XYND_ASPAC
ID XYND_ASPAC Reviewed; 805 AA.
AC C0STH4;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 25-MAY-2022, entry version 41.
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=xyl2, xylA;
OS Aspergillus aculeatus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=5053;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=F-50;
RA Sumitani J., Konishi T., Tani S., Arai M., Kawaguchi T.;
RT "Cloning of two xylosidase genes from Aspergillus aculeatus F-50.";
RL Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases.
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; AB462375; BAH30675.1; -; Genomic_DNA.
DR AlphaFoldDB; C0STH4; -.
DR SMR; C0STH4; -.
DR CAZy; GH3; Glycoside Hydrolase Family 3.
DR VEuPathDB; FungiDB:ASPACDRAFT_74214; -.
DR UniPathway; UPA00114; -.
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..17
FT /evidence="ECO:0000255"
FT CHAIN 18..805
FT /note="Probable exo-1,4-beta-xylosidase xlnD"
FT /id="PRO_0000393283"
FT ACT_SITE 308
FT /evidence="ECO:0000250"
FT CARBOHYD 20
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 115
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 140
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 235
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 244
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 350
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 383
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 405
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 434
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 445
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 486
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 490
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 622
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 653
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 667
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 689
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 711
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 805 AA; 86343 MW; 9357F5B982135A27 CRC64;
MAVAALALLA LLPQALGQHN SSYVDYNVEA NPDLFPQCLD TISLSFPDCQ SGPLSKNLVC
DSTASPYDRA AALVSLFTLE ELIANTGNTS PGVPRLGLPP YQVWSEALHG LGRANFTDNG
ALHAGRPSFP SPILSAAAFN RTLINQIASI ISTQGRAFNN AGRFGLDVYS PNINTFRHPV
WGRGQETPGE DAYTLTAAYA YEYITGIQGG VNPEHLKLAA TAKHFAGYDI ENWDNHSRLG
NDVNITQQDL AEYYTPQFLV AARDAHVHSF MCSYNAVNGV PSCSNTFFLQ TLLRDTFSFV
DHGYVSGDCG AVYGVFNPHG YAANEPSAAA DAILAGTDID CGTSYQYHFN ESITTGAVAR
DDIERGFIRL YANLVELGYF DGNSSSSNPY RSLGWPDVQK TDAWNISYEA AVEGIVLLKN
DGTLPLASPS EGKNKSIALI GPWANATTQL QGNYYGDAPY LISPVDAFTA AGYTVHYAPG
TEISTNSTAN FSAALSAARA ADTIVFLGGI DNTIEAEAQD RSSIAWPGNQ LELISQLAAQ
KSDDQPLVVY QMGGGQVDSS SLKFNAKVNA LLWGGYPGQS GGLALRDILT GARAPAGRLT
TTQYPAAYAE SFSALDMNLR PNETTQNPGQ TYMWYTGEPV YAFGHGLFYT TFNASSAQAA
KTKYTFNITD LTSAAHPDTT TVGQRTLFNF TASITNSGQR DSDYTALVYA NTSTAGPSPY
PNKWLVGFDR LAAVAKEGGT AELNVPVAVD RLARVDEAGN TVLFPGRYEV ALNNEREVVV
EVELVGEQVV LLKWPEEVQG VAGDE
