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Database: UniProt
Entry: A2R4D1
LinkDB: A2R4D1
Original site: A2R4D1 
ID   XYN5_ASPNC              Reviewed;         211 AA.
AC   A2R4D1;
DT   23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   10-APR-2019, entry version 65.
DE   RecName: Full=Probable endo-1,4-beta-xylanase 5;
DE            Short=Xylanase 5;
DE            EC=3.2.1.8;
DE   AltName: Full=1,4-beta-D-xylan xylanohydrolase 5;
DE   Flags: Precursor;
GN   Name=XYN5; ORFNames=An14g07390;
OS   Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=425011;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 513.88 / FGSC A1513;
RX   PubMed=17259976; DOI=10.1038/nbt1282;
RA   Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G.,
RA   Schaap P.J., Turner G., de Vries R.P., Albang R., Albermann K.,
RA   Andersen M.R., Bendtsen J.D., Benen J.A.E., van den Berg M.,
RA   Breestraat S., Caddick M.X., Contreras R., Cornell M., Coutinho P.M.,
RA   Danchin E.G.J., Debets A.J.M., Dekker P., van Dijck P.W.M.,
RA   van Dijk A., Dijkhuizen L., Driessen A.J.M., d'Enfert C., Geysens S.,
RA   Goosen C., Groot G.S.P., de Groot P.W.J., Guillemette T.,
RA   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.,
RA   van der Kaaij R.M., Klis F.M., Kools H.J., Kubicek C.P.,
RA   van Kuyk P.A., Lauber J., Lu X., van der Maarel M.J.E.C.,
RA   Meulenberg R., Menke H., Mortimer M.A., Nielsen J., Oliver S.G.,
RA   Olsthoorn M., Pal K., van Peij N.N.M.E., Ram A.F.J., Rinas U.,
RA   Roubos J.A., Sagt C.M.J., Schmoll M., Sun J., Ussery D., Varga J.,
RA   Vervecken W., van de Vondervoort P.J.J., Wedler H., Woesten H.A.B.,
RA   Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT   "Genome sequencing and analysis of the versatile cell factory
RT   Aspergillus niger CBS 513.88.";
RL   Nat. Biotechnol. 25:221-231(2007).
CC   -!- FUNCTION: Endo-1,4-beta-xylanase involved in the hydrolysis of
CC       xylan, a major structural heterogeneous polysaccharide found in
CC       plant biomass representing the second most abundant polysaccharide
CC       in the biosphere, after cellulose. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in
CC         xylans.; EC=3.2.1.8;
CC   -!- PATHWAY: Glycan degradation; xylan degradation.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 11 (cellulase G)
CC       family. {ECO:0000305}.
DR   EMBL; AM270327; CAK46731.1; -; Genomic_DNA.
DR   RefSeq; XP_001401361.1; XM_001401324.1.
DR   ProteinModelPortal; A2R4D1; -.
DR   SMR; A2R4D1; -.
DR   PaxDb; A2R4D1; -.
DR   EnsemblFungi; CAK46731; CAK46731; An14g07390.
DR   GeneID; 4987596; -.
DR   KEGG; ang:ANI_1_1008124; -.
DR   HOGENOM; HOG000179135; -.
DR   KO; K01181; -.
DR   UniPathway; UPA00114; -.
DR   Proteomes; UP000006706; Chromosome 1R.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0031176; F:endo-1,4-beta-xylanase activity; IEA:UniProtKB-EC.
DR   GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 2.60.120.180; -; 1.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR013319; GH11/12.
DR   InterPro; IPR018208; GH11_AS_1.
DR   InterPro; IPR033123; GH11_dom.
DR   InterPro; IPR001137; Glyco_hydro_11.
DR   Pfam; PF00457; Glyco_hydro_11; 1.
DR   PRINTS; PR00911; GLHYDRLASE11.
DR   SUPFAM; SSF49899; SSF49899; 1.
DR   PROSITE; PS00776; GH11_1; 1.
DR   PROSITE; PS51761; GH11_3; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Complete proteome; Glycosidase; Hydrolase;
KW   Polysaccharide degradation; Reference proteome; Secreted; Signal;
KW   Xylan degradation.
FT   SIGNAL        1     16       {ECO:0000255}.
FT   CHAIN        17    211       Probable endo-1,4-beta-xylanase 5.
FT                                /FTId=PRO_5000220988.
FT   DOMAIN       19    210       GH11. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01097}.
FT   COMPBIAS     86     92       Poly-Ser.
FT   ACT_SITE    106    106       Nucleophile. {ECO:0000255|PROSITE-
FT                                ProRule:PRU10062}.
FT   ACT_SITE    197    197       Proton donor. {ECO:0000250}.
SQ   SEQUENCE   211 AA;  22639 MW;  DECA078B58E362F0 CRC64;
     MKVTAAFASL LLTAFAAPAP EPVLVSRSAG INYVQNYNGN LGDFTYDEST GTFSMYWEDG
     VSSDFVVGLG WTTGSSKSIT YSAQYSASSS SSYLAVYGWV NSPQAEYYIV EDYGDYNPCS
     SATSLGTVYS DGSTYQVCTD TRTNAPSITG TSTFTQYFSV RESTRTSGTV TIANHFNFWA
     QHGFGNSNFN YQVMAVEAWN GAGSASVTIS S
//
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