ID   XYNA_GLOTR              Reviewed;          45 AA.
AC   P84195;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   25-MAY-2022, entry version 34.
DE   RecName: Full=Endo-1,4-beta-xylanase Xyn10A;
DE            EC=3.2.1.4;
DE            EC=3.2.1.8;
DE   Flags: Fragments;
OS   Gloeophyllum trabeum (Brown rot fungus) (Agaricus trabeus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Gloeophyllales; Gloeophyllaceae; Gloeophyllum.
OX   NCBI_TaxID=104355;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RC   STRAIN=ATCC 11539 / Madison 617 {ECO:0000269|PubMed:15870328};
RX   PubMed=15870328; DOI=10.1128/aem.71.5.2412-2417.2005;
RA   Cohen R., Suzuki M.R., Hammel K.E.;
RT   "Processive endoglucanase active in crystalline cellulose hydrolysis by the
RT   brown rot basidiomycete Gloeophyllum trabeum.";
RL   Appl. Environ. Microbiol. 71:2412-2417(2005).
CC   -!- FUNCTION: Has xylanase, avicelase and cellobiohydrolase activity.
CC       {ECO:0000269|PubMed:15870328}.
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:15870328};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of (1->4)-beta-D-glucosidic linkages in
CC         cellulose, lichenin and cereal beta-D-glucans.; EC=3.2.1.4;
CC         Evidence={ECO:0000269|PubMed:15870328};
CC   -!- PATHWAY: Glycan degradation; xylan degradation.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space
CC       {ECO:0000269|PubMed:15870328}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F) family.
CC       {ECO:0000255}.
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DR   AlphaFoldDB; P84195; -.
DR   CAZy; GH10; Glycoside Hydrolase Family 10.
DR   UniPathway; UPA00114; -.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR   GO; GO:0008810; F:cellulase activity; IDA:UniProtKB.
DR   GO; GO:0031176; F:endo-1,4-beta-xylanase activity; IDA:UniProtKB.
DR   GO; GO:0030245; P:cellulose catabolic process; IDA:UniProtKB.
DR   GO; GO:0045493; P:xylan catabolic process; IDA:UniProtKB.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Cellulose degradation; Direct protein sequencing;
KW   Glycosidase; Hydrolase; Polysaccharide degradation; Secreted;
KW   Xylan degradation.
FT   CHAIN           <1..>45
FT                   /note="Endo-1,4-beta-xylanase Xyn10A"
FT                   /id="PRO_0000184066"
FT   NON_CONS        10..11
FT                   /evidence="ECO:0000303|PubMed:15870328"
FT   NON_CONS        22..23
FT                   /evidence="ECO:0000303|PubMed:15870328"
FT   NON_TER         1
FT                   /evidence="ECO:0000303|PubMed:15870328"
FT   NON_TER         45
FT                   /evidence="ECO:0000303|PubMed:15870328"
SQ   SEQUENCE   45 AA;  4771 MW;  8C14D9073D3D8A86 CRC64;
     LYMGTATDNG ATAMLNLVES LKYSWVPSTF SGQGAATPYD SNLVK