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Database: UniProt
Entry: P40943
LinkDB: P40943
Original site: P40943 
ID   XYN1_GEOSE              Reviewed;         407 AA.
AC   P40943; Q09LX3;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   05-DEC-2018, entry version 103.
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   Geobacillus stearothermophilus (Bacillus stearothermophilus).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=1422;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=T-6 / NCIMB 40221;
RX   PubMed=8031084;
RA   Gat O., Lapidot A., Alchanati I., Regueros C., Shoham Y.;
RT   "Cloning and DNA sequence of the gene coding for Bacillus
RT   stearothermophilus T-6 xylanase.";
RL   Appl. Environ. Microbiol. 60:1889-1896(1994).
RN   [2]
RP   PROTEIN SEQUENCE OF 29-73.
RC   STRAIN=T-6;
RX   PubMed=8328796;
RA   Khasin A., Alchanati I., Shoham Y.;
RT   "Purification and characterization of a thermostable xylanase from
RT   Bacillus stearothermophilus T-6.";
RL   Appl. Environ. Microbiol. 59:1725-1730(1993).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in
CC         xylans.; EC=3.2.1.8;
CC   -!- PATHWAY: Glycan degradation; xylan degradation.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- INDUCTION: By xylose.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F)
CC       family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABI49951.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; DQ868502; ABI49951.1; ALT_INIT; Genomic_DNA.
DR   PIR; I40570; I40570.
DR   PDB; 1HIZ; X-ray; 2.40 A; A=29-407.
DR   PDB; 1R85; X-ray; 1.45 A; A=29-407.
DR   PDB; 1R86; X-ray; 1.80 A; A=29-407.
DR   PDB; 1R87; X-ray; 1.67 A; A=29-407.
DR   PDB; 3MMD; X-ray; 1.70 A; A=29-407.
DR   PDB; 4PRW; X-ray; 1.80 A; A=29-407.
DR   PDB; 4PUD; X-ray; 2.01 A; A=37-407.
DR   PDB; 4PUE; X-ray; 2.20 A; A=37-407.
DR   PDBsum; 1HIZ; -.
DR   PDBsum; 1R85; -.
DR   PDBsum; 1R86; -.
DR   PDBsum; 1R87; -.
DR   PDBsum; 3MMD; -.
DR   PDBsum; 4PRW; -.
DR   PDBsum; 4PUD; -.
DR   PDBsum; 4PUE; -.
DR   ProteinModelPortal; P40943; -.
DR   SMR; P40943; -.
DR   DrugBank; DB03389; alpha-D-Xylopyranose.
DR   DrugBank; DB02379; Beta-D-Glucose.
DR   CAZy; GH10; Glycoside Hydrolase Family 10.
DR   UniPathway; UPA00114; -.
DR   EvolutionaryTrace; P40943; -.
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; IPR031158; GH10_AS.
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; PS00591; GH10_1; 1.
DR   PROSITE; PS51760; GH10_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Carbohydrate metabolism; Direct protein sequencing;
KW   Glycosidase; Hydrolase; Polysaccharide degradation; Secreted; Signal;
KW   Xylan degradation.
FT   SIGNAL        1     28       {ECO:0000269|PubMed:8328796}.
FT   CHAIN        29    407       Endo-1,4-beta-xylanase.
FT                                /FTId=PRO_0000007968.
FT   DOMAIN       42    406       GH10. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01096}.
FT   ACT_SITE    187    187       Proton donor. {ECO:0000250}.
FT   ACT_SITE    293    293       Nucleophile. {ECO:0000255|PROSITE-
FT                                ProRule:PRU10061}.
FT   TURN         34     36       {ECO:0000244|PDB:1HIZ}.
FT   HELIX        42     44       {ECO:0000244|PDB:1R85}.
FT   HELIX        48     52       {ECO:0000244|PDB:1R85}.
FT   TURN         53     55       {ECO:0000244|PDB:1R85}.
FT   STRAND       57     62       {ECO:0000244|PDB:1R85}.
FT   HELIX        64     68       {ECO:0000244|PDB:1R85}.
FT   HELIX        70     79       {ECO:0000244|PDB:1R85}.
FT   STRAND       81     87       {ECO:0000244|PDB:1R85}.
FT   HELIX        91     94       {ECO:0000244|PDB:1R85}.
FT   HELIX       104    115       {ECO:0000244|PDB:1R85}.
FT   STRAND      119    123       {ECO:0000244|PDB:1R85}.
FT   STRAND      128    130       {ECO:0000244|PDB:1R87}.
FT   HELIX       133    136       {ECO:0000244|PDB:1R85}.
FT   STRAND      141    143       {ECO:0000244|PDB:1R85}.
FT   HELIX       144    146       {ECO:0000244|PDB:1R85}.
FT   HELIX       150    175       {ECO:0000244|PDB:1R85}.
FT   TURN        176    178       {ECO:0000244|PDB:1R85}.
FT   STRAND      181    187       {ECO:0000244|PDB:1R85}.
FT   STRAND      193    195       {ECO:0000244|PDB:1R85}.
FT   HELIX       199    204       {ECO:0000244|PDB:1R85}.
FT   HELIX       207    220       {ECO:0000244|PDB:1R85}.
FT   STRAND      224    231       {ECO:0000244|PDB:1R85}.
FT   HELIX       238    251       {ECO:0000244|PDB:1R85}.
FT   STRAND      258    261       {ECO:0000244|PDB:1R85}.
FT   STRAND      267    270       {ECO:0000244|PDB:1R85}.
FT   HELIX       272    284       {ECO:0000244|PDB:1R85}.
FT   STRAND      288    296       {ECO:0000244|PDB:1R85}.
FT   STRAND      306    308       {ECO:0000244|PDB:1R87}.
FT   HELIX       309    311       {ECO:0000244|PDB:1R85}.
FT   HELIX       314    333       {ECO:0000244|PDB:1R85}.
FT   HELIX       335    337       {ECO:0000244|PDB:1R85}.
FT   STRAND      338    347       {ECO:0000244|PDB:1R85}.
FT   HELIX       352    356       {ECO:0000244|PDB:1R85}.
FT   STRAND      359    361       {ECO:0000244|PDB:1R85}.
FT   STRAND      376    379       {ECO:0000244|PDB:1R85}.
FT   STRAND      388    390       {ECO:0000244|PDB:1R85}.
FT   STRAND      394    396       {ECO:0000244|PDB:1R85}.
FT   HELIX       398    404       {ECO:0000244|PDB:1R85}.
SQ   SEQUENCE   407 AA;  46763 MW;  AD385C90B252B82A CRC64;
     MRNVVRKPLT IGLALTLLLP MGMTATSAKN ADSYAKKPHI SALNAPQLDQ RYKNEFTIGA
     AVEPYQLQNE KDVQMLKRHF NSIVAENVMK PISIQPEEGK FNFEQADRIV KFAKANGMDI
     RFHTLVWHSQ VPQWFFLDKE GKPMVNETDP VKREQNKQLL LKRLETHIKT IVERYKDDIK
     YWDVVNEVVG DDGKLRNSPW YQIAGIDYIK VAFQAARKYG GDNIKLYMND YNTEVEPKRT
     ALYNLVKQLK EEGVPIDGIG HQSHIQIGWP SEAEIEKTIN MFAALGLDNQ ITELDVSMYG
     WPPRAYPTYD AIPKQKFLDQ AARYDRLFKL YEKLSDKISN VTFWGIADNH TWLDSRADVY
     YDANGNVVVD PNAPYAKVEK GKGKDAPFVF GPDYKVKPAY WAIIDHK
//
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