XYND_ASPFC
ID XYND_ASPFC Reviewed; 792 AA.
AC B0XP71;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 25-MAY-2022, entry version 48.
DE RecName: Full=Probable exo-1,4-beta-xylosidase xlnD;
DE EC=3.2.1.37;
DE AltName: Full=1,4-beta-D-xylan xylohydrolase xlnD;
DE AltName: Full=Beta-xylosidase A;
DE AltName: Full=Beta-xylosidase xlnD;
DE AltName: Full=Xylobiase xlnD;
DE Flags: Precursor;
GN Name=xlnD; Synonyms=xylA; ORFNames=AFUB_016310;
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; DS499594; EDP56909.1; -; Genomic_DNA.
DR AlphaFoldDB; B0XP71; -.
DR SMR; B0XP71; -.
DR EnsemblFungi; EDP56909; EDP56909; AFUB_016310.
DR VEuPathDB; FungiDB:AFUB_016310; -.
DR HOGENOM; CLU_004542_5_3_1; -.
DR PhylomeDB; B0XP71; -.
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 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..20
FT /evidence="ECO:0000255"
FT CHAIN 21..792
FT /note="Probable exo-1,4-beta-xylosidase xlnD"
FT /id="PRO_0000393286"
FT ACT_SITE 310
FT /evidence="ECO:0000250"
FT CARBOHYD 23
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 87
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 118
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 142
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 246
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 326
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 385
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 404
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 440
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 477
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 518
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 679
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 701
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 792 AA; 86399 MW; B178269570DE7682 CRC64;
MSVAKSIAAV LVALLPGALA QANTSYVDYN VEANPNLTPQ SVATIDLSFP DCENGPLSKT
LVCDTSARPH DRAAALVSMF TFEELVNNTG NTSPGVPRLG LPPYQVWSEA LHGLDRANFT
DEGEYSWATS FPMPILTMSA LNRTLINQIA TIIATQGRAF NNVGRYGLDV YAPNINAFRS
AMWGRGQETP GEDAYCLASA YAYEYITGIQ GGVDPEHLKL VATAKHYAGY DLENWDGHSR
LGNDMNITQQ ELSEYYTPQF LVAARDAKVH SVMCSYNAVN GVPSCANSFF LQTLLRDTFG
FVEDGYVSSD CDSAYNVWNP HEFAANITGA AADSIRAGTD IDCGTTYQYY FGEAFDEQEV
TRAEIERGVI RLYSNLVRLG YFDGNGSVYR DLTWNDVVTT DAWNISYEAA VEGIVLLKND
GTLPLAKSVR SVALIGPWMN VTTQLQGNYF GPAPYLISPL NAFQNSDFDV NYAFGTNISS
HSTDGFSEAL SAAKKSDVII FAGGIDNTLE AEAMDRMNIT WPGNQLQLID QLSQLGKPLI
VLQMGGGQVD SSSLKSNKNV NSLIWGGYPG QSGGQALLDI ITGKRAPAGR LVVTQYPAEY
ATQFPATDMS LRPHGNNPGQ TYMWYTGTPV YEFGHGLFYT TFHASLPGTG KDKTSFNIQD
LLTQPHPGFA NVEQMPLLNF TVTITNTGKV ASDYTAMLFA NTTAGPAPYP NKWLVGFDRL
ASLEPHRSQT MTIPVTIDSV ARTDEAGNRV LYPGKYELAL NNERSVVLQF VLTGREAVIF
KWPVEQQQIS SA
