ID   XYNA_PENCN              Reviewed;         327 AA.
AC   Q5S7A8;
DT   09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 58.
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=xylA;
OS   Penicillium canescens.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=5083;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, FUNCTION,
RP   CATALYTIC ACTIVITY, AND INDUCTION.
RC   STRAIN=F178;
RX   PubMed=12391748;
RA   Serebrianyi V.A., Vavilova E.A., Chulkin A.M., Vinetskii I.U.P.;
RT   "Cloning of an endo-1,4-beta-xylanase gene from Penicillium canescens and
RT   construction of multicopy strains.";
RL   Appl. Biochem. Microbiol. 38:495-501(2002).
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:12391748}.
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:12391748};
CC   -!- PATHWAY: Glycan degradation; xylan degradation.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12391748}.
CC   -!- INDUCTION: Nucleotide sequences for binding catabolite repression
CC       protein CREA were detected in the promoter region.
CC       {ECO:0000269|PubMed:12391748}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F) family.
CC       {ECO:0000305}.
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DR   EMBL; AY756109; AAV65488.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q5S7A8; -.
DR   SMR; Q5S7A8; -.
DR   CAZy; GH10; Glycoside Hydrolase Family 10.
DR   CLAE; XYN10A_PENCA; -.
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; Glycosidase; Hydrolase;
KW   Polysaccharide degradation; Secreted; Signal; Xylan degradation.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..327
FT                   /note="Endo-1,4-beta-xylanase A"
FT                   /id="PRO_0000429614"
FT   DOMAIN          46..326
FT                   /note="GH10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01096"
FT   ACT_SITE        157
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        263
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10061"
FT   DISULFID        281..287
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   327 AA;  35091 MW;  62C0BB32926005ED CRC64;
     MVQLKTAALA LLFAGQALSG PVDSRQASVS IDAKFKAHGK KYLGTIGDQY TLTKNTKNPA
     IIKADFGQLT PENSMKWDAT EPNRGQFTFS GSDYLVNFAQ SNGKLIRGHT LVWHSQLPGW
     VSSITDKNTL ISVLKNHITT VMTRYKGKIY AWDVLNEIFN EDGSLRNSVF YNVIGEDYVR
     IAFETARSVD PNAKLYINDY NLDSAGYSKV NGMVSHVKKW LAAGIPIDGI GSQTHLGAGA
     GSAVAGALNA LASAGTKEIA ITELDIAGAS STDYVNVVNA CLNQAKCVGI TVWGVADPDS
     WRSSSSPLLF DGNYNPKAAY NAIANAL