ID   XYN2_HUMGT              Reviewed;         227 AA.
AC   Q9HGE1;
DT   09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   25-MAY-2022, entry version 79.
DE   RecName: Full=Endo-1,4-beta-xylanase 2;
DE            Short=Xylanase 2;
DE            EC=3.2.1.8;
DE   AltName: Full=1,4-beta-D-xylan xylanohydrolase 2;
DE   Flags: Precursor;
GN   Name=xyn2;
OS   Humicola grisea var. thermoidea.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Chaetomiaceae; Trichocladium;
OC   Trichocladium griseum.
OX   NCBI_TaxID=5528;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=60849;
RA   Faria F.P., Pocas-Fonseca M.J., Azevedo M.O.;
RT   "Cloning of a xylanase-encoding gene from the thermophilic fungus Humicola
RT   grisea and its expression in Escherichia coli.";
RL   Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PROTEIN SEQUENCE OF 37-43, SUBCELLULAR LOCATION, FUNCTION, AND CATALYTIC
RP   ACTIVITY.
RX   PubMed=11849507; DOI=10.1046/j.1472-765x.2002.01057.x;
RA   de Faria F.P., Te'O V.S., Bergquist P.L., Azevedo M.O., Nevalainen K.M.;
RT   "Expression and processing of a major xylanase (XYN2) from the thermophilic
RT   fungus Humicola grisea var. thermoidea in Trichoderma reesei.";
RL   Lett. Appl. Microbiol. 34:119-123(2002).
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:11849507}.
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:11849507};
CC   -!- PATHWAY: Glycan degradation; xylan degradation.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11849507}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 11 (cellulase G) family.
CC       {ECO:0000305}.
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DR   EMBL; AF155594; AAG16891.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9HGE1; -.
DR   SMR; Q9HGE1; -.
DR   CAZy; GH11; Glycoside Hydrolase Family 11.
DR   CLAE; XYN11B_HUMGT; -.
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; Glycoprotein;
KW   Glycosidase; Hydrolase; Polysaccharide degradation; Secreted; Signal;
KW   Xylan degradation.
FT   SIGNAL          1..36
FT                   /evidence="ECO:0000269|PubMed:11849507"
FT   CHAIN           37..227
FT                   /note="Endo-1,4-beta-xylanase 2"
FT                   /id="PRO_0000429618"
FT   DOMAIN          37..225
FT                   /note="GH11"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01097"
FT   ACT_SITE        121
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10062"
FT   ACT_SITE        212
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10063"
FT   CARBOHYD        29
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   227 AA;  25615 MW;  991815AD84EB2939 CRC64;
     MVSIKSVLAA ATAVSSALAA PFDFVPRDNS TALQARQVTP NAEGWHNGYF YSWWSDGGGQ
     VQYTNLEGSR YQVRWRNTGN FVGGKGWNPG TGRTINYGGY FNPQGNGYLA VYGWTRNPLV
     EYYVIESYGT YNPGSQAQYK GTFYTDGDQY DIFVSTRYNQ PSIDGTRTFQ QYWSIRKNKR
     VGGSVNMQNH FNAWQQHGMP LGQHYYQIVA TEGYQSSGES DIYVQTH