GenomeNet

Database: UniProt
Entry: B8NKE9
LinkDB: B8NKE9
Original site: B8NKE9 
ID   XYNA_ASPFN              Reviewed;         232 AA.
AC   B8NKE9;
DT   23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-MAR-2010, sequence version 2.
DT   16-JAN-2019, entry version 49.
DE   RecName: Full=Probable endo-1,4-beta-xylanase A;
DE            Short=Xylanase A;
DE            EC=3.2.1.8;
DE   AltName: Full=1,4-beta-D-xylan xylanohydrolase A;
DE   Flags: Precursor;
GN   Name=xlnA; ORFNames=AFLA_090240;
OS   Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / NRRL 3357 / JCM
OS   12722 / SRRC 167).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=332952;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 200026 / FGSC A1120 / NRRL 3357 / JCM 12722 / SRRC 167;
RX   PubMed=25883274; DOI=10.1128/genomeA.00168-15;
RA   Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA   Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT   "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT   aflatoxin contamination of food and feed.";
RL   Genome Announc. 3:E0016815-E0016815(2015).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EED48943.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; EQ963480; EED48943.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; XP_002380844.1; XM_002380803.1.
DR   ProteinModelPortal; B8NKE9; -.
DR   SMR; B8NKE9; -.
DR   STRING; 5059.CADAFLAP00008709; -.
DR   EnsemblFungi; EED48943; EED48943; AFLA_090240.
DR   GeneID; 7917023; -.
DR   KEGG; afv:AFLA_090240; -.
DR   EuPathDB; FungiDB:AFLA_090240; -.
DR   HOGENOM; HOG000179135; -.
DR   KO; K01181; -.
DR   UniPathway; UPA00114; -.
DR   Proteomes; UP000001875; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0031176; F:endo-1,4-beta-xylanase activity; ISS:UniProtKB.
DR   GO; GO:0045493; P:xylan catabolic process; ISS:UniProtKB.
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; IPR033119; GH11_AS_2.
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; PS00777; GH11_2; 1.
DR   PROSITE; PS51761; GH11_3; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Complete proteome; Glycoprotein; Glycosidase;
KW   Hydrolase; Polysaccharide degradation; Reference proteome; Secreted;
KW   Signal; Xylan degradation.
FT   SIGNAL        1     19       {ECO:0000255}.
FT   CHAIN        20    232       Probable endo-1,4-beta-xylanase A.
FT                                /FTId=PRO_0000393160.
FT   DOMAIN       44    232       GH11. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01097}.
FT   ACT_SITE    128    128       Nucleophile. {ECO:0000255|PROSITE-
FT                                ProRule:PRU10062}.
FT   ACT_SITE    219    219       Proton donor. {ECO:0000255|PROSITE-
FT                                ProRule:PRU10063}.
FT   CARBOHYD     34     34       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
SQ   SEQUENCE   232 AA;  24605 MW;  1F73104751EA561C CRC64;
     MVSFSSILLA CSAAIGALAT PIEPLADHPN EAFNETAFND LVGRSTPSST GYNNGYYYSF
     WTDGGGDVTY TNGNGGSYSV QWSNVGNFVG GKGWNPGSSR AITYSGSFNP SGNGYLAVYG
     WTTDPLIEYY IVESYGTYNP GSGGTYKGQV TSDGGTYNIY TSVRTNAPSI IGTATFTQFW
     SVRTSKRVGG TVTTGNHFNA WAKYGLTLGT HNYQIVATEG YQSSGSSAIT VY
//
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