XYNA_BYSSP
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 25-MAY-2022, entry version 86.
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; 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 PDBsum; 1PVX; -.
DR AlphaFoldDB; P81536; -.
DR SMR; P81536; -.
DR CAZy; GH11; Glycoside Hydrolase Family 11.
DR CLAE; 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
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 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