ID   XYNF1_ASPFN             Reviewed;         327 AA.
AC   B8NER4; A0A7U2MGQ3;
DT   23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2026, sequence version 2.
DT   02-SEP-2026, entry version 72.
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, F9C07_2107378;
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; 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 /
RC   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).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 /
RC   SRRC 167;
RX   PubMed=34849826; DOI=10.1093/g3journal/jkab213;
RA   Skerker J.M., Pianalto K.M., Mondo S.J., Yang K., Arkin A.P., Keller N.P.,
RA   Grigoriev I.V., Glass N.L.;
RT   "Chromosome assembled and annotated genome sequence of Aspergillus flavus
RT   NRRL 3357.";
RL   G3 (Bethesda) 11:jkab213-jkab213(2021).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EED52088.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; EQ963477; EED52088.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP044621; QRD83434.1; -; Genomic_DNA.
DR   AlphaFoldDB; B8NER4; -.
DR   SMR; B8NER4; -.
DR   STRING; 332952.B8NER4; -.
DR   EnsemblFungi; AFLA_005410_t1; KAF7617369.1; AFLA_005410.
DR   VEuPathDB; FungiDB:AFLA_005410; -.
DR   eggNOG; ENOG502QSCW; Eukaryota.
DR   HOGENOM; CLU_020161_2_0_1; -.
DR   OMA; QINDRAT; -.
DR   UniPathway; UPA00114; -.
DR   Proteomes; UP000596276; Chromosome 5.
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   FunFam; 3.20.20.80:FF:000094; Endo-1,4-beta-xylanase; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR044846; GH10.
DR   InterPro; IPR031158; GH10_AS.
DR   InterPro; IPR001000; GH10_dom.
DR   InterPro; IPR017853; GH_hydrolase_sf.
DR   PANTHER; PTHR31490:SF76; ENDO-1,4-BETA-XYLANASE C; 1.
DR   PANTHER; PTHR31490; GLYCOSYL HYDROLASE; 1.
DR   Pfam; PF00331; Glyco_hydro_10; 1.
DR   PRINTS; PR00134; GLHYDRLASE10.
DR   SMART; SM00633; Glyco_10; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 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; Reference proteome; Secreted; Signal;
KW   Xylan degradation.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..327
FT                   /note="Probable endo-1,4-beta-xylanase F1"
FT                   /id="PRO_0000393186"
FT   DOMAIN          45..326
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        263
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10061"
FT   DISULFID        281..287
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   327 AA;  35056 MW;  B9A98CEB5782D044 CRC64;
     MVQFSSIVQC TLLATAASAY VTSRQAAESL HDAFTAAGKK YFGNIAEQAL LENPQNEPII
     AADFGALTCE NSMKWDATEP TQGGYNFDGA DYVVNYAVEK GKLLRGHTLL WHSQLPSWVS
     QISDPATLTG VIQDHVTTLV SRWKGQIYAW DVVNEIFAED GSLRESVFSN VLGEDFVRIA
     FEAARAADPD CKLYINDYNL DDASYSKTQG FVSKVGEWIA AGVPIDGIGS QSHFGAGGFP
     TSGAQAALEA LASTGASEVA VTELDIGGAT SDDWVNVVNA CLNVEKCIGI TVWGVSDKDS
     WRADESPLLF DVNYQPKDAY GAIIAAL
//