ID   BXLB_ASPFN              Reviewed;         776 AA.
AC   B8NYD8;
DT   18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 66.
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=AFLA_011080;
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 / SRRC
RC   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: 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; EQ963486; EED45224.1; -; Genomic_DNA.
DR   RefSeq; XP_002385353.1; XM_002385312.1.
DR   AlphaFoldDB; B8NYD8; -.
DR   SMR; B8NYD8; -.
DR   STRING; 5059.CADAFLAP00013218; -.
DR   EnsemblFungi; EED45224; EED45224; AFLA_011080.
DR   VEuPathDB; FungiDB:AFLA_011080; -.
DR   eggNOG; ENOG502QQ55; Eukaryota.
DR   HOGENOM; CLU_004542_5_3_1; -.
DR   OMA; QCARDSN; -.
DR   UniPathway; UPA00114; -.
DR   Proteomes; UP000001875; 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   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..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..776
FT                   /note="Probable exo-1,4-beta-xylosidase bxlB"
FT                   /id="PRO_0000394087"
FT   ACT_SITE        291
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        65
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        105
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        343
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        410
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        421
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        462
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        623
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        766
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   776 AA;  84162 MW;  25E2FC7EA4E23BFF CRC64;
     MVHLSPLLRP LAAFSFFTSL ASTESIFPDC STGPLSKNNV CDTSLDPVSR AKSLVAAMTL
     EEKINNTKYD SSGAPRLGLP AYNWWNEALH GVAEGHGVSF SDSGNFSYAT SFPMPILLGA
     AFDDDLVKQV ATVISTEARA FANGGHAGLD YWTPNINPFR DPRWGRGQET PGEDPLHLSR
     YVYHLVDGLQ DGIGPERPKV VATCKHFAAY DLENWEGIER YAFDAVVSPQ DLSEYYLPSF
     KTCTRDAKVD AVMCSYNSLN GIPTCADRWL LQTLLREHWG WEQTGHWVTG DCGAIDNIYA
     DHHYVADGAH AAAAALNAGT DLDCGSVFPE YLRSALQQGL YNNQTLNNAL IRLYSSLVKL
     GYFDPADDQP YRSIGWNEVF TPAAEELAHK ATVEGIVMLK NDGTLPLKSN GTVAIIGPFA
     NATTQLQGNY EGPPKYIRTL IWAAVHNGYK VKFSQGTDIN SNSSAGFAEA ISAAKEADTV
     IYAGGIDNTI EKESQDRTTI VWPGNQLDLI EQLSDLEKPL IVVQFGGGQV DDSSLLANAG
     VGALLWAGYP SQAGGAAVFD ILTGKSAPAG RLPVTQYPAS YVDEVPMTDM TLRPGSNNPG
     RTYRWYDKAV LPFGFGLHYT TFNVSWNHAE YGPYNTDSVA SGTTNAPVDT ELFDTFSITV
     TNTGNVASDY IALLFLTADR VGPEPYPIKT LVGYSRAKGI EPGQSQQVKL DVSVGSVART
     AENGDLVLYP GSYKLEVDVG QDFPTATFTV SGKEKVLDEF PEPQQNATSA VTRWGR