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Database: UniProt
Entry: A6YAP7
LinkDB: A6YAP7
Original site: A6YAP7 
ID   XYN1_LEUGO              Reviewed;         234 AA.
AC   A6YAP7;
DT   09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   05-DEC-2018, entry version 43.
DE   RecName: Full=Endo-1,4-beta-xylanase 1;
DE            Short=Xylanase 1;
DE            EC=3.2.1.8;
DE   AltName: Full=1,4-beta-D-xylan xylanohydrolase 1;
DE   Flags: Precursor;
GN   Name=Xyn1;
OS   Leucoagaricus gongylophorus (Leaf-cutting ant fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
OC   Agaricomycetes; Agaricomycetidae; Agaricales; Agaricaceae;
OC   Leucoagaricus.
OX   NCBI_TaxID=79220;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=18307762; DOI=10.1186/1471-2180-8-40;
RA   Schioett M., De Fine Licht H.H., Lange L., Boomsma J.J.;
RT   "Towards a molecular understanding of symbiont function:
RT   Identification of a fungal gene for the degradation of xylan in the
RT   fungus gardens of leaf-cutting ants.";
RL   BMC Microbiol. 8:40-40(2008).
CC   -!- FUNCTION: Endo-1,4-beta-xylanase involved in the hydrolysis of
CC       xylan, a major structural heterogeneous polysaccharide found in
CC       plant biomass representing the second most abundant polysaccharide
CC       in the biosphere, after cellulose. {ECO:0000269|PubMed:18307762}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in
CC         xylans.; EC=3.2.1.8; Evidence={ECO:0000269|PubMed:18307762};
CC   -!- PATHWAY: Glycan degradation; xylan degradation.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 11 (cellulase G)
CC       family. {ECO:0000305}.
DR   EMBL; EF208066; ABN81018.1; -; Genomic_DNA.
DR   ProteinModelPortal; A6YAP7; -.
DR   SMR; A6YAP7; -.
DR   CAZy; GH11; Glycoside Hydrolase Family 11.
DR   mycoCLAP; XYN11A_LEUGO; -.
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; Glycoprotein; Glycosidase; Hydrolase;
KW   Polysaccharide degradation; Secreted; Signal; Xylan degradation.
FT   SIGNAL        1     21       {ECO:0000255}.
FT   CHAIN        22    234       Endo-1,4-beta-xylanase 1.
FT                                /FTId=PRO_0000429619.
FT   DOMAIN       38    234       GH11. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01097}.
FT   COMPBIAS     67     70       Poly-Gly.
FT   ACT_SITE    124    124       Nucleophile. {ECO:0000255|PROSITE-
FT                                ProRule:PRU10062}.
FT   ACT_SITE    221    221       Proton donor. {ECO:0000255|PROSITE-
FT                                ProRule:PRU10063}.
FT   CARBOHYD     25     25       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD     75     75       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    167    167       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
SQ   SEQUENCE   234 AA;  25156 MW;  2782B00187A29EFD CRC64;
     MVSFIFTRII LFAAAINGAV ALPMNTTEPE DFSILSRSGT PSSTGYSNGY YYSWWTDGAA
     QATYANGGGG QYSLNWSGNN GNLVGGKGWN PGFNGRVIQY SGTYQPNGNS YLSVYGWTLN
     PLIEYYIVES YGSYNPSSAA ARKGSVNCDG ANYDILTTTR YNEPSINGTQ TFQQFWSVRN
     PKKNPGGSIS GSVSTGCHFT AWGNLGMNLG STWNYQIVAT EGYQSSGFSS ITVA
//
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