ID   XYN1_AURPU              Reviewed;         221 AA.
AC   Q96TR7;
DT   09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   25-MAY-2022, entry version 76.
DE   RecName: Full=Endo-1,4-beta-xylanase 1;
DE            Short=Xylanase 1;
DE            EC=3.2.1.8;
DE   AltName: Full=1,4-beta-D-xylan xylanohydrolase 1;
DE   Flags: Precursor;
GN   Name=xynI;
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 [GENOMIC DNA], SUBCELLULAR LOCATION, CATALYTIC
RP   ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=ATCC 20524;
RX   PubMed=16233094; DOI=10.1263/jbb.92.262;
RA   Ohta K., Moriyama S., Tanaka H., Shige T., Akimoto H.;
RT   "Purification and characterization of an acidophilic xylanase from
RT   Aureobasidium pullulans var. melanigenum and sequence analysis of the
RT   encoding gene.";
RL   J. Biosci. Bioeng. 92:262-270(2001).
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. Hydrolyzes xylans from oat spelt and birchwood at
CC       similar rates, but it has no detectable activity toward Avicel or
CC       carboxymethyl 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:16233094};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 2.0. {ECO:0000269|PubMed:16233094};
CC       Temperature dependence:
CC         Optimum temperature is 50 degrees Celsius.
CC         {ECO:0000269|PubMed:16233094};
CC   -!- PATHWAY: Glycan degradation; xylan degradation.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16233094}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 11 (cellulase G) family.
CC       {ECO:0000305}.
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DR   EMBL; AB053298; BAB69655.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q96TR7; -.
DR   SMR; Q96TR7; -.
DR   CAZy; GH11; Glycoside Hydrolase Family 11.
DR   CLAE; XYN11C_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..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..221
FT                   /note="Endo-1,4-beta-xylanase 1"
FT                   /id="PRO_5000049676"
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;  23374 MW;  2578AD73D7436029 CRC64;
     MKFFATIAAL VVAAVAAPVA EADAEASSPM LIERAGPGGI NYVQNYNGNL GQFTYNENAG
     TYSMYWTNGV SGDFVVGLGW STGAARSITY SSSYTASGGS YLSVYGWINS PQAEYYIVES
     YGSYNPCGAG QSGVTQLGTV VSDGATYTVC TDERVNEPSI TGTSTFKQYW SVRQTKRTSG
     TVTTGNHFAY WAKYGFGNSY NFQVMAVEAF SGTGSASVTV S