ID   XYNA_AURPU              Reviewed;         221 AA.
AC   Q12562;
DT   09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 86.
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   Flags: Precursor;
GN   Name=xynA;
OS   Aureobasidium pullulans (Black yeast) (Pullularia pullulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX   NCBI_TaxID=5580;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
RC   STRAIN=NRRL Y-2311-1;
RX   PubMed=7944361; DOI=10.1128/aem.60.9.3160-3166.1994;
RA   Li X.L., Ljungdahl L.G.;
RT   "Cloning, sequencing, and regulation of a xylanase gene from the fungus
RT   Aureobasidium pullulans Y-2311-1.";
RL   Appl. Environ. Microbiol. 60:3160-3166(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=NRRL Y-2311-1;
RA   Kernan R.M., Li X.-L., Ljungdahl L.G.;
RT   "Genomic Sequence of A. Pullulans xynA locus.";
RL   Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   SUBCELLULAR LOCATION, AND CATALYTIC ACTIVITY.
RX   PubMed=8572698; DOI=10.1128/aem.62.1.209-213.1996;
RA   Li X.L., Ljungdahl L.G.;
RT   "Expression of Aureobasidium pullulans xynA in, and secretion of the
RT   xylanase from, Saccharomyces cerevisiae.";
RL   Appl. Environ. Microbiol. 62:209-213(1996).
RN   [4]
RP   INDUCTION.
RX   PubMed=10585539; DOI=10.1111/j.1574-6968.1999.tb08845.x;
RA   Vanden Wymelenberg A., Cullen D., Spear R., Andrews J.;
RT   "Regulated expression of green fluorescent protein under the control of
RT   Aureobasidium pullulans xylanase gene xynA.";
RL   FEMS Microbiol. Lett. 181:205-209(1999).
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; Evidence={ECO:0000269|PubMed:8572698};
CC   -!- PATHWAY: Glycan degradation; xylan degradation.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8572698}.
CC   -!- INDUCTION: Expressed in cultures grown in medium containing D-xylose or
CC       oat spelt xylan. Transcription is completely repressed in the presence
CC       of glucose. {ECO:0000269|PubMed:10585539, ECO:0000269|PubMed:7944361}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 11 (cellulase G) family.
CC       {ECO:0000305}.
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DR   EMBL; U10298; AAA67558.1; -; mRNA.
DR   EMBL; AF011782; AAC39487.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q12562; -.
DR   SMR; Q12562; -.
DR   CAZy; GH11; Glycoside Hydrolase Family 11.
DR   CLAE; XYN11A_AURPU; -.
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; IPR033123; GH11_dom.
DR   InterPro; IPR001137; Glyco_hydro_11.
DR   Pfam; PF00457; Glyco_hydro_11; 1.
DR   PRINTS; PR00911; GLHYDRLASE11.
DR   SUPFAM; SSF49899; SSF49899; 1.
DR   PROSITE; PS00776; GH11_1; 1.
DR   PROSITE; PS51761; GH11_3; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Glycosidase; Hydrolase;
KW   Polysaccharide degradation; Secreted; Signal; Xylan degradation.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   CHAIN           17..221
FT                   /note="Endo-1,4-beta-xylanase A"
FT                   /id="PRO_5000053298"
FT   DOMAIN          29..221
FT                   /note="GH11"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01097"
FT   ACT_SITE        114
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10062"
FT   ACT_SITE        208
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   221 AA;  23531 MW;  81596F3478A3B608 CRC64;
     MKFFATIAAL VVGAVAAPVA EAEAEASSPM LIERAGPGGI NYVQNYNGNL GQFTYNENAG
     TYSMYWNNGV NGDFVVGLGW STGAARSITY SSNYQASGGS YLSVYGWINS PQAEYYIVES
     YGSYNPCGAG QSGVTQLGTV CSDGATYTVY TDTRTNQPSI TGTSTFKQYW SVRQTKRTSG
     TVTTGNHFAY WAKYGFGNSY NFQVMPVEAF SGTGSASVTV S