference proteome;
KW   Secreted; Signal.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..400
FT                   /note="Probable glucan endo-1,6-beta-glucosidase B"
FT                   /id="PRO_0000394711"
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   400 AA;  44823 MW;  F95C0A9E0C957F8A CRC64;
     MIRRLAALSA LSGLATAWLP EVNKKITSTN GTNLFSSSNG KIRGVNLGSQ FVFEPWIAEK
     AWSDMGCGGQ KSEFDCVSSL GQAKANGAFA SHWGSWITQD DLAEMVSYGL NTIRVPVGYW
     MREDLVYSDS EHFPQGGLQY LENLCGWASD AGLYIIIDLH GAPGAQTPQN PFTGQYAPTA
     GFYQDYQFER ALKFLEWMTT NIHQNDKFRN VGMLEVVNEP VQDAGKVGSM RSTYYPNAFK
     RIRAAEQSLN IDRNNYLHIQ MMDRLWGSGD PNESLTDTYY AAYDDHRYLK WAGVAVSKDS
     YISTSCSDQL NSNTPTIVGE WSLSVPDSVQ WNSDWAPDSN KDFYKKWFAA QVTAYEKQQG
     WIFWTWKAQL GDYRWSYQDA VAAGVIPTDL NSLAGLKVCG
//