ID   XYNG_VERDA              Reviewed;         250 AA.
AC   Q0ZHI9;
DT   09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   25-MAY-2022, entry version 57.
DE   RecName: Full=Endo-1,4-beta-xylanase G;
DE            Short=Xylanase G;
DE            EC=3.2.1.8;
DE   AltName: Full=1,4-beta-D-xylan xylanohydrolase G;
DE   Flags: Precursor;
GN   Name=xynG;
OS   Verticillium dahliae (Verticillium wilt).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX   NCBI_TaxID=27337;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, FUNCTION,
RP   CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=18720841;
RA   Zhang G., Rao B., Ye J., Ma L., Zhang X.;
RT   "Molecular cloning and heterologous expression of a new xylanase gene from
RT   Verticillium dahliae.";
RL   Wei Sheng Wu Xue Bao 48:765-771(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. The most favorable substrate is beechwood xylan.
CC       {ECO:0000269|PubMed:18720841}.
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:18720841};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 6.0. {ECO:0000269|PubMed:18720841};
CC       Temperature dependence:
CC         Optimum temperature is 45 degrees Celsius.
CC         {ECO:0000269|PubMed:18720841};
CC   -!- PATHWAY: Glycan degradation; xylan degradation.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18720841}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 11 (cellulase G) family.
CC       {ECO:0000305}.
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DR   EMBL; DQ449069; ABE02800.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q0ZHI9; -.
DR   SMR; Q0ZHI9; -.
DR   CAZy; GH11; Glycoside Hydrolase Family 11.
DR   CLAE; XYN11G_VERDA; -.
DR   HOGENOM; CLU_052631_0_0_1; -.
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..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..250
FT                   /note="Endo-1,4-beta-xylanase G"
FT                   /id="PRO_0000429616"
FT   DOMAIN          43..231
FT                   /note="GH11"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01097"
FT   ACT_SITE        127
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10062"
FT   ACT_SITE        218
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10063"
FT   CARBOHYD        31
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   250 AA;  27410 MW;  E9AEDE784AE4D995 CRC64;
     MVSFKSLLLA ASAFTAVLGR PFDSFDGPDV NITDADELLV RRQVTANSEG THNGYFYSWW
     SDGGGQVTYT MGAGSRYSVT WKDTGNFVGG KGWNPGTGRT INYGGSFSPQ GNGYLAVYGW
     TRNPLIEYYV VESYGTYNPG SGGQLKGTVT TDGGTYNVYV STRTNQPSID GTRTFQQYWS
     VRTSKRVGGA VTMQNHFNAW AQFGMNLGAH YYQIVATEGY QSSGPSDIYV QTQCKSLCDR
     GRVTWRDVVC