XYND_ASPFU
ID XYND_ASPFU Reviewed; 792 AA.
AC Q4WRB0; Q0H905;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 25-MAY-2022, entry version 92.
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=AFUA_1G16920;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=SL1;
RA Dabrowski S., Ahring B.K.;
RT "Characterization of recombinant xylan degrading enzymes from Aspergillus
RT fumigatus isolate SL1.";
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
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; DQ156554; ABA40420.1; -; mRNA.
DR EMBL; AAHF01000004; EAL91022.1; -; Genomic_DNA.
DR RefSeq; XP_753060.1; XM_747967.1.
DR AlphaFoldDB; Q4WRB0; -.
DR SMR; Q4WRB0; -.
DR STRING; 746128.CADAFUBP00001599; -.
DR CAZy; GH3; Glycoside Hydrolase Family 3.
DR PRIDE; Q4WRB0; -.
DR EnsemblFungi; EAL91022; EAL91022; AFUA_1G16920.
DR GeneID; 3510092; -.
DR KEGG; afm:AFUA_1G16920; -.
DR VEuPathDB; FungiDB:Afu1g16920; -.
DR eggNOG; ENOG502QQ55; Eukaryota.
DR HOGENOM; CLU_004542_5_3_1; -.
DR InParanoid; Q4WRB0; -.
DR OMA; WATSFPM; -.
DR OrthoDB; 321444at2759; -.
DR UniPathway; UPA00114; -.
DR Proteomes; UP000002530; Chromosome 1.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046556; F:alpha-L-arabinofuranosidase activity; IBA:GO_Central.
DR GO; GO:0009044; F:xylan 1,4-beta-xylosidase activity; IBA:GO_Central.
DR GO; GO:0031222; P:arabinan catabolic process; IBA:GO_Central.
DR GO; GO:0045493; P:xylan catabolic process; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Carbohydrate metabolism; Glycoprotein; Glycosidase; Hydrolase;
KW Polysaccharide degradation; Reference proteome; Secreted; Signal;
KW 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_0000393288"
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"
FT CONFLICT 2
FT /note="S -> A (in Ref. 1; ABA40420)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 792 AA; 86386 MW; 40B9A6757053240F CRC64;
MSVAKSIAAV LVALLPGALA QANTSYVDYN VEANPDLTPQ 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 VLTGREAVVF
KWPVEQQQIS SA
