ID   XYN2_AURPU              Reviewed;         361 AA.
AC   Q2PGV8;
DT   09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   25-MAY-2022, entry version 52.
DE   RecName: Full=Endo-1,4-beta-xylanase 2;
DE            Short=Xylanase 2;
DE            EC=3.2.1.8;
DE   AltName: Full=1,4-beta-D-xylan xylanohydrolase 2;
DE   Flags: Precursor;
GN   Name=xynII;
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], PROTEIN SEQUENCE OF 27-43; 75-84 AND
RP   277-286, SUBCELLULAR LOCATION, FUNCTION, CATALYTIC ACTIVITY, AND
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=ATCC 20524;
RX   PubMed=15988573; DOI=10.1007/s00253-005-0045-3;
RA   Tanaka H., Muguruma M., Ohta K.;
RT   "Purification and properties of a family-10 xylanase from Aureobasidium
RT   pullulans ATCC 20524 and characterization of the encoding gene.";
RL   Appl. Microbiol. Biotechnol. 70:202-211(2006).
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 birch-wood xylan, with a similar activity
CC       toward oat-spelt xylan. Also shows weak activities toward pNP-beta-D-
CC       cellobioside and pNP-beta-D-xylopyranoside, but no detectable activity
CC       toward carboxymethyl cellulose and pNP-beta-L-arabinofuranoside.-.
CC       {ECO:0000269|PubMed:15988573}.
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:15988573};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 6.0. {ECO:0000269|PubMed:15988573};
CC       Temperature dependence:
CC         Optimum temperature is 70 degrees Celsius.
CC         {ECO:0000269|PubMed:15988573};
CC   -!- PATHWAY: Glycan degradation; xylan degradation.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15988573}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F) family.
CC       {ECO:0000305}.
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DR   EMBL; AB201542; BAE71410.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2PGV8; -.
DR   SMR; Q2PGV8; -.
DR   CAZy; GH10; Glycoside Hydrolase Family 10.
DR   CLAE; XYN10B_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   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   1: Evidence at protein level;
KW   Carbohydrate metabolism; Direct protein sequencing; Disulfide bond;
KW   Glycoprotein; Glycosidase; Hydrolase; Polysaccharide degradation; Secreted;
KW   Signal; Xylan degradation.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000269|PubMed:15988573"
FT   CHAIN           27..361
FT                   /note="Endo-1,4-beta-xylanase 2"
FT                   /id="PRO_5000052217"
FT   DOMAIN          46..354
FT                   /note="GH10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01096"
FT   ACT_SITE        160
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        276
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        88
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        130
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        304..310
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   361 AA;  39938 MW;  DB1DFFC29CF91942 CRC64;
     MHFSTITAAL ALLGLGAATP TDYSTSSYSK NQGLAQAWTS KGRQYIGTAL TIRDDPVEQG
     IIQSRTDFNS ITPENAMKWE STEPQRNNFT FAGADAVADF ADRYNKEMRC HTLVWHSQLP
     AWVSQGNFDN KTLISIMENH IKKVAGRYKN KCTHWDVVNE ALNEDGTYRS SVFYNTIGEA
     FIPIAFRFAE KYAGSKTKLY YNDYNLEYGS AKALGAQRIL KLVQSYGVQI DGVGLQAHLS
     SEATASTGGG VTPDVQTLTN VLKLYTDLGV EVAYTELDVR FTTPATDAKL KAQADAYARV
     VQSCINVKRC VGITVWGVSD KYSWIPGVFP TEGAALLWDE NFNKKPAYSS VLKTIQSFRK
     S