GenomeNet

Database: UniProt
Entry: P81536
LinkDB: P81536
Original site: P81536 
ID   XYNA_BYSSP              Reviewed;         194 AA.
AC   P81536;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2000, sequence version 1.
DT   05-DEC-2018, entry version 79.
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   Byssochlamys spectabilis (Paecilomyces variotii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Thermoascaceae; Byssochlamys.
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
RT   acid sequence of a family-11 xylanase from the thermophilic fungus
RT   Paecilomyces varioti bainier.";
RL   J. Mol. Biol. 295:581-593(2000).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in
CC         xylans.; 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)
CC       family. {ECO:0000305}.
DR   PDB; 1PVX; X-ray; 1.59 A; A=1-194.
DR   PDBsum; 1PVX; -.
DR   ProteinModelPortal; P81536; -.
DR   SMR; P81536; -.
DR   CAZy; GH11; Glycoside Hydrolase Family 11.
DR   mycoCLAP; XYN11A_BYSSP; -.
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   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; Acetylation; Carbohydrate metabolism;
KW   Direct protein sequencing; Disulfide bond; Glycosidase; Hydrolase;
KW   Polysaccharide degradation; Xylan degradation.
FT   CHAIN         1    194       Endo-1,4-beta-xylanase.
FT                                /FTId=PRO_0000184069.
FT   DOMAIN        1    191       GH11. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01097}.
FT   ACT_SITE     86     86       Nucleophile. {ECO:0000255|PROSITE-
FT                                ProRule:PRU10062}.
FT   ACT_SITE    178    178       Proton donor. {ECO:0000255|PROSITE-
FT                                ProRule:PRU10063}.
FT   MOD_RES       1      1       N-acetylglycine.
FT                                {ECO:0000269|PubMed:10623548}.
FT   DISULFID    110    154
FT   STRAND        6     10       {ECO:0000244|PDB:1PVX}.
FT   STRAND       13     19       {ECO:0000244|PDB:1PVX}.
FT   STRAND       25     29       {ECO:0000244|PDB:1PVX}.
FT   STRAND       34     39       {ECO:0000244|PDB:1PVX}.
FT   STRAND       41     53       {ECO:0000244|PDB:1PVX}.
FT   STRAND       59     81       {ECO:0000244|PDB:1PVX}.
FT   TURN         82     84       {ECO:0000244|PDB:1PVX}.
FT   STRAND       85     96       {ECO:0000244|PDB:1PVX}.
FT   TURN         98    101       {ECO:0000244|PDB:1PVX}.
FT   STRAND      102    110       {ECO:0000244|PDB:1PVX}.
FT   STRAND      113    127       {ECO:0000244|PDB:1PVX}.
FT   STRAND      130    143       {ECO:0000244|PDB:1PVX}.
FT   STRAND      146    151       {ECO:0000244|PDB:1PVX}.
FT   HELIX       152    161       {ECO:0000244|PDB:1PVX}.
FT   STRAND      168    182       {ECO:0000244|PDB:1PVX}.
FT   STRAND      184    192       {ECO:0000244|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
//
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