ID   XYNA_DICTH              Reviewed;         352 AA.
AC   Q12603;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   28-JUN-2023, entry version 81.
DE   RecName: Full=Beta-1,4-xylanase;
DE            EC=3.2.1.8;
DE   AltName: Full=1,4-beta-D-xylan xylanohydrolase;
DE   AltName: Full=Endo-1,4-beta-xylanase;
DE   Flags: Precursor;
GN   Name=xynA;
OS   Dictyoglomus thermophilum.
OC   Bacteria; Dictyoglomota; Dictyoglomia; Dictyoglomales; Dictyoglomaceae;
OC   Dictyoglomus.
OX   NCBI_TaxID=14;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Rt46 B.1;
RX   PubMed=8534104; DOI=10.1128/aem.61.12.4403-4408.1995;
RA   Gibbs M.D., Reeves R.A., Bergquist P.L.;
RT   "Cloning, sequencing, and expression of a xylanase gene from the extreme
RT   thermophile Dictyoglomus thermophilum Rt46B.1 and activity of the enzyme on
RT   fiber-bound substrate.";
RL   Appl. Environ. Microbiol. 61:4403-4408(1995).
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 {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F) family.
CC       {ECO:0000305}.
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DR   EMBL; L39866; AAA96979.1; -; Genomic_DNA.
DR   PIR; T08469; T08469.
DR   AlphaFoldDB; Q12603; -.
DR   SMR; Q12603; -.
DR   CAZy; GH10; Glycoside Hydrolase Family 10.
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; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR044846; GH10.
DR   InterPro; IPR001000; GH10_dom.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR31490:SF88; BETA-XYLANASE; 1.
DR   PANTHER; PTHR31490; GLYCOSYL HYDROLASE; 1.
DR   Pfam; PF00331; Glyco_hydro_10; 1.
DR   PRINTS; PR00134; GLHYDRLASE10.
DR   SMART; SM00633; Glyco_10; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   PROSITE; PS51760; GH10_2; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Glycosidase; Hydrolase;
KW   Polysaccharide degradation; Secreted; Signal; Xylan degradation.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..352
FT                   /note="Beta-1,4-xylanase"
FT                   /id="PRO_0000184065"
FT   DOMAIN          29..352
FT                   /note="GH10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01096"
FT   ACT_SITE        155
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        262
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   352 AA;  41486 MW;  393F702B5B8AA9AB CRC64;
     MINQRFSILV LLLILLTFSL GFLKEEAKGM EIPSLKEVYK DYFTIGAAVS HLNIYHYENL
     LKKHFNSLTP ENQMKWEVIH PKPYVYDFGP ADEIVDFAMK NGMKVRGHTL VWHNQTPGWV
     YAGTKDEILA RLKEHIKEVV GHYKGKVYAW DVVNEALSDN PNEFLRRAPW YDICGEEVIE
     KAFIWAHEVD PDAKLFYNDY NLEDPIKREK AYKLVKKLKD KGVPIHGIGI QGHWTLAWPT
     PKMLEDSIKR FAELGVEVQV TEFDISIYYD RNENNNFKVP PEDRLERQAQ LYKEAFEILR
     KYKGIVTGVT FWGVADDYTW LYFWPVRGRE DYPLLFDKNH NPKKAFWEIV KF
//