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
//
