XYND_ASPJA
ID XYND_ASPJA Reviewed; 804 AA.
AC B6EY09;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, 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=xylA;
OS Aspergillus japonicus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=34381;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 82-91 AND 413-422,
RP SUBCELLULAR LOCATION, GLYCOSYLATION, FUNCTION, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX DOI=10.1263/jbb.106.398;
RA Wakiyama M., Yosihara K., Hayashi S., Ohta K.;
RT "Purification and properties of an extracellular beta-xylosidase from
RT Aspergillus japonicus and sequence analysis of the encoding gene.";
RL J. Biosci. Bioeng. 106:398-404(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, ECO:0000269|Ref.1}.
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=314 uM for p-nitrophenyl (pNP)-beta-D-xylopyranoside
CC {ECO:0000269|Ref.1};
CC Vmax=114 umol/min/mg enzyme {ECO:0000269|Ref.1};
CC pH dependence:
CC Optimum pH is 4.0. Retains greater than 90 percent of its original
CC activity between pH 2.0 and 7.0 at room temperature for 3 h.
CC {ECO:0000269|Ref.1};
CC Temperature dependence:
CC Optimum temperature 70 degrees Celsius. Remains stable up to 60
CC degrees Celsius for 30 min, but loses activity at 80 degrees Celsius.
CC {ECO:0000269|Ref.1};
CC -!- PATHWAY: Glycan degradation; xylan degradation.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|Ref.1}.
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; AB379633; BAG82824.1; -; Genomic_DNA.
DR AlphaFoldDB; B6EY09; -.
DR SMR; B6EY09; -.
DR CAZy; GH3; Glycoside Hydrolase Family 3.
DR CLAE; XYL3A_ASPJA; -.
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 1: Evidence at protein level;
KW Carbohydrate metabolism; Direct protein sequencing; Glycoprotein;
KW Glycosidase; Hydrolase; Polysaccharide degradation; Secreted; Signal;
KW Xylan degradation.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..804
FT /note="Probable exo-1,4-beta-xylosidase xlnD"
FT /id="PRO_0000393289"
FT ACT_SITE 307
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 139
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 234
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 243
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 349
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 382
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 433
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 444
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 485
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 489
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 621
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 652
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 666
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 688
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 710
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 804 AA; 86258 MW; D12E982EF2227943 CRC64;
MAVAALALLA LLPQALGQHN SSYVDYNVEA NPDLFPQCLD TISLSFPDCQ SGPLSKNLVC
DSTASPYDRA AALVSLFTLE ELIANTGNTS PGVPRLGLPP YQVWSEALHG LARANFTDNG
AYSWATSFPS PILSAAAFNR TLINQIASII STQGRAFNNA GRFGLDVYSP NINTFRHPVW
GRGQETPGED AYTLTAAYAY EYITGIQGGV NPEHLKLAAT AKHFAGYDIE NWDNHSRLGN
DVNITQQDLA EYYTPQFLVA ARDAHVHSFM CSYNAVNGVP SCSNTFFLQT LLRDTFSFVD
HGYVSGDCGA VYGVFNPHGY AANEPSAAAD AILAGTDIDC GTSYQYHFNE SITTGAVARD
DIERGFIRLY ANLVELGYFD GNSSSSNPYR SLGWPDVQKT DAWNISYEAA VEGIVLLKND
GTLPLASPSE GKNKSIALIG PWANATTQLQ GNYYGDAPYL ISPVDAFTAA GYTVHYAPGT
EISTNSTANF SAALSAARAA DTIVFLGGID NTIEAEAQDR SSIAWPGNQL ELISQLAAQK
SDDQPLVVYQ MGGGQVDSSA LKSNAKVNAL LWGGYPGQSG GLALRDILTG ARAPAGRLTT
TQYPAAYAES FSALDMNLRP NETTQNPGQT YMWYTGEPVY AFGHGLFYTT FNASSAQAAK
TKYTFNITDL TSAAHPDTTT VGQRTLFNFT ASITNSGQRD SDYTALVYAN TSTAGPSPYP
NKWLVGFDRL AAVAKEGGTA ELNVPVAVDR LARVDEAGNT VLFPGRYEVA LNNEREVVVE
VELVGEQVVL LKWPEEVQGV AGDE
