ID   XYNA_PAEVA              Reviewed;         194 AA.
AC   P81536;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2000, sequence version 1.
DT   02-SEP-2026, entry version 92.
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;
DE   AltName: Full=PVX;
OS   Paecilomyces variotii (Byssochlamys spectabilis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Thermoascaceae; Paecilomyces.
OX   NCBI_TaxID=264951;
RN   [1]
RP   X-RAY CRYSTALLOGRAPHY (1.59 ANGSTROMS), PROTEIN SEQUENCE OF 50-58 AND
RP   123-128, AND ACETYLATION AT GLY-1.
RC   STRAIN=Bainier;
RX   PubMed=10623548; DOI=10.1006/jmbi.1999.3348;
RA   Kumar P.R., Eswaramoorthy S., Vithayathil P.J., Viswamitra M.A.;
RT   "The tertiary structure at 1.59 A resolution and the proposed amino acid
RT   sequence of a family-11 xylanase from the thermophilic fungus Paecilomyces
RT   varioti bainier.";
RL   J. Mol. Biol. 295:581-593(2000).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.;
CC         EC=3.2.1.8;
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Temperature dependence:
CC         Thermostable.;
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   PDB; 1PVX; X-ray; 1.59 A; A=1-194.
DR   AlphaFoldDB; P81536; -.
DR   MDposit; P81536; -.
DR   SMR; P81536; -.
DR   CAZy; GH11; Glycoside Hydrolase Family 11.
DR   iPTMnet; P81536; -.
DR   UniPathway; UPA00114; -.
DR   EvolutionaryTrace; P81536; -.
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   FunFam; 2.60.120.180:FF:000001; Endo-1,4-beta-xylanase; 1.
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   PANTHER; PTHR46828:SF3; ENDO-1,4-BETA-XYLANASE; 1.
DR   PANTHER; PTHR46828; ENDO-1,4-BETA-XYLANASE A-RELATED; 1.
DR   Pfam; PF00457; Glyco_hydro_11; 1.
DR   PRINTS; PR00911; GLHYDRLASE11.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   PROSITE; PS00776; GH11_1; 1.
DR   PROSITE; PS00777; GH11_2; 1.
DR   PROSITE; PS51761; GH11_3; 1.
DR   PDBsum; 1PVX; -.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Carbohydrate metabolism;
KW   Direct protein sequencing; Disulfide bond; Glycosidase; Hydrolase;
KW   Polysaccharide degradation; Xylan degradation.
FT   CHAIN           1..194
FT                   /note="Endo-1,4-beta-xylanase"
FT                   /id="PRO_0000184069"
FT   DOMAIN          1..191
FT                   /note="GH11"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01097"
FT   ACT_SITE        86
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10062"
FT   ACT_SITE        178
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10063"
FT   MOD_RES         1
FT                   /note="N-acetylglycine"
FT                   /evidence="ECO:0000269|PubMed:10623548"
FT   DISULFID        110..154
FT   HELIX           3..5
FT                   /evidence="ECO:0007829|PDB:1PVX"
FT   STRAND          6..10
FT                   /evidence="ECO:0007829|PDB:1PVX"
FT   STRAND          13..19
FT                   /evidence="ECO:0007829|PDB:1PVX"
FT   STRAND          25..29
FT                   /evidence="ECO:0007829|PDB:1PVX"
FT   STRAND          34..39
FT                   /evidence="ECO:0007829|PDB:1PVX"
FT   STRAND          41..53
FT                   /evidence="ECO:0007829|PDB:1PVX"
FT   STRAND          59..81
FT                   /evidence="ECO:0007829|PDB:1PVX"
FT   TURN            82..84
FT                   /evidence="ECO:0007829|PDB:1PVX"
FT   STRAND          85..96
FT                   /evidence="ECO:0007829|PDB:1PVX"
FT   TURN            98..101
FT                   /evidence="ECO:0007829|PDB:1PVX"
FT   STRAND          102..110
FT                   /evidence="ECO:0007829|PDB:1PVX"
FT   STRAND          113..127
FT                   /evidence="ECO:0007829|PDB:1PVX"
FT   STRAND          130..143
FT                   /evidence="ECO:0007829|PDB:1PVX"
FT   STRAND          146..151
FT                   /evidence="ECO:0007829|PDB:1PVX"
FT   HELIX           152..161
FT                   /evidence="ECO:0007829|PDB:1PVX"
FT   STRAND          168..182
FT                   /evidence="ECO:0007829|PDB:1PVX"
FT   STRAND          184..192
FT                   /evidence="ECO:0007829|PDB:1PVX"
SQ   SEQUENCE   194 AA;  20947 MW;  1D5C50AA4F6EDB90 CRC64;
     GTTPNSEGWH DGYYYSWWSD GGGDSTYTNN SGGTYEITWG NGGNLVGGKG WNPGLNARAI
     HFTGVYQPNG TSYLSVYGWT RNPLVEYYIV ENFGSSNPSS GSTDLGTVSC DGSTYTLGQS
     TRYNAPSIDG TQTFNQYWSV RQDKRSSGTV QTGCHFDAWA SAGLNVTGDH YYQIVATEGY
     FSSGYARITV ADVG
//