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XYND_ASPNC
ID   XYND_ASPNC              Reviewed;         804 AA.
AC   A2QA27;
DT   23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   25-MAY-2022, entry version 68.
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=An01g09960;
OS   Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=425011;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
RX   PubMed=17259976; DOI=10.1038/nbt1282;
RA   Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA   Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA   Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA   Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA   Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA   d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA   Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA   van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA   Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA   van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA   Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA   Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA   Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA   Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT   "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT   niger CBS 513.88.";
RL   Nat. Biotechnol. 25:221-231(2007).
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; AM269980; CAK37179.1; -; Genomic_DNA.
DR   RefSeq; XP_001389416.1; XM_001389379.2.
DR   AlphaFoldDB; A2QA27; -.
DR   SMR; A2QA27; -.
DR   Allergome; 82; Asp n 14.
DR   CAZy; GH3; Glycoside Hydrolase Family 3.
DR   PaxDb; A2QA27; -.
DR   EnsemblFungi; CAK37179; CAK37179; An01g09960.
DR   GeneID; 4977682; -.
DR   KEGG; ang:ANI_1_1358014; -.
DR   VEuPathDB; FungiDB:An01g09960; -.
DR   HOGENOM; CLU_004542_5_3_1; -.
DR   UniPathway; UPA00114; -.
DR   Proteomes; UP000006706; Chromosome 2R.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0009044; F:xylan 1,4-beta-xylosidase activity; IDA:AspGD.
DR   GO; GO:0045493; P:xylan catabolic process; IDA:AspGD.
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; Reference proteome; Secreted; Signal;
KW   Xylan degradation.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..804
FT                   /note="Probable exo-1,4-beta-xylosidase xlnD"
FT                   /id="PRO_5000219423"
FT   ACT_SITE        315
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        29
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        124
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        148
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        242
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        251
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        357
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        390
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        413
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        455
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        573
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        576
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        665
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        696
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        718
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   804 AA;  87211 MW;  440D875498C79DF0 CRC64;
     MAHSMSRPVA ATAAALLALA LPQALAQANT SYVDYNIEAN PDLYPLCIET IPLSFPDCQN
     GPLRSHLICD ETATPYDRAA SLISLFTLDE LIANTGNTGL GVSRLGLPAY QVWSEALHGL
     DRANFSDSGA YNWATSFPQP ILTTAALNRT LIHQIASIIS TQGRAFNNAG RYGLDVYAPN
     INTFRHPVWG RGQETPGEDV SLAAVYAYEY ITGIQGPDPE SNLKLAATAK HYAGYDIENW
     HNHSRLGNDM NITQQDLSEY YTPQFHVAAR DAKVQSVMCA YNAVNGVPAC ADSYFLQTLL
     RDTFGFVDHG YVSSDCDAAY NIYNPHGYAS SQAAAAAEAI LAGTDIDCGT TYQWHLNESI
     AAGDLSRDDI EQGVIRLYTT LVQAGYFDSN TTKANNPYRD LSWSDVLETD AWNISYQAAT
     QGIVLLKNSN NVLPLTEKAY PPSNTTVALI GPWANATTQL LGNYYGNAPY MISPRAAFEE
     AGYKVNFAEG TGISSTSTSG FAAALSAAQS ADVIIYAGGI DNTLEAEALD RESIAWPGNQ
     LDLIQKLASA AGKKPLIVLQ MGGGQVDSSS LKNNTNVSAL LWGGYPGQSG GFALRDIITG
     KKNPAGRLVT TQYPASYAEE FPATDMNLRP EGDNPGQTYK WYTGEAVYEF GHGLFYTTFA
     ESSSNTTTKE VKLNIQDILS QTHEDLASIT QLPVLNFTAN IRNTGKLESD YTAMVFANTS
     DAGPAPYPKK WLVGWDRLGE VKVGETRELR VPVEVGSFAR VNEDGDWVVF PGTFELALNL
     ERKVRVKVVL EGEEEVVLKW PGKE
 
 
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