ID   XYNA_SCHCO              Reviewed;         197 AA.
AC   P35809;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   25-MAY-2022, entry version 99.
DE   RecName: Full=Endo-1,4-beta-xylanase A;
DE            Short=Xylanase A;
DE            EC=3.2.1.8;
DE   AltName: Full=1,4-beta-D-xylan xylanohydrolase A;
GN   Name=XYNA;
OS   Schizophyllum commune (Split gill fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Schizophyllaceae; Schizophyllum.
OX   NCBI_TaxID=5334;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   STRAIN=ATCC 38548 / Delmar / 13 / IHEM 5263;
RA   Yaguchi M., Roy C., Ujiie M., Watson D.C., Wakarchuk W.;
RL   (In) Visser J., Beldman G., Kusters-van Someren M.A., Voragen A.G.J.
RL   (eds.);
RL   Xylans and xylanases, pp.149-154, Elsevier, Amsterdam (1992).
RN   [2]
RP   PROTEIN SEQUENCE, AND DISULFIDE BONDS.
RC   STRAIN=ATCC 38548 / Delmar / 13 / IHEM 5263;
RX   PubMed=8243636; DOI=10.1016/0014-5793(93)80698-t;
RA   Oku T., Roy C., Watson D.C., Wakarchuk W., Campbell R., Yaguchi M.,
RA   Jurasek L., Paice M.G.;
RT   "Amino acid sequence and thermostability of xylanase A from Schizophyllum
RT   commune.";
RL   FEBS Lett. 334:296-300(1993).
RN   [3]
RP   PARTIAL PROTEIN SEQUENCE, AND ACTIVE SITE GLU-87.
RC   STRAIN=ATCC 38548 / Delmar / 13 / IHEM 5263;
RX   PubMed=7906649; DOI=10.1111/j.1432-1033.1994.tb18563.x;
RA   Bray M.R., Clarke A.J.;
RT   "Identification of a glutamate residue at the active site of xylanase A
RT   from Schizophyllum commune.";
RL   Eur. J. Biochem. 219:821-827(1994).
CC   -!- FUNCTION: Hydrolyzes xylans into xylobiose and xylose.
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       pH dependence:
CC         Active over a very broad pH range.;
CC   -!- PATHWAY: Glycan degradation; xylan degradation.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 11 (cellulase G) family.
CC       {ECO:0000305}.
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DR   PIR; A44597; A44597.
DR   AlphaFoldDB; P35809; -.
DR   SMR; P35809; -.
DR   CAZy; GH11; Glycoside Hydrolase Family 11.
DR   CLAE; XYN11A_SCHCO; -.
DR   BRENDA; 3.2.1.8; 5611.
DR   UniPathway; UPA00114; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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   Carbohydrate metabolism; Direct protein sequencing; Disulfide bond;
KW   Glycosidase; Hydrolase; Polysaccharide degradation; Secreted;
KW   Xylan degradation.
FT   CHAIN           1..197
FT                   /note="Endo-1,4-beta-xylanase A"
FT                   /id="PRO_0000184071"
FT   DOMAIN          1..197
FT                   /note="GH11"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01097"
FT   ACT_SITE        87
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000305|PubMed:7906649"
FT   ACT_SITE        184
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10063"
FT   DISULFID        111..160
FT                   /evidence="ECO:0000269|PubMed:8243636"
SQ   SEQUENCE   197 AA;  20979 MW;  42C8074E67C1FBE9 CRC64;
     SGTPSSTGTD GGYYYSWWTD GAGDATYQNN GGGSYTLTWS GNNGNLVGGK GWNPGAASRS
     ISYSGTYQPN GNSYLSVYGW TRSSLIEYYI VESYGSYDPS SAASHKGSVT CNGATYDILS
     TWRYNAPSID GTQTFEQFWS VRNPKKAPGG SISGTVDVQC HFDAWKGLGM NLGSEHNYQI
     VATEGYQSSG TATITVT