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Database: UniProt
Entry: Q12603
LinkDB: Q12603
Original site: Q12603 
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   05-JUL-2017, entry version 71.
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; Dictyoglomi; Dictyoglomales; Dictyoglomaceae; Dictyoglomus.
OX   NCBI_TaxID=14;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Rt46 B.1;
RX   PubMed=8534104;
RA   Gibbs M.D., Reeves R.A., Bergquist P.L.;
RT   "Cloning, sequencing, and expression of a xylanase gene from the
RT   extreme thermophile Dictyoglomus thermophilum Rt46B.1 and activity of
RT   the enzyme on fiber-bound substrate.";
RL   Appl. Environ. Microbiol. 61:4403-4408(1995).
CC   -!- CATALYTIC ACTIVITY: Endohydrolysis of (1->4)-beta-D-xylosidic
CC       linkages in xylans.
CC   -!- PATHWAY: Glycan degradation; xylan degradation.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F)
CC       family. {ECO:0000305}.
DR   EMBL; L39866; AAA96979.1; -; Genomic_DNA.
DR   PIR; T08469; T08469.
DR   ProteinModelPortal; Q12603; -.
DR   SMR; Q12603; -.
DR   CAZy; GH10; Glycoside Hydrolase Family 10.
DR   eggNOG; ENOG4105D9F; Bacteria.
DR   eggNOG; COG3693; LUCA.
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   InterPro; IPR001000; GH10.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   Pfam; PF00331; Glyco_hydro_10; 1.
DR   PRINTS; PR00134; GLHYDRLASE10.
DR   SMART; SM00633; Glyco_10; 1.
DR   SUPFAM; SSF51445; SSF51445; 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       {ECO:0000255}.
FT   CHAIN        24    352       Beta-1,4-xylanase.
FT                                /FTId=PRO_0000184065.
FT   DOMAIN       29    352       GH10. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01096}.
FT   ACT_SITE    155    155       Proton donor. {ECO:0000250}.
FT   ACT_SITE    262    262       Nucleophile. {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
//
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