XYND_NEOFI
ID XYND_NEOFI Reviewed; 771 AA.
AC A1DJS5;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 74.
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=NFIA_003180;
OS Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=331117;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC / WB 181;
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(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: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; DS027697; EAW16964.1; -; Genomic_DNA.
DR RefSeq; XP_001258861.1; XM_001258860.1.
DR AlphaFoldDB; A1DJS5; -.
DR SMR; A1DJS5; -.
DR STRING; 36630.CADNFIAP00000147; -.
DR EnsemblFungi; EAW16964; EAW16964; NFIA_003180.
DR GeneID; 4585718; -.
DR KEGG; nfi:NFIA_003180; -.
DR VEuPathDB; FungiDB:NFIA_003180; -.
DR eggNOG; ENOG502QQ55; Eukaryota.
DR HOGENOM; CLU_004542_5_3_1; -.
DR OMA; DKVAMTD; -.
DR OrthoDB; 321444at2759; -.
DR UniPathway; UPA00114; -.
DR Proteomes; UP000006702; 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 PRINTS; PR00133; GLHYDRLASE3.
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..25
FT /evidence="ECO:0000255"
FT CHAIN 26..771
FT /note="Probable exo-1,4-beta-xylosidase xlnD"
FT /id="PRO_0000393294"
FT ACT_SITE 293
FT /evidence="ECO:0000250"
FT CARBOHYD 67
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 305
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 345
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 423
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 464
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 771 AA; 83607 MW; 58D3DA74FF1F3F5D CRC64;
MARIMSWHYG KAITLFVCLG PVALSLDTFP DCSSGPLSKL AVCDTSLDVT TRARSLVNAM
TFEEKVNNTQ YNSPGVPRLG LPAYNWWSEA LHGVAGSPGV EFADSGPFSY ATSFPQPILL
GATFDDDLIK QVATVVSTEG RAFGNAGRAG LDFWTPNINP FRDARWGRGQ ETPGEDPLHV
SRYVYHLVDG LQNGIGPANP KVVATCKHFA AYDLEDWNGV VRHSFNAEVS TQDLSEFYLP
PFKSCARDAK VDAVMCSYNA LNGVPACADS YLLQTILREH WKWDEPGHWI TGDCGAIDDI
YNGHNYTKTP AEAAATALNA GTDLDCGTVF PKYLGQAADE GLYTNKTLDK ALVRLYSSLV
KLGYFDPAED QPYRSIGWKD VDSPAAEALA HKAAVEGIVL LKNDKTLPLK AKGTLALIGP
YANATKQMQG NYEGPPKYIR TLLWAATQAG YDVKYVAGTA INANSTAGFD AALSAAKQAD
VVVYAGGIDN TIEAEGHDRT TIVWPGNQLD LIDQLSKIGK PLVVVQFGGG QVDDSSLLSN
PHVNALLWTG YPSQEGGSAI FDILTGKTAP AGRLPVTQYP ADYVNQVPLT DMALRPGSNT
PGRTYRWYDK AVLPFGFGLH YTTFKISWPR RALGPYDTAA LVSRSPKNVP IDRAAFDTFH
IQVTNTGKTT SDYVALLFLK TIDAGPKPYP LKTLVGYTRA KQIKPGEKRS VDIKVSLGSL
ARTAENGDLV LYPGRYTLEV DVGENQYPTA SFTVKGKEAI LDSFPQPPET R
