XYND_ASPNG
ID XYND_ASPNG Reviewed; 804 AA.
AC O00089; O93933;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 2.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=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 niger.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=5061;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=9128738; DOI=10.1111/j.1432-1033.1997.00164.x;
RA van Peij N.N., Brinkmann J., Vrsanska M., Visser J., de Graaff L.H.;
RT "beta-Xylosidase activity, encoded by xlnD, is essential for complete
RT hydrolysis of xylan by Aspergillus niger but not for induction of the
RT xylanolytic enzyme spectrum.";
RL Eur. J. Biochem. 245:164-173(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC 90196 / Alo MP-22;
RX PubMed=11722900; DOI=10.1128/aem.67.12.5512-5519.2001;
RA La Grange D.C., Pretorius I.S., Claeyssens M., van Zyl W.H.;
RT "Degradation of xylan to D-xylose by recombinant Saccharomyces cerevisiae
RT coexpressing the Aspergillus niger beta-xylosidase (xlnD) and the
RT Trichoderma reesei xylanase II (xyn2) genes.";
RL Appl. Environ. Microbiol. 67:5512-5519(2001).
RN [3]
RP INDUCTION.
RX PubMed=9758775; DOI=10.1128/aem.64.10.3615-3619.1998;
RA van Peij N.N., Gielkens M.M., de Vries R.P., Visser J., de Graaff L.H.;
RT "The transcriptional activator XlnR regulates both xylanolytic and
RT endoglucanase gene expression in Aspergillus niger.";
RL Appl. Environ. Microbiol. 64:3615-3619(1998).
RN [4]
RP INDUCTION.
RX PubMed=10376490; DOI=10.1016/s0923-2508(99)80053-9;
RA de Vries R.P., Visser J., de Graaff L.H.;
RT "CreA modulates the XlnR-induced expression on xylose of Aspergillus niger
RT genes involved in xylan degradation.";
RL Res. Microbiol. 150:281-285(1999).
RN [5]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=18421587; DOI=10.1007/s12010-007-8069-z;
RA Selig M.J., Knoshaug E.P., Decker S.R., Baker J.O., Himmel M.E.,
RA Adney W.S.;
RT "Heterologous expression of Aspergillus niger beta-D-xylosidase (XlnD):
RT characterization on lignocellulosic substrates.";
RL Appl. Biochem. Biotechnol. 146:57-68(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:0000269|PubMed:11722900,
CC ECO:0000269|PubMed:18421587, ECO:0000269|PubMed:9128738}.
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=255 uM for pNP-beta-D-xylopyranoside {ECO:0000269|PubMed:11722900,
CC ECO:0000269|PubMed:18421587};
CC pH dependence:
CC Optimum pH is 3.2. {ECO:0000269|PubMed:11722900,
CC ECO:0000269|PubMed:18421587};
CC Temperature dependence:
CC Optimum temperature is 60 degrees Celsius. Has a high thermal
CC denaturation point. The Tmax of the protein was estimated to be 78.2
CC degrees Celsius. {ECO:0000269|PubMed:11722900,
CC ECO:0000269|PubMed:18421587};
CC -!- PATHWAY: Glycan degradation; xylan degradation.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- INDUCTION: Expression is under the control of the xylanolytic
CC transcriptional activator xlnR and the repressor creA.
CC {ECO:0000269|PubMed:10376490, ECO:0000269|PubMed:9758775}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family. {ECO:0000305}.
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DR EMBL; Z84377; CAB06417.1; -; Genomic_DNA.
DR EMBL; AF108944; AAD13106.1; -; mRNA.
DR AlphaFoldDB; O00089; -.
DR SMR; O00089; -.
DR STRING; 5061.CADANGAP00000967; -.
DR BindingDB; O00089; -.
DR ChEMBL; CHEMBL4728; -.
DR Allergome; 3129; Asp n 14.0101.
DR Allergome; 82; Asp n 14.
DR CAZy; GH3; Glycoside Hydrolase Family 3.
DR CLAE; XYL3D_ASPNG; -.
DR VEuPathDB; FungiDB:An01g09960; -.
DR VEuPathDB; FungiDB:ASPNIDRAFT2_1156695; -.
DR VEuPathDB; FungiDB:ATCC64974_15350; -.
DR VEuPathDB; FungiDB:M747DRAFT_324817; -.
DR eggNOG; ENOG502QQ55; Eukaryota.
DR BioCyc; MetaCyc:MON-16902; -.
DR BRENDA; 3.2.1.37; 518.
DR SABIO-RK; O00089; -.
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; IDA:CACAO.
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; Glycoprotein; Glycosidase; Hydrolase;
KW Polysaccharide degradation; Secreted; Signal; Xylan degradation.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..804
FT /note="Exo-1,4-beta-xylosidase xlnD"
FT /id="PRO_0000393290"
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"
FT CONFLICT 37
FT /note="I -> V (in Ref. 2; AAD13106)"
FT /evidence="ECO:0000305"
FT CONFLICT 72
FT /note="T -> S (in Ref. 2; AAD13106)"
FT /evidence="ECO:0000305"
FT CONFLICT 130
FT /note="A -> S (in Ref. 2; AAD13106)"
FT /evidence="ECO:0000305"
FT CONFLICT 220
FT /note="E -> D (in Ref. 2; AAD13106)"
FT /evidence="ECO:0000305"
FT CONFLICT 275
FT /note="Q -> H (in Ref. 2; AAD13106)"
FT /evidence="ECO:0000305"
FT CONFLICT 285
FT /note="N -> D (in Ref. 2; AAD13106)"
FT /evidence="ECO:0000305"
FT CONFLICT 361
FT /note="A -> T (in Ref. 2; AAD13106)"
FT /evidence="ECO:0000305"
FT CONFLICT 372
FT /note="Q -> K (in Ref. 2; AAD13106)"
FT /evidence="ECO:0000305"
FT CONFLICT 402
FT /note="S -> T (in Ref. 2; AAD13106)"
FT /evidence="ECO:0000305"
FT CONFLICT 509
FT /note="Q -> R (in Ref. 2; AAD13106)"
FT /evidence="ECO:0000305"
FT CONFLICT 550
FT /note="A -> S (in Ref. 2; AAD13106)"
FT /evidence="ECO:0000305"
FT CONFLICT 553
FT /note="K -> S (in Ref. 2; AAD13106)"
FT /evidence="ECO:0000305"
FT CONFLICT 578
FT /note="S -> T (in Ref. 2; AAD13106)"
FT /evidence="ECO:0000305"
FT CONFLICT 685
FT /note="D -> E (in Ref. 2; AAD13106)"
FT /evidence="ECO:0000305"
FT CONFLICT 702
FT /note="R -> K (in Ref. 2; AAD13106)"
FT /evidence="ECO:0000305"
FT CONFLICT 729
FT /note="K -> V (in Ref. 2; AAD13106)"
FT /evidence="ECO:0000305"
FT CONFLICT 740
FT /note="E -> D (in Ref. 2; AAD13106)"
FT /evidence="ECO:0000305"
FT CONFLICT 769
FT /note="V -> L (in Ref. 2; AAD13106)"
FT /evidence="ECO:0000305"
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
