ID   XYN_PHACE               Reviewed;         217 AA.
AC   O97402; P81525;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   25-MAY-2022, entry version 79.
DE   RecName: Full=Endo-1,4-beta-xylanase;
DE            Short=Xylanase;
DE            EC=3.2.1.8;
DE   AltName: Full=1,4-beta-D-xylan xylanohydrolase;
DE   Flags: Precursor;
OS   Phaedon cochleariae (Mustard beetle).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC   Chrysomeloidea; Chrysomelidae; Chrysomelinae; Chrysomelini; Phaedon.
OX   NCBI_TaxID=80249;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:CAA76932.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC   TISSUE=Larval gut {ECO:0000269|PubMed:10612046};
RX   PubMed=10612046; DOI=10.1016/s0965-1748(99)00104-6;
RA   Girard C., Jouanin L.;
RT   "Molecular cloning of cDNAs encoding a range of digestive enzymes from a
RT   phytophagous beetle, Phaedon cochleariae.";
RL   Insect Biochem. Mol. Biol. 29:1129-1142(1999).
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       {ECO:0000250|UniProtKB:P36217}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed in larval carcasses and gut, and adult
CC       gut. {ECO:0000269|PubMed:10612046}.
CC   -!- DEVELOPMENTAL STAGE: Larvae and adult. {ECO:0000269|PubMed:10612046}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 11 (cellulase G) family.
CC       {ECO:0000255}.
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DR   EMBL; Y17908; CAA76932.1; -; mRNA.
DR   AlphaFoldDB; O97402; -.
DR   SMR; O97402; -.
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:0007586; P:digestion; IEA:UniProtKB-KW.
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; Digestion; Glycoprotein; Glycosidase; Hydrolase;
KW   Polysaccharide degradation; Secreted; Signal; Xylan degradation.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..217
FT                   /note="Endo-1,4-beta-xylanase"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_5000147330"
FT   DOMAIN          20..217
FT                   /note="GH11"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01097"
FT   ACT_SITE        107
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P36217,
FT                   ECO:0000255|PROSITE-ProRule:PRU10062"
FT   ACT_SITE        204
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P36217,
FT                   ECO:0000255|PROSITE-ProRule:PRU10063"
FT   CARBOHYD        56
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        80
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   217 AA;  23942 MW;  92185C41BF39A644 CRC64;
     MQFLIPVVIL CVSLVDSQKV LYNNEIGFNN GFYYAFWKDS GSATFTLESG GRYAGNWTTS
     TNNWVGGKGW NPGNSWRTVN YSGYYGINEY ANSYLSLYGW TTNPLIEYYV VESYGSYSPL
     NCPGGTDEGS FTSGGATYQV RKCRRTNAPS IIGTQSFDQY FSVRTPKKGF GQVSGSVNFA
     DHVQYWASKG LPLGTHAHQI FATEGYQSSG FADITVS