XY11A_BOTFU
ID XY11A_BOTFU Reviewed; 227 AA.
AC Q2LMP0;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2006, sequence version 1.
DT 25-MAY-2022, entry version 61.
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;
OS Botryotinia fuckeliana (Noble rot fungus) (Botrytis cinerea).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Botrytis.
OX NCBI_TaxID=40559;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION, FUNCTION, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=SAS56;
RX PubMed=16404950; DOI=10.1094/mpmi-19-0025;
RA Brito N., Espino J.J., Gonzalez C.;
RT "The endo-beta-1,4-xylanase xyn11A is required for virulence in Botrytis
RT cinerea.";
RL Mol. Plant Microbe Interact. 19:25-32(2006).
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:16404950}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.;
CC EC=3.2.1.8;
CC -!- PATHWAY: Glycan degradation; xylan degradation.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- INDUCTION: Expression is maximal when xylan is the only carbon source,
CC and repressed by glucose. Expression is detected from the beginning of
CC tomato leaves infection in the just-inoculated leaves, and the level
CC sof transcript increased between 24 and 48 hours postinfection
CC simultaneously with the appearance of visible lesions on the leaves.
CC {ECO:0000269|PubMed:16404950}.
CC -!- DISRUPTION PHENOTYPE: Leads to reduced ability to infect tomato leaves
CC or grape berries. {ECO:0000269|PubMed:16404950}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 11 (cellulase G) family.
CC {ECO:0000305}.
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DR EMBL; DQ057980; AAZ03776.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2LMP0; -.
DR SMR; Q2LMP0; -.
DR CAZy; GH11; Glycoside Hydrolase Family 11.
DR CLAE; XYN11A_BOTFU; -.
DR BRENDA; 3.2.1.8; 918.
DR UniPathway; UPA00114; -.
DR PHI-base; PHI:546; -.
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 2: Evidence at transcript level;
KW Carbohydrate metabolism; Glycosidase; Hydrolase;
KW Polysaccharide degradation; Secreted; Signal; Virulence; Xylan degradation.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..227
FT /note="Endo-1,4-beta-xylanase 11A"
FT /id="PRO_5000140289"
FT DOMAIN 37..227
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:0000255|PROSITE-ProRule:PRU10063"
SQ SEQUENCE 227 AA; 23824 MW; F4969A37C3A9B887 CRC64;
MVSASSLLLA ASAIAGVFSA PAAAPVSENL NVLQERALTS SATGTSGGYY YSFWTDGSGG
VTYSNGANGQ YAVSWTGNKG NFVGGKGWAV GSERSISYTG SYKPNGNSYL SVYGWTTSPL
IEYYIVEDFG TYDPSSAATE IGSVTSDGST YKILETTRTN QPSVQGTATF KQYWSVRTSK
RTSGTVTTAN HFAAWKKLGL TLGSTYNYQI VAVEGYQSSG SASITVS