GenomeNet

Database: UniProt
Entry: B8NER4
LinkDB: B8NER4
Original site: B8NER4 
ID   XYNF1_ASPFN             Reviewed;         332 AA.
AC   B8NER4;
DT   23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   05-JUL-2017, entry version 44.
DE   RecName: Full=Probable endo-1,4-beta-xylanase F1;
DE            Short=Xylanase F1;
DE            EC=3.2.1.8;
DE   AltName: Full=1,4-beta-D-xylan xylanohydrolase F1;
DE   Flags: Precursor;
GN   Name=xynF1; Synonyms=xlnF1; ORFNames=AFLA_063510;
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: Endohydrolysis of (1->4)-beta-D-xylosidic
CC       linkages in xylans.
CC   -!- PATHWAY: Glycan degradation; xylan degradation.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F)
CC       family. {ECO:0000305}.
DR   EMBL; EQ963477; EED52088.1; -; Genomic_DNA.
DR   RefSeq; XP_002379095.1; XM_002379054.1.
DR   ProteinModelPortal; B8NER4; -.
DR   SMR; B8NER4; -.
DR   STRING; 5059.CADAFLAP00006960; -.
DR   EnsemblFungi; EED52088; EED52088; AFLA_063510.
DR   GeneID; 7918606; -.
DR   KEGG; afv:AFLA_063510; -.
DR   EuPathDB; FungiDB:AFLA_063510; -.
DR   HOGENOM; HOG000019847; -.
DR   KO; K01181; -.
DR   OMA; GALTCEN; -.
DR   OrthoDB; EOG092C45ID; -.
DR   UniPathway; UPA00114; -.
DR   Proteomes; UP000001875; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR   GO; GO:0031176; F:endo-1,4-beta-xylanase activity; ISS:UniProtKB.
DR   GO; GO:0045493; P:xylan catabolic process; ISS:UniProtKB.
DR   InterPro; IPR001000; GH10.
DR   InterPro; IPR031158; GH10_AS.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   Pfam; PF00331; Glyco_hydro_10; 1.
DR   PRINTS; PR00134; GLHYDRLASE10.
DR   SMART; SM00633; Glyco_10; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS00591; GH10_1; 1.
DR   PROSITE; PS51760; GH10_2; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Complete proteome; Disulfide bond;
KW   Glycosidase; Hydrolase; Polysaccharide degradation;
KW   Reference proteome; Secreted; Signal; Xylan degradation.
FT   SIGNAL        1     19       {ECO:0000255}.
FT   CHAIN        20    332       Probable endo-1,4-beta-xylanase F1.
FT                                /FTId=PRO_0000393186.
FT   DOMAIN       45    331       GH10. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01096}.
FT   ACT_SITE    155    155       Proton donor. {ECO:0000250}.
FT   ACT_SITE    268    268       Nucleophile. {ECO:0000255|PROSITE-
FT                                ProRule:PRU10061}.
FT   DISULFID    286    292       {ECO:0000250}.
SQ   SEQUENCE   332 AA;  35777 MW;  A374339B5129FDA4 CRC64;
     MVQFSSIVQC TLLATAASAY VTSRQAAESL HDAFTAAGKK YFGNIAEQAL LENPQNEPII
     AADFGALTCE NSMKWDATEP TQGGYNFDGA DYVVNYAVEK GKLLRGHTLL WHSQLPSWVS
     QISDPATLTG VIQDHVTTLV SRWKGQIYAW DVVNEIFAED GSLRESVFSN VLGEDFVRIA
     FEAARAADPD CKLYINDYNL DDASYSKTQG FVSKVGEWIA AGVPIDGIGM WLACLFKHAY
     AGGFPTSGAQ AALEALASTG ASEVAVTELD IGGATSDDWV NVVNACLNVE KCIGITVWGV
     SDKDSWRADE SPLLFDVNYQ PKDAYGAIIA AL
//
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