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EXGB_ASPFU
ID   EXGB_ASPFU              Reviewed;         396 AA.
AC   Q4X1N4;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   25-MAY-2022, entry version 86.
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=AFUA_2G09350;
OS   Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS   A1100) (Aspergillus fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=330879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA   Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA   Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA   Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA   Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA   Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA   Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA   O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA   Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA   Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA   Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA   Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA   Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA   Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA   Barrell B.G., Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(2005).
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; AAHF01000001; EAL93231.1; -; Genomic_DNA.
DR   RefSeq; XP_755269.1; XM_750176.1.
DR   AlphaFoldDB; Q4X1N4; -.
DR   SMR; Q4X1N4; -.
DR   STRING; 746128.CADAFUBP00002464; -.
DR   EnsemblFungi; EAL93231; EAL93231; AFUA_2G09350.
DR   GeneID; 3513261; -.
DR   KEGG; afm:AFUA_2G09350; -.
DR   VEuPathDB; FungiDB:Afu2g09350; -.
DR   eggNOG; ENOG502RBRB; Eukaryota.
DR   HOGENOM; CLU_004624_7_0_1; -.
DR   InParanoid; Q4X1N4; -.
DR   OMA; WMLPAEW; -.
DR   OrthoDB; 916629at2759; -.
DR   Proteomes; UP000002530; Chromosome 2.
DR   GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR   GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR   GO; GO:0008422; F:beta-glucosidase activity; IBA:GO_Central.
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:0006073; P:cellular glucan metabolic process; IBA:GO_Central.
DR   GO; GO:0009251; P:glucan catabolic process; IBA:GO_Central.
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; Reference proteome;
KW   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_0000394707"
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;  44795 MW;  D53B00929BC0E598 CRC64;
     MIRRLAAFSA LSGLATAWLP EVNKKITSTN GTNLFTSSNG KIRGVNLGSQ FVFEPWIAEK
     AWSDMGCGGQ KSEFDCVSRL GQANANSAFA SHWGSWITQD DIAEMVSYGL NTIRVPVGYW
     MREDLVYSDS EHFPQGGLQY LENLCEWASD AGLYIIIDLH GAPGAQTPQN PFTGQYAPIA
     GFYQDYQFEG ALKFLEWMTT NIHQNDKFRN VGMLEVVNEP VQDAGKVGSM RSSYYPNAFK
     RIRAAEQSLN IDRNNYLHIQ MMDRLWGSGD PNESLTDTYY AAYDDHRYLK WASVAVSKDS
     YISTSCSDQL NSNTPTIVGE WSLSVPDNVQ WNSDWSPDSN KDFYKKWFAA QVTAYERQQG
     WIFWTWKAQL GDYRWSYQGG LLLTRPGIGD QQVLTL
 
 
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