ID   XYN2_TRIHA              Reviewed;         221 AA.
AC   B5A7N4;
DT   09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   25-MAY-2022, entry version 38.
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=Xyn2;
OS   Trichoderma harzianum (Hypocrea lixii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX   NCBI_TaxID=5544;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, FUNCTION, CATALYTIC
RP   ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=C4;
RX   PubMed=19734721;
RA   Lee J.M., Shin J.W., Nam J.K., Choi J.Y., Jeong C.S., Han I.S., Nam S.W.,
RA   Choi Y.J., Chung D.K.;
RT   "Molecular cloning and expression of the trichoderma harzianum C4 endo-
RT   beta-1,4-Xylanase Gene in Saccharomyces cerevisiae.";
RL   J. Microbiol. Biotechnol. 19:823-828(2009).
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:19734721}.
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:19734721};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 5.1. {ECO:0000269|PubMed:19734721};
CC       Temperature dependence:
CC         Optimum temperature is 50 degrees Celsius.
CC         {ECO:0000269|PubMed:19734721};
CC   -!- PATHWAY: Glycan degradation; xylan degradation.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19734721}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 11 (cellulase G) family.
CC       {ECO:0000305}.
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DR   EMBL; EU821597; ACF40831.1; -; mRNA.
DR   AlphaFoldDB; B5A7N4; -.
DR   SMR; B5A7N4; -.
DR   CAZy; GH11; Glycoside Hydrolase Family 11.
DR   CLAE; XYN11B_TRIHA; -.
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; IPR033119; GH11_AS_2.
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; PS00777; GH11_2; 1.
DR   PROSITE; PS51761; GH11_3; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Glycoprotein; Glycosidase; Hydrolase;
KW   Polysaccharide degradation; Secreted; Signal; Xylan degradation.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..221
FT                   /note="Endo-1,4-beta-xylanase 2"
FT                   /id="PRO_0000429668"
FT   DOMAIN          32..221
FT                   /note="GH11"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01097"
FT   ACT_SITE        117
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10062"
FT   ACT_SITE        208
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10063"
FT   CARBOHYD        69
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        92
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   221 AA;  23824 MW;  D3C3EE4A9FBA0FB2 CRC64;
     MVAFTSLLAG FAAIAGVLSA PTESSVEVEK RQTIGPGTGY SNGYYYSYWN DGHAGVTYTN
     GGGGSFTVNW SNSGNFVGGK GWQPGTKNKV INFSGSYNPN GNSYLSIYGW SRNPLIEYYI
     VENFGTYNPS TGATKLGEVT SDGSVYDIYR TQRVNQPSII GTATFYQYWS VRRNHRSSGS
     VNTANHFNAW ASHGLTLGTM DYQIVAVEGY FSSGSASITV S