ID   XYS20_NEOPA             Reviewed;         335 AA.
AC   A8TGA1;
DT   09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   25-MAY-2022, entry version 48.
DE   RecName: Full=Endo-1,4-beta-xylanase S20;
DE            Short=Xylanase S20;
DE            EC=3.2.1.8;
DE   AltName: Full=1,4-beta-D-xylan xylanohydrolase S20;
DE   Flags: Precursor;
GN   Name=xynS20;
OS   Neocallimastix patriciarum (Rumen fungus).
OC   Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC   Chytridiomycota incertae sedis; Neocallimastigomycetes; Neocallimastigales;
OC   Neocallimastigaceae; Neocallimastix.
OX   NCBI_TaxID=4758;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, FUNCTION, CATALYTIC
RP   ACTIVITY, AND BIOPHISICOCHEMICAL PROPERTIES.
RC   STRAIN=S20;
RX   PubMed=18415096; DOI=10.1007/s00253-008-1418-1;
RA   Liu J.R., Duan C.H., Zhao X., Tzen J.T., Cheng K.J., Pai C.K.;
RT   "Cloning of a rumen fungal xylanase gene and purification of the
RT   recombinant enzyme via artificial oil bodies.";
RL   Appl. Microbiol. Biotechnol. 79:225-233(2008).
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:18415096}.
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:18415096};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=4.9 mg/ml for oat spelt xylan;
CC         Vmax=3.886 umol/min/mg enzyme toward oat spelt xylan;
CC       pH dependence:
CC         Optimum pH is 6.0.;
CC       Temperature dependence:
CC         Optimum temperature is 45 degrees Celsius.;
CC   -!- PATHWAY: Glycan degradation; xylan degradation.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18415096}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 11 (cellulase G) family.
CC       {ECO:0000305}.
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DR   EMBL; EU030626; ABW04217.1; -; mRNA.
DR   AlphaFoldDB; A8TGA1; -.
DR   SMR; A8TGA1; -.
DR   CAZy; CBM1; Carbohydrate-Binding Module Family 1.
DR   CAZy; GH11; Glycoside Hydrolase Family 11.
DR   CLAE; XYN11B_NEOPA; -.
DR   BRENDA; 3.2.1.8; 6834.
DR   UniPathway; UPA00114; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0030248; F:cellulose binding; IEA:InterPro.
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; IPR035971; CBD_sf.
DR   InterPro; IPR000254; Cellulose-bd_dom_fun.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR013319; GH11/12.
DR   InterPro; IPR018208; GH11_AS_1.
DR   InterPro; IPR033123; GH11_dom.
DR   InterPro; IPR001137; Glyco_hydro_11.
DR   Pfam; PF00734; CBM_1; 1.
DR   Pfam; PF00457; Glyco_hydro_11; 1.
DR   PRINTS; PR00911; GLHYDRLASE11.
DR   SMART; SM00236; fCBD; 1.
DR   SUPFAM; SSF49899; SSF49899; 1.
DR   SUPFAM; SSF57180; SSF57180; 1.
DR   PROSITE; PS00562; CBM1_1; 1.
DR   PROSITE; PS51164; CBM1_2; 1.
DR   PROSITE; PS00776; GH11_1; 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..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..335
FT                   /note="Endo-1,4-beta-xylanase S20"
FT                   /id="PRO_0000429664"
FT   DOMAIN          39..241
FT                   /note="GH11"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01097"
FT   DOMAIN          300..335
FT                   /note="CBM1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00597"
FT   REGION          251..291
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        134
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10062"
FT   ACT_SITE        228
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        42
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        78
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        202
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        251
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   335 AA;  36094 MW;  5F2B450DA1CA8D34 CRC64;
     MLRKLVTGAL AAALLLSGQS NAQNACQQTQ QLSGGRTINN KNETGNGNGN YKYEIWRDGN
     GGSLTLYPKD AAFKASWNNS GDFLGRVGLT FNKPAATNLG GDLIANYNYK KSGSDGGTYS
     YIGIYGWMDN PQIEYYVVDD WMHNRGAPGG SYMGSQKGTI TVDGGTYKVW SGQRTGASKW
     GTSTFTQIFS IRTSPRQCGS INVSEHFRQW QKLGLRLGGL MEAQLLAESG GGSGYVDFTY
     ATITIGGSSS NASAPSNNNN NNNNNNDNNG NWNNWNNNNN NNNNNNNNNN NNNNNQGGGN
     CAAIWGQCGG SGYNGPKCCK QGSCKQINQW YSQCQ