ID   XYNA_ASPTU              Reviewed;         211 AA.
AC   P55331; Q12568;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 2.
DT   22-FEB-2023, entry version 89.
DE   RecName: Full=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   AltName: Full=Endo-1,4-beta-xylanase I;
DE            Short=Xylanase I;
DE   Flags: Precursor;
GN   Name=xynA; Synonyms=xlnA;
OS   Aspergillus tubingensis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=5068;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=NW756;
RX   PubMed=8065265; DOI=10.1111/j.1365-2958.1994.tb01036.x;
RA   de Graaff L.H., van den Broeck H.C., van Ooijen A.J.J., Visser J.;
RT   "Regulation of the xylanase-encoding xlnA gene of Aspergillus tubigensis.";
RL   Mol. Microbiol. 12:479-490(1994).
RN   [2]
RP   SEQUENCE REVISION.
RA   de Graaff L.H., van den Broeck H.C., van Ooijen A.J.J., Visser J.;
RL   Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases.
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.
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 11 (cellulase G) family.
CC       {ECO:0000305}.
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DR   EMBL; L26988; AAB05996.1; -; Genomic_DNA.
DR   PIR; S49542; S49542.
DR   AlphaFoldDB; P55331; -.
DR   SMR; P55331; -.
DR   CAZy; GH11; Glycoside Hydrolase Family 11.
DR   CLAE; XYN11A_ASPTU; -.
DR   VEuPathDB; FungiDB:ASPTUDRAFT_35332; -.
DR   UniPathway; UPA00114; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0031176; F:endo-1,4-beta-xylanase activity; IEA:UniProtKB-EC.
DR   GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-UniPathway.
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   PANTHER; PTHR46828; ENDO-1,4-BETA-XYLANASE A-RELATED; 1.
DR   PANTHER; PTHR46828:SF2; ENDO-1,4-BETA-XYLANASE A-RELATED; 1.
DR   Pfam; PF00457; Glyco_hydro_11; 1.
DR   PRINTS; PR00911; GLHYDRLASE11.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 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; Glycosidase; Hydrolase;
KW   Polysaccharide degradation; Secreted; Signal; Xylan degradation.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000250"
FT   CHAIN           28..211
FT                   /note="Endo-1,4-beta-xylanase A"
FT                   /id="PRO_0000007995"
FT   DOMAIN          28..210
FT                   /note="GH11"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01097"
FT   ACT_SITE        106
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10062"
FT   ACT_SITE        197
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10063"
SQ   SEQUENCE   211 AA;  22576 MW;  1A88D060C67080D4 CRC64;
     MKVTAAFAGL LVTAFAAPAP EPDLVSRSAG INYVQNYNGN LGDFTYDESA GTFSMYWEDG
     VSSDFVVGLG WTTGSSNAIT YSAEYSASGS ASYLAVYGWV NYPQAEYYIV EDYGDYNPCS
     SATSLGTVYS DGSTYQVCTD TRTNEPSITG TSTFTQYFSV RESTRTSGTV TVANHFNFWA
     HHGFGNSDFN YQVVAVEAWS GAGSASVTIS S
//