ID   XYNF3_ASPFN             Reviewed;         324 AA.
AC   B8NXJ2;
DT   23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 63.
DE   RecName: Full=Probable endo-1,4-beta-xylanase F3;
DE            Short=Xylanase F3;
DE            EC=3.2.1.8;
DE   AltName: Full=1,4-beta-D-xylan xylanohydrolase F3;
DE   Flags: Precursor;
GN   Name=xynF3; Synonyms=xlnF3; ORFNames=AFLA_008110;
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   -!- INDUCTION: Expressed in presence of xylan and repressed by glucose.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F) family.
CC       {ECO:0000305}.
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DR   EMBL; EQ963486; EED44928.1; -; Genomic_DNA.
DR   RefSeq; XP_002385057.1; XM_002385016.1.
DR   AlphaFoldDB; B8NXJ2; -.
DR   SMR; B8NXJ2; -.
DR   STRING; 5059.CADAFLAP00012922; -.
DR   EnsemblFungi; EED44928; EED44928; AFLA_008110.
DR   VEuPathDB; FungiDB:AFLA_008110; -.
DR   eggNOG; ENOG502QSCW; Eukaryota.
DR   HOGENOM; CLU_020161_2_0_1; -.
DR   OMA; PENQMKW; -.
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; 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; PS51760; GH10_2; 1.
PE   2: Evidence at transcript level;
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..324
FT                   /note="Probable endo-1,4-beta-xylanase F3"
FT                   /id="PRO_0000393187"
FT   DOMAIN          45..323
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        260
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   DISULFID        278..284
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   324 AA;  35239 MW;  AD8AEFAF8EDB4496 CRC64;
     MVHLKALASG TLFASLASSA VISRQAAASI NDAFVAHGKK YFGTCSDQAL LQNSQNEAIV
     RADFGQLTPE NSMKWDALEP SQGSFSFAGA DFLADYAKTN NKLVRGHTLV WHSQLPSWVQ
     GITDKDTLTE VIKNHITTIM QRYKGQIYAW DVVNEIFDED GTLRDSVFSQ VLGEDFVRIA
     FETAREADPN AKLYINDYNL DSADYAKTKG MVSYVKKWLD AGVPIDGIVS LLPPRDEGLT
     SCTALTALAS TGVSEVAVTE LDIEGASSES YLEVVNACLD VSSCVGITVW GVSDKDSWRS
     STSPLLFDSN YQAKDAYNAI IDAL