ID   XY11A_BOTFB             Reviewed;         226 AA.
AC   B3VSG7;
DT   09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   25-MAY-2022, entry version 35.
DE   RecName: Full=Endo-1,4-beta-xylanase 11A;
DE            Short=Xylanase 11A;
DE            EC=3.2.1.8;
DE   AltName: Full=1,4-beta-D-xylan xylanohydrolase 11A;
DE   Flags: Precursor;
GN   Name=xyn11A; Synonyms=xynB;
OS   Botryotinia fuckeliana (strain B05.10) (Noble rot fungus) (Botrytis
OS   cinerea).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Sclerotiniaceae; Botrytis.
OX   NCBI_TaxID=332648;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 37-43, SUBCELLULAR
RP   LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, INDUCTION, FUNCTION,
RP   CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY REGULATION.
RX   PubMed=16185656; DOI=10.1016/j.bbrc.2005.09.030;
RA   Brutus A., Reca I.B., Herga S., Mattei B., Puigserver A., Chaix J.C.,
RA   Juge N., Bellincampi D., Giardina T.;
RT   "A family 11 xylanase from the pathogen Botrytis cinerea is inhibited by
RT   plant endoxylanase inhibitors XIP-I and TAXI-I.";
RL   Biochem. Biophys. Res. Commun. 337:160-166(2005).
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. Required for planr infection and the appearance of
CC       secondary lesions. {ECO:0000269|PubMed:16185656}.
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:16185656};
CC   -!- ACTIVITY REGULATION: Significantly inhibited by the wheat xylanase
CC       inhibiting protein I (XIP-I) and the proteinaceous endoxylanase
CC       Triticum aestivum xylanase inhibitors I (TAXI-I), whereas no inhibition
CC       is detected with TAXI-II. {ECO:0000269|PubMed:16185656}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=10 mg/ml for low viscosity xylan {ECO:0000269|PubMed:16185656};
CC         Vmax=0.5 umol/min/mg enzyme toward xylose
CC         {ECO:0000269|PubMed:16185656};
CC       pH dependence:
CC         Optimum pH is 4.5-5.0. {ECO:0000269|PubMed:16185656};
CC       Temperature dependence:
CC         Optimum temperature is between 38 and 42 degrees Celsius.
CC         {ECO:0000269|PubMed:16185656};
CC   -!- PATHWAY: Glycan degradation; xylan degradation.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16185656}.
CC   -!- INDUCTION: Shows constitutive expression during the early stage of
CC       tobacco leaves infection. {ECO:0000269|PubMed:16185656}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 11 (cellulase G) family.
CC       {ECO:0000305}.
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DR   EMBL; EU798759; ACF16413.1; -; mRNA.
DR   AlphaFoldDB; B3VSG7; -.
DR   SMR; B3VSG7; -.
DR   CAZy; GH11; Glycoside Hydrolase Family 11.
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; 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; PS51761; GH11_3; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Direct protein sequencing; Glycosidase; Hydrolase;
KW   Polysaccharide degradation; Secreted; Signal; Xylan degradation.
FT   SIGNAL          1..36
FT                   /evidence="ECO:0000255"
FT   CHAIN           37..226
FT                   /note="Endo-1,4-beta-xylanase 11A"
FT                   /id="PRO_0000429752"
FT   DOMAIN          37..226
FT                   /note="GH11"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01097"
FT   ACT_SITE        122
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10062"
FT   ACT_SITE        214
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   226 AA;  23856 MW;  A7DDE861EDB6E252 CRC64;
     MVSASSLLLA ASAIAGVFSA PAAAPVSENL NVLQERALTS SATGTSGGYY YSFWTDGSGG
     VTYSNGDNGQ YAVSWTGNKG NFVGGKGWAV GSERSISYTG SYKPNGNSYL SVYGWTTFPL
     IEYYIVEDFG TYDPSSAATE IGSVTSDGST YKILETTRTN QPSIQGTATF KQYWSVRTSK
     RTSGTVTTAN HFAAWKKLGL TLGSTYDYQI VAVEGYQSGS ASITVS