ID   XYNA_TALPU              Reviewed;         329 AA.
AC   Q9P8J1;
DT   09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 76.
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   Talaromyces purpureogenus (Soft rot fungus) (Penicillium purpureogenum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC   Talaromyces sect. Talaromyces.
OX   NCBI_TaxID=1266744;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=11715859; DOI=10.4067/s0716-97602001000300009;
RA   Chavez R., Almarza C., Schachter K., Peirano A., Bull P., Eyzaguirre J.;
RT   "Structure analysis of the endoxylanase A gene from penicillium
RT   purpurogenum.";
RL   Biol. Res. 34:217-226(2001).
RN   [2]
RP   SUBCELLULAR LOCATION, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP   PROPERTIES, AND ACTIVITY REGULATION.
RX   PubMed=7640003; DOI=10.1016/0168-1656(95)00057-w;
RA   Belancic A., Scarpa J., Peirano A., Diaz R., Steiner J., Eyzaguirre J.;
RT   "Penicillium purpurogenum produces several xylanases: purification and
RT   properties of two of the enzymes.";
RL   J. Biotechnol. 41:71-79(1995).
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. {ECO:0000269|PubMed:7640003}.
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:7640003};
CC   -!- ACTIVITY REGULATION: N-bromosuccinimide completely inhibits the
CC       catalytic activity. {ECO:0000269|PubMed:7640003}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 7.0. {ECO:0000269|PubMed:7640003};
CC       Temperature dependence:
CC         Optimum temperature is 60 degrees Celsius.
CC         {ECO:0000269|PubMed:7640003};
CC   -!- PATHWAY: Glycan degradation; xylan degradation.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- INDUCTION: Expression is induced by oat spelt xylan but not by
CC       birchwood xylan, xylose, or xylitol. Expression is repressed by
CC       glucose. The promoter contains 3 creA consensus binding sites, 1 xlnR
CC       consensus binding site, and 3 pH activator pacC consensus binding
CC       sites.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F) family.
CC       {ECO:0000305}.
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DR   EMBL; AF249328; AAF71268.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9P8J1; -.
DR   SMR; Q9P8J1; -.
DR   CAZy; GH10; Glycoside Hydrolase Family 10.
DR   CLAE; XYN10A_PENPU; -.
DR   BRENDA; 3.2.1.8; 4635.
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; IPR031158; GH10_AS.
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; PS00591; GH10_1; 1.
DR   PROSITE; PS51760; GH10_2; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Disulfide bond; Glycoprotein; Glycosidase;
KW   Hydrolase; Polysaccharide degradation; Secreted; Signal; Xylan degradation.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..329
FT                   /note="Endo-1,4-beta-xylanase A"
FT                   /id="PRO_0000429661"
FT   DOMAIN          48..328
FT                   /note="GH10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01096"
FT   ACT_SITE        159
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        265
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10061"
FT   CARBOHYD        285
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        283..289
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   329 AA;  35351 MW;  EF4AEFCC8D1F5175 CRC64;
     MVQLKTAALA LLFAGQAISS PVDIDSRQAS VSIDAKFKAH GKKYLGTIGD QYTLTKNSKN
     PAIIKADFGQ LTPENSMKWD ATEPNRGQFS FSGSDYLVNF AQSNGKLIRG HTLVWHSQLP
     GWVSSITDKN TLISVLKNHI TTVMTRYKGK IYAWDVLNEI FNEDGSLRNS VFYNVIGEDY
     VRIAFETARS VDPNAKLYIN DYNLDSAGYS KVNGMVSHVK KWLAAGIPID GIGSQTHLGA
     GAGANVAGAL NALAGAGTTE IAITELDIAG ASSTDYVNVV KACLNQSKCV GITVWGVADP
     DSWRSSSSPL LFDSNYNPKA AYNAIANAL