XYND_ASPAW
ID XYND_ASPAW Reviewed; 804 AA.
AC Q4AEG8; B5AK91;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 25-MAY-2022, entry version 51.
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=xyl, xylA;
OS Aspergillus awamori (Black koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=105351;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX PubMed=16202538; DOI=10.1016/j.bbagen.2005.08.009;
RA Kurakake M., Fujii T., Yata M., Okazaki T., Komaki T.;
RT "Characteristics of transxylosylation by beta-xylosidase from Aspergillus
RT awamori K4.";
RL Biochim. Biophys. Acta 1726:272-279(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Var. X100;
RA Bobrov K.S., Piens K., Callewaert N., Shabalin K.A., Kulminskaya A.A.;
RT "High-level expression of beta-xylosidase from Aspergillus awamori in
RT Pichia pastoris for the enzymatic production of xylose-containing
RT derivatives.";
RL Submitted (JUN-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:0000269|PubMed:16202538}.
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}.
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; AB154359; BAE19756.1; -; mRNA.
DR EMBL; EU854433; ACF61038.1; -; Genomic_DNA.
DR AlphaFoldDB; Q4AEG8; -.
DR SMR; Q4AEG8; -.
DR CAZy; GH3; Glycoside Hydrolase Family 3.
DR CLAE; XYL3A_ASPAW; -.
DR BRENDA; 3.2.1.37; 494.
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 2: Evidence at transcript 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_0000393284"
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 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; ACF61038)"
FT /evidence="ECO:0000305"
FT CONFLICT 72
FT /note="T -> S (in Ref. 2; ACF61038)"
FT /evidence="ECO:0000305"
FT CONFLICT 130
FT /note="A -> S (in Ref. 2; ACF61038)"
FT /evidence="ECO:0000305"
FT CONFLICT 220
FT /note="E -> D (in Ref. 2; ACF61038)"
FT /evidence="ECO:0000305"
FT CONFLICT 275
FT /note="Q -> H (in Ref. 2; ACF61038)"
FT /evidence="ECO:0000305"
FT CONFLICT 372
FT /note="Q -> K (in Ref. 2; ACF61038)"
FT /evidence="ECO:0000305"
FT CONFLICT 402
FT /note="S -> T (in Ref. 2; ACF61038)"
FT /evidence="ECO:0000305"
FT CONFLICT 509
FT /note="Q -> R (in Ref. 2; ACF61038)"
FT /evidence="ECO:0000305"
FT CONFLICT 550
FT /note="A -> S (in Ref. 2; ACF61038)"
FT /evidence="ECO:0000305"
FT CONFLICT 553
FT /note="K -> S (in Ref. 2; ACF61038)"
FT /evidence="ECO:0000305"
FT CONFLICT 576..578
FT /note="KVS -> NVT (in Ref. 2; ACF61038)"
FT /evidence="ECO:0000305"
FT CONFLICT 681
FT /note="R -> Q (in Ref. 2; ACF61038)"
FT /evidence="ECO:0000305"
FT CONFLICT 702
FT /note="R -> K (in Ref. 2; ACF61038)"
FT /evidence="ECO:0000305"
FT CONFLICT 729
FT /note="K -> V (in Ref. 2; ACF61038)"
FT /evidence="ECO:0000305"
FT CONFLICT 740
FT /note="E -> D (in Ref. 2; ACF61038)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 804 AA; 87311 MW; 23AB04FC19B96211 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
TAGDLSRDDI EQGVIRLYTT LVQAGYFDSN TTKANNPYRD LSWSDVLETD AWNISYQAAT
QGIVLLKNSN NVLPLTEKAY PPSNTTVALI GPWANATTQL LGNYYGNAPY MISPRAAFEE
AGYKVNFAEG TGISSTSTSG FAAALSAAQS ADVIIYAGGI DNTLEAEALD RESIAWPGNQ
LDLIQKLASA AGKKPLIVLQ MGGGQVDSSS LKNNTKVSAL LWGGYPGQSG GFALRDIITG
KKNPAGRLVT TQYPASYAEE FPATDMNLRP EGDNPGQTYK WYTGEAVYEF GHGLFYTTFA
ESSSNTTTKE VKLNIQDILS RTHEELASIT QLPVLNFTAN IRNTGKLESD YTAMVFANTS
DAGPAPYPKK WLVGWDRLGE VKVGETRELR VPVEVGSFAR VNEDGDWVLF PGTFELALNL
ERKVRVKVVL EGEEEVVLKW PGKE
