ID   BXLB_ASPFC              Reviewed;         771 AA.
AC   B0Y0I4;
DT   18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 50.
DE   RecName: Full=Probable exo-1,4-beta-xylosidase bxlB;
DE            EC=3.2.1.37;
DE   AltName: Full=1,4-beta-D-xylan xylohydrolase bxlB;
DE   AltName: Full=Beta-xylosidase bxlB;
DE   AltName: Full=Xylobiase bxlB;
DE   Flags: Precursor;
GN   Name=bxlB; ORFNames=AFUB_046310;
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: Xylan 1,4-beta-xylosidase involved in the hydrolysis of
CC       xylan, a major structural heterogeneous polysaccharide found in plant
CC       biomass representing the second most abundant polysaccharide in the
CC       biosphere, after cellulose. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of (1->4)-beta-D-xylans, to remove successive D-
CC         xylose residues from the non-reducing termini.; EC=3.2.1.37;
CC   -!- PATHWAY: Glycan degradation; xylan degradation.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family. {ECO:0000305}.
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DR   EMBL; DS499596; EDP53454.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0Y0I4; -.
DR   SMR; B0Y0I4; -.
DR   EnsemblFungi; EDP53454; EDP53454; AFUB_046310.
DR   VEuPathDB; FungiDB:AFUB_046310; -.
DR   HOGENOM; CLU_004542_5_3_1; -.
DR   PhylomeDB; B0Y0I4; -.
DR   UniPathway; UPA00114; -.
DR   Proteomes; UP000001699; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0009044; F:xylan 1,4-beta-xylosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 2.60.40.10; -; 1.
DR   Gene3D; 3.20.20.300; -; 1.
DR   Gene3D; 3.40.50.1700; -; 1.
DR   InterPro; IPR044993; BXL.
DR   InterPro; IPR026891; Fn3-like.
DR   InterPro; IPR002772; Glyco_hydro_3_C.
DR   InterPro; IPR036881; Glyco_hydro_3_C_sf.
DR   InterPro; IPR001764; Glyco_hydro_3_N.
DR   InterPro; IPR036962; Glyco_hydro_3_N_sf.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
DR   PANTHER; PTHR42721; PTHR42721; 1.
DR   Pfam; PF14310; Fn3-like; 1.
DR   Pfam; PF00933; Glyco_hydro_3; 1.
DR   Pfam; PF01915; Glyco_hydro_3_C; 1.
DR   PRINTS; PR00133; GLHYDRLASE3.
DR   SMART; SM01217; Fn3_like; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   SUPFAM; SSF52279; SSF52279; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Glycoprotein; Glycosidase; Hydrolase;
KW   Polysaccharide degradation; Secreted; Signal; Xylan degradation.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..771
FT                   /note="Probable exo-1,4-beta-xylosidase bxlB"
FT                   /id="PRO_0000394086"
FT   ACT_SITE        293
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        67
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        305
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        345
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        423
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        464
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   771 AA;  83338 MW;  CCD470944B5AC300 CRC64;
     MAHITSWHYG NAIALLVSLA PGALSLNTFP DCSSGPLSKL AVCDTSLDVT TRAQSLVNAM
     TFEEKVNNTQ YNSPGVPRLG LPAYNWWSEA LHGVAGSPGV EFADSGPFSY ATSFPQPILL
     GATFDDDLIK QVATVVSTEG RAFGNAGRSG LDFWTPNINP FRDARWGRGQ ETPGEDPLHV
     SRYVYHLVDG LQNGIGPANP KVVATCKHFA AYDLEDWNGV VRHSFNAEVS TQDLSEFYLP
     PFKSCARDAR VDAVMCSYNA LNGVPACADS YLLQTILREH WKWDEPGRWI TSDCGAIDDI
     YNGHNFTTTP AEAAATALNA GTDLDCGTVF PKYLGQAADE GLYSNQTLDR ALVRLYSSLV
     KLGYFDPAED QPYRSIGWTD VDTPAAEALA HKAAGEGIVL LKNDKTLPLK AKGTLALIGP
     YANATKQMQG NYEGPAKYIR TLLWAATQAG YDVKYAAGTA INTNSTAGFD AALSAAKQAD
     VVVYAGGIDN TIEAEGRDRT TIAWPGNQVN LIDQLSKIGK PLVVVQFGGG QVDDSSLLSN
     PRVNALLWAG YPSQEGGSAI FDILTGKTAP AGRLPVTQYP ADYVNQVPMT DMALRPGSNT
     PGRTYRWYDK AVLPFGFGLH YTTFKISWPR RALGPYNTAA LVSRSPKNVP IDRAAFDTFH
     IQVTNTGKTT SDYVALLFLK TTDAGPKPYP LKTLVGYTRA KQIKPGEKRS VDIEVSLGSL
     ARTAENGDLV LYPGRYTLEV DVGESQYPTA SFTVTGKETI LDSFPQPPKT R