ID   XYN3_HYPJR              Reviewed;         347 AA.
AC   A0A024SIB3;
DT   06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT   09-JUL-2014, sequence version 1.
DT   25-MAY-2022, entry version 27.
DE   RecName: Full=Endo-1,4-beta-xylanase 3;
DE            Short=Xylanase 3;
DE            EC=3.2.1.8 {ECO:0000255|PROSITE-ProRule:PRU01096};
DE   AltName: Full=1,4-beta-D-xylan xylanohydrolase 3;
DE   Flags: Precursor;
GN   Name=xyn3; ORFNames=M419DRAFT_23616;
OS   Hypocrea jecorina (strain ATCC 56765 / BCRC 32924 / NRRL 11460 / Rut C-30)
OS   (Trichoderma reesei).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX   NCBI_TaxID=1344414;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 56765 / BCRC 32924 / NRRL 11460 / Rut C-30;
RX   DOI=10.1089/ind.2013.0015;
RA   Koike H., Aerts A., LaButti K., Grigoriev I.V., Baker S.E.;
RT   "Comparative genomics analysis of Trichoderma reesei strains.";
RL   Ind. Biotechnol. 9:352-367(2013).
CC   -!- FUNCTION: Glycoside hydrolase involved in the hydrolysis of xylan, a
CC       major plant cell wall hemicellulose made up of 1,4-beta-linked D-
CC       xylopyranose residues. Catalyzes the endohydrolysis of the main-chain
CC       1,4-beta-glycosidic bonds connecting the xylose subunits yielding
CC       various xylooligosaccharides and xylose. Produces xylobiose and
CC       xylotriose as the main degradation products.
CC       {ECO:0000250|UniProtKB:Q9P973}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.;
CC         EC=3.2.1.8; Evidence={ECO:0000250|UniProtKB:Q9P973};
CC   -!- PATHWAY: Glycan degradation; xylan degradation. {ECO:0000255|PROSITE-
CC       ProRule:PRU01096}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q9P973}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q9P973}.
CC   -!- PTM: Not glycosylated. {ECO:0000250|UniProtKB:Q9P973}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F) family.
CC       {ECO:0000255|PROSITE-ProRule:PRU01096}.
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DR   EMBL; KI911140; ETS05245.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A024SIB3; -.
DR   SMR; A0A024SIB3; -.
DR   EnsemblFungi; ETS05245; ETS05245; M419DRAFT_23616.
DR   KEGG; trr:M419DRAFT_23616; -.
DR   HOGENOM; CLU_020161_2_0_1; -.
DR   OrthoDB; 829814at2759; -.
DR   UniPathway; UPA00114; -.
DR   Proteomes; UP000024376; Unassembled WGS sequence.
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   3: Inferred from homology;
KW   Carbohydrate metabolism; Disulfide bond; Glycosidase; Hydrolase;
KW   Polysaccharide degradation; Pyrrolidone carboxylic acid; Secreted; Signal;
KW   Xylan degradation.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   PROPEP          17..45
FT                   /evidence="ECO:0000250|UniProtKB:Q9P973"
FT                   /id="PRO_0000436706"
FT   CHAIN           46..347
FT                   /note="Endo-1,4-beta-xylanase 3"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_5001537149"
FT   DOMAIN          46..345
FT                   /note="GH10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01096"
FT   ACT_SITE        176
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01096"
FT   ACT_SITE        282
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01096"
FT   MOD_RES         46
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000250|UniProtKB:Q9P973"
FT   DISULFID        300..306
FT                   /evidence="ECO:0000250|UniProtKB:G0RA32"
SQ   SEQUENCE   347 AA;  38076 MW;  1AD305498D0216CF CRC64;
     MKANVILCLL APLVAALPTE TIHLDPELAA LRANLTERTA DLWDRQASQS IDQLIKRKGK
     LYFGTATDRG LLQREKNAAI IQADLGQVTP ENSMKWQSLE NNQGQLNWGD ADYLVNFAQQ
     NGKSIRGHTL IWHSQLPAWV NNINNADTLR QVIRTHVSTV VGRYKGKIRA WDVVNEIFNE
     DGTLRSSVFS RLLGEEFVSI AFRAARDADP SARLYINDYN LDRANYGKVN GLKTYVSKWI
     SQGVPIDGIG SQSHLSGGGG SGTLGALQQL ATVPVTELAI TELDIQGAPT TDYTQVVQAC
     LSVSKCVGIT VWGISDKDSW RASTNPLLFD ANFNPKPAYN SIVGILQ