XYN_TRIHA
ID XYN_TRIHA Reviewed; 190 AA.
AC P48793;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 25-MAY-2022, entry version 90.
DE RecName: Full=Endo-1,4-beta-xylanase;
DE Short=Xylanase;
DE EC=3.2.1.8;
DE AltName: Full=1,4-beta-D-xylan xylanohydrolase;
OS Trichoderma harzianum (Hypocrea lixii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=5544;
RN [1]
RP PROTEIN SEQUENCE.
RC STRAIN=E58;
RA Yaguchi M., Roy C., Watson D.C., Rollin F., Tan L.U.L., Senior D.J.,
RA Saddler J.N.;
RT "The amino acid sequence of the 20 Kd xylanase from Trichoderma harzianum
RT E58.";
RL (In) Visser J., Beldman G., Kusters-van Someren M.A., Voragen A.G.J.
RL (eds.);
RL Xylans and xylanases, pp.435-438, Elsevier, Amsterdam (1992).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RA Campbell R.L., Rose D.R., Wakarchuk W.W., To R.J., Sung W., Yaguchi M.;
RT "High-resolution structures of xylanases from B.circulans and T.harzianum
RT identify a new folding pattern and implications for the atomic basis of the
RT catalysis.";
RL (In) Suominen P., Reinikainen T. (eds.);
RL Trichoderma reesei cellulases and other hydrolases, pp.63-72, Foundation
RL for Biotechnical and Industrial Fermentation Research, Helsinki (1993).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.;
CC EC=3.2.1.8;
CC -!- PATHWAY: Glycan degradation; xylan degradation.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 11 (cellulase G) family.
CC {ECO:0000305}.
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DR PIR; A44593; A44593.
DR PDB; 1XND; X-ray; 2.00 A; A=1-190.
DR PDBsum; 1XND; -.
DR AlphaFoldDB; P48793; -.
DR SMR; P48793; -.
DR CAZy; GH11; Glycoside Hydrolase Family 11.
DR CLAE; XYN11A_TRIHA; -.
DR UniPathway; UPA00114; -.
DR EvolutionaryTrace; P48793; -.
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 3D-structure; Carbohydrate metabolism; Direct protein sequencing;
KW Glycosidase; Hydrolase; Polysaccharide degradation; Xylan degradation.
FT CHAIN 1..190
FT /note="Endo-1,4-beta-xylanase"
FT /id="PRO_0000184072"
FT DOMAIN 1..190
FT /note="GH11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01097"
FT ACT_SITE 86
FT /note="Nucleophile"
FT ACT_SITE 177
FT /note="Proton donor"
FT STRAND 5..12
FT /evidence="ECO:0007829|PDB:1XND"
FT STRAND 14..19
FT /evidence="ECO:0007829|PDB:1XND"
FT STRAND 25..29
FT /evidence="ECO:0007829|PDB:1XND"
FT STRAND 34..41
FT /evidence="ECO:0007829|PDB:1XND"
FT STRAND 44..53
FT /evidence="ECO:0007829|PDB:1XND"
FT STRAND 59..81
FT /evidence="ECO:0007829|PDB:1XND"
FT TURN 82..84
FT /evidence="ECO:0007829|PDB:1XND"
FT STRAND 85..93
FT /evidence="ECO:0007829|PDB:1XND"
FT TURN 98..101
FT /evidence="ECO:0007829|PDB:1XND"
FT STRAND 103..110
FT /evidence="ECO:0007829|PDB:1XND"
FT STRAND 113..125
FT /evidence="ECO:0007829|PDB:1XND"
FT STRAND 130..143
FT /evidence="ECO:0007829|PDB:1XND"
FT STRAND 146..151
FT /evidence="ECO:0007829|PDB:1XND"
FT HELIX 152..161
FT /evidence="ECO:0007829|PDB:1XND"
FT STRAND 168..180
FT /evidence="ECO:0007829|PDB:1XND"
FT STRAND 182..189
FT /evidence="ECO:0007829|PDB:1XND"
SQ SEQUENCE 190 AA; 20703 MW; 6A0F4D1C3599C698 CRC64;
QTIGPGTGYS NGYYYSYWND GHAGVTYTNG GGGSFTVNWS NSGNFVAGKG WQPGTKNKVI
NFSGSYNPNG NSYLSIYGWS RNPLIEYYIV ENFGTYNPST GATKLGEVTS DGSVYDIYRT
QRVNQPSIIG TATFYQYWSV RRNHRSSGSV NTANHFNAWA SHGLTLGTMD YQIVAVEGYF
SSGSASITVS