ID   B8E346_DICTD            Unreviewed;       323 AA.
AC   B8E346;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 67.
DE   RecName: Full=Beta-xylanase {ECO:0000256|RuleBase:RU361174};
DE            EC=3.2.1.8 {ECO:0000256|RuleBase:RU361174};
GN   OrderedLocusNames=Dtur_1647 {ECO:0000313|EMBL:ACK42920.1};
OS   Dictyoglomus turgidum (strain DSM 6724 / Z-1310).
OC   Bacteria; Dictyoglomota; Dictyoglomia; Dictyoglomales; Dictyoglomaceae;
OC   Dictyoglomus.
OX   NCBI_TaxID=515635 {ECO:0000313|EMBL:ACK42920.1, ECO:0000313|Proteomes:UP000007719};
RN   [1] {ECO:0000313|Proteomes:UP000007719}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 6724 / Z-1310 {ECO:0000313|Proteomes:UP000007719};
RX   PubMed=28066333; DOI=10.3389/fmicb.2016.01979;
RA   Brumm P.J., Gowda K., Robb F.T., Mead D.A.;
RT   "The complete genome sequence of hyperthermophile Dictyoglomus turgidum DSM
RT   6724 reveals a specialized carbohydrate fermentor.";
RL   Front. Microbiol. 7:1979-1979(2016).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.;
CC         EC=3.2.1.8; Evidence={ECO:0000256|RuleBase:RU361174};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F) family.
CC       {ECO:0000256|RuleBase:RU361174}.
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DR   EMBL; CP001251; ACK42920.1; -; Genomic_DNA.
DR   RefSeq; WP_012583995.1; NC_011661.1.
DR   RefSeq; YP_002353534.1; NC_011661.1.
DR   AlphaFoldDB; B8E346; -.
DR   SMR; B8E346; -.
DR   STRING; 515635.Dtur_1647; -.
DR   CAZy; GH10; Glycoside Hydrolase Family 10.
DR   EnsemblBacteria; ACK42920; ACK42920; Dtur_1647.
DR   KEGG; dtu:Dtur_1647; -.
DR   PATRIC; fig|515635.4.peg.1696; -.
DR   eggNOG; COG3693; Bacteria.
DR   HOGENOM; CLU_020161_6_1_0; -.
DR   InParanoid; B8E346; -.
DR   OrthoDB; 9809277at2; -.
DR   Proteomes; UP000007719; Chromosome.
DR   GO; GO:0031176; F:endo-1,4-beta-xylanase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
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 {ECO:0000256|ARBA:ARBA00023277,
KW   ECO:0000256|RuleBase:RU361174};
KW   Glycosidase {ECO:0000256|RuleBase:RU361174, ECO:0000313|EMBL:ACK42920.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361174};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326,
KW   ECO:0000256|RuleBase:RU361174};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007719}.
FT   DOMAIN          1..323
FT                   /note="GH10"
FT                   /evidence="ECO:0000259|PROSITE:PS51760"
SQ   SEQUENCE   323 AA;  38154 MW;  F86DF6BC936A8DDD CRC64;
     MEIPSLKEVY KDYFPIGAAV SHLNIYTYED LLKKHFNSLT PENQMKWEVI HPKPYVYDFG
     PADEIVDFAM KNGMKVRGHT LVWHNQTPGW VYAGTKDEIL ARLKEHIYEV VGHYKGKVYA
     WDVVNEALSD NPNEFLRKAP WYDICGEEVI EKAFIWANEA DPNAKLFYND YNLEDPIKRE
     KAYQLVKRLK EKGIPIHGVG IQGHWTLAWP TPKMLEDSIK RFSELGVEVQ ITEFDISIYY
     DRNENNNFKV PPDDRIEKQA QLYKQAFEIL RKYRGVVTGV TFWGVADDYT WLYFWPVRGR
     EDYPLLFDKN HNPKKAFWEI VKF
//