XYND_ASPTN
ID XYND_ASPTN Reviewed; 793 AA.
AC Q0CMH8;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-MAR-2010, sequence version 2.
DT 25-MAY-2022, entry version 59.
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=ATEG_05106;
OS Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=341663;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIH 2624 / FGSC A1156;
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA Nierman W.C., Milne T., Madden K.;
RT "Annotation of the Aspergillus terreus NIH2624 genome.";
RL Submitted (SEP-2005) 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: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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAU34175.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; CH476600; EAU34175.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001214284.1; XM_001214284.1.
DR AlphaFoldDB; Q0CMH8; -.
DR SMR; Q0CMH8; -.
DR STRING; 341663.Q0CMH8; -.
DR GeneID; 4320717; -.
DR eggNOG; ENOG502QQ55; Eukaryota.
DR OrthoDB; 321444at2759; -.
DR UniPathway; UPA00114; -.
DR Proteomes; UP000007963; Unassembled WGS sequence.
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 3: Inferred from homology;
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..793
FT /note="Probable exo-1,4-beta-xylosidase xlnD"
FT /id="PRO_0000393292"
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 142
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 559
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 614
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 679
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 701
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 793 AA; 86222 MW; 74BFEEB5256164C6 CRC64;
MPRVASVAAV LAALLPSALG QANTSYVDYN HEANPDLFPQ CVATIELSFP DCENGPLSKT
LVCDKSARPH DRAAALVSMF TLEELVNNTG NTGTGVPRLG LPKYQVWSES LHGVYRANWA
SEGDYSWATS FPQPILTMAA LNRTLIHQIG DILSTQARAF SNVGRYGLDT YAPNINSFRH
PVWGRGQETP GEDAYYLAST YAYEYITGIQ GGVDPETLKL VATAKHYAGY DIENWDGHSR
LGNDMQITQQ DLSEYYTPQF LVSARDAKVH SVMCSYNAVN GVPSCSNSFF LQTLLRETFG
FVEDGYVSGD CGAVYNAFNP HEYAANESSA SADSIRAGTD IDCGTSYQYH FTNAFDEGEI
SRQDIERGVI RLYTNLVRLG YFDGNSSQYR DLTWSDVQTT DAWNISHEAA VEGTVLLKND
GTLPLADSIR SVALIGPWAN ATTQMQGNYY GPAPYLTSPL AALEASDLDV HYAFGTNISS
TTTAGFADAL AAARKADAII FAGGIDNTIE GEALDRMNIT WPGNQLDLIN QLSALGKPLV
VLQMGGGQVD SSALKHNTNV SALLWGGYPG QSGGTALLDI IRGVRAPAGR LVTTQYPAGY
ATQFPAIDMG LRPNGTNPGQ TYMWYTGTPV YEFGHGLFYT TFEAKRASTA TNHSSFNIED
LLTAPHPGYA YPQLRPFLNF TAHITNTGRT TSDYTAMLFA NTTAGPAPHP NKWLVGFDRL
GALEPGASQT MTFPITIDNV ARTDELGNRV LYPGRYELAL NNERSVVLRF TLTGEKAVLM
KWPLEKQEIP PAA
