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   03-AUG-2022, entry version 61.
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 / IAM 13836 / NRRL 3357
OS   / JCM 12722 / SRRC 167).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=332952;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC
RC   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 xylan, a
CC       major structural heterogeneous polysaccharide found in plant biomass
CC       representing the second most abundant polysaccharide in the biosphere,
CC       after cellulose. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.;
CC         EC=3.2.1.8;
CC   -!- PATHWAY: Glycan degradation; xylan degradation.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F) family.
CC       {ECO:0000305}.
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DR   EMBL; EQ963477; EED52088.1; -; Genomic_DNA.
DR   RefSeq; XP_002379095.1; XM_002379054.1.
DR   AlphaFoldDB; B8NER4; -.
DR   SMR; B8NER4; -.
DR   STRING; 5059.CADAFLAP00006960; -.
DR   EnsemblFungi; EED52088; EED52088; AFLA_063510.
DR   VEuPathDB; FungiDB:AFLA_063510; -.
DR   eggNOG; ENOG502QSCW; Eukaryota.
DR   HOGENOM; CLU_020161_2_0_1; -.
DR   OMA; GALTCEN; -.
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; IPR044846; GH10.
DR   InterPro; IPR031158; GH10_AS.
DR   InterPro; IPR001000; GH10_dom.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR31490; PTHR31490; 1.
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; Disulfide bond; Glycosidase; Hydrolase;
KW   Polysaccharide degradation; Secreted; Signal; Xylan degradation.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..332
FT                   /note="Probable endo-1,4-beta-xylanase F1"
FT                   /id="PRO_0000393186"
FT   DOMAIN          45..331
FT                   /note="GH10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01096"
FT   ACT_SITE        155
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        268
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10061"
FT   DISULFID        286..292
FT                   /evidence="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