ID   BXLB_ASPCL              Reviewed;         771 AA.
AC   A1CCL9;
DT   18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 2.
DT   24-JAN-2024, entry version 68.
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=ACLA_062400;
OS   Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS   NRRL 1 / QM 1276 / 107).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=344612;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAW12276.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; DS027050; EAW12276.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; XP_001273702.1; XM_001273701.1.
DR   AlphaFoldDB; A1CCL9; -.
DR   SMR; A1CCL9; -.
DR   STRING; 344612.A1CCL9; -.
DR   GlyCosmos; A1CCL9; 6 sites, No reported glycans.
DR   EnsemblFungi; EAW12276; EAW12276; ACLA_062400.
DR   GeneID; 4705939; -.
DR   KEGG; act:ACLA_062400; -.
DR   eggNOG; ENOG502QQ55; Eukaryota.
DR   OrthoDB; 366914at2759; -.
DR   UniPathway; UPA00114; -.
DR   Proteomes; UP000006701; 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; 3.40.50.1700; Glycoside hydrolase family 3 C-terminal domain; 1.
DR   Gene3D; 3.20.20.300; Glycoside hydrolase, family 3, N-terminal domain; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 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:SF3; BETA-D-XYLOSIDASE 5-RELATED; 1.
DR   PANTHER; PTHR42721; SUGAR HYDROLASE-RELATED; 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; (Trans)glycosidases; 1.
DR   SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Glycoprotein; Glycosidase; Hydrolase;
KW   Polysaccharide degradation; Reference proteome; Secreted; Signal;
KW   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_0000394085"
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        462
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        463
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   771 AA;  83355 MW;  4EA258993A6B26C1 CRC64;
     MVGLTPQHYG NAIALMTYLA STALADNKFP DCTSGPLSKL AVCDTSRDVT TRAQSLVDAM
     SFAEKVNNTQ YEAPGVPRLG LPAYNWWSEA LHGVAGAPGV HFADSGPFSY ATSFAQPILL
     GASFDDELVK QVATVVGTEG RAFGNAGRAG LDYWTPNINP FRDPRWGRGQ ETPGEDPLHV
     SRYVYHLVDG LQGGIGPARP QIAATCKHFA AYDMEDWNGV SRHEFDARVS TQDLAEFYLP
     SFKSCVRDAQ VDAVMCSYNA LNGVPTCADP YLLQTLLREH WDWDQPGHWV VSDCGAIDDI
     YIGHNYTKTG AEAAAVALNA GTDLDCGTVF PKHLGEAAEQ GLYTNQTLDR ALVRLYSSLV
     KLGYFDPAEK QPYGSIGWKD VDTPAAEQLA HKAAVEGIVL LKNDQTLPLK AKGTLALIGP
     YANATKQMQG NYQGPPKYIR TLEWAATQHG YQVQYSPGTA INNSSTAGFA AALAAAKDAD
     VVLYAGGIDN TIESETLDRT TITWPGNQLS LISELSNLHK PLIVIQFGGG QVDDTPLLTN
     PHVNALLWAG YPSQEGGAAI FDILTGKAAP AGRLPITQYP AAYTAQVPMT EMGLRAGGDN
     PGRTYRWYDK AVVPFGFGLH YTSFEVSWDR GRLGPYNTAA LVNRAPGGSH VDRALFDTFR
     VQVQNTGTVT SDYVALLFVK TEDAGPEPYP LKTLVGYTRV QQVKPGERRS VEIEVTLGAM
     ARTAANGDLV LYPGKYTLQV DVGERGYPTA RVSVHGKEVV LDHFPQPPEG R
//