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Database: UniProt
Entry: P09850
LinkDB: P09850
Original site: P09850 
ID   XYNA_BACCI              Reviewed;         213 AA.
AC   P09850;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   05-JUN-2019, entry version 110.
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;
GN   Name=xlnA;
OS   Bacillus circulans.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1397;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3405767; DOI=10.1093/nar/16.14.7187;
RA   Yang R.C.A., MacKenzie C.R., Narang S.A.;
RT   "Nucleotide sequence of a Bacillus circulans xylanase gene.";
RL   Nucleic Acids Res. 16:7187-7187(1988).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), AND MUTAGENESIS.
RX   PubMed=8019418; DOI=10.1002/pro.5560030312;
RA   Wakarchuk W.W., Campbell R.L., Sung W.L., Davoodi J., Yaguchi M.;
RT   "Mutational and crystallographic analyses of the active site residues
RT   of the Bacillus circulans xylanase.";
RL   Protein Sci. 3:467-475(1994).
RN   [3]
RP   STRUCTURE BY NMR.
RX   PubMed=8756457; DOI=10.1021/bi9613234;
RA   McIntosh L.P., Hand G., Johnson P.E., Joshi M.D., Koerner M.,
RA   Plesniak L.A., Ziser L., Wakarchuk W.W., Withers S.G.;
RT   "The pKa of the general acid/base carboxyl group of a glycosidase
RT   cycles during catalysis: a 13C-NMR study of Bacillus circulans
RT   xylanase.";
RL   Biochemistry 35:9958-9966(1996).
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   -!- SIMILARITY: Belongs to the glycosyl hydrolase 11 (cellulase G)
CC       family. {ECO:0000305}.
DR   EMBL; X07723; CAA30553.1; -; Genomic_DNA.
DR   PIR; S01734; S01734.
DR   PDB; 1BCX; X-ray; 1.81 A; A=29-213.
DR   PDB; 1BVV; X-ray; 1.80 A; A=29-213.
DR   PDB; 1C5H; X-ray; 1.55 A; A=29-213.
DR   PDB; 1C5I; X-ray; 1.80 A; A=29-213.
DR   PDB; 1HV0; X-ray; 1.60 A; A=29-213.
DR   PDB; 1HV1; X-ray; 1.80 A; A=29-213.
DR   PDB; 1XNB; X-ray; 1.49 A; A=29-213.
DR   PDB; 1XNC; X-ray; 1.60 A; A=29-213.
DR   PDB; 2BVV; X-ray; 1.50 A; A=29-213.
DR   PDB; 3LB9; X-ray; 3.00 A; A/B/C=29-213.
DR   PDB; 3VZJ; X-ray; 2.41 A; A/B/C/D=29-213.
DR   PDB; 3VZK; X-ray; 1.55 A; A/B=29-213.
DR   PDB; 3VZL; X-ray; 2.00 A; A/B/C/D=29-213.
DR   PDB; 3VZM; X-ray; 1.86 A; A=29-213.
DR   PDB; 3VZN; X-ray; 1.67 A; A/B=29-213.
DR   PDB; 3VZO; X-ray; 1.73 A; A=29-213.
DR   PDBsum; 1BCX; -.
DR   PDBsum; 1BVV; -.
DR   PDBsum; 1C5H; -.
DR   PDBsum; 1C5I; -.
DR   PDBsum; 1HV0; -.
DR   PDBsum; 1HV1; -.
DR   PDBsum; 1XNB; -.
DR   PDBsum; 1XNC; -.
DR   PDBsum; 2BVV; -.
DR   PDBsum; 3LB9; -.
DR   PDBsum; 3VZJ; -.
DR   PDBsum; 3VZK; -.
DR   PDBsum; 3VZL; -.
DR   PDBsum; 3VZM; -.
DR   PDBsum; 3VZN; -.
DR   PDBsum; 3VZO; -.
DR   SMR; P09850; -.
DR   DrugBank; DB03389; alpha-D-Xylopyranose.
DR   CAZy; GH11; Glycoside Hydrolase Family 11.
DR   mycoCLAP; XYN11A_BACCI; -.
DR   BRENDA; 3.2.1.8; 649.
DR   SABIO-RK; P09850; -.
DR   UniPathway; UPA00114; -.
DR   EvolutionaryTrace; P09850; -.
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; 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   1: Evidence at protein level;
KW   3D-structure; Carbohydrate metabolism; Glycosidase; Hydrolase;
KW   Polysaccharide degradation; Signal; Xylan degradation.
FT   SIGNAL        1     28
FT   CHAIN        29    213       Endo-1,4-beta-xylanase.
FT                                {ECO:0000269|PubMed:3405767}.
FT                                /FTId=PRO_0000007996.
FT   DOMAIN       29    213       GH11. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01097}.
FT   ACT_SITE    106    106       Nucleophile. {ECO:0000255|PROSITE-
FT                                ProRule:PRU10062,
FT                                ECO:0000269|PubMed:8019418}.
FT   ACT_SITE    200    200       Proton donor. {ECO:0000255|PROSITE-
FT                                ProRule:PRU10063,
FT                                ECO:0000269|PubMed:8019418}.
FT   STRAND       23     26       {ECO:0000244|PDB:3LB9}.
FT   STRAND       33     38       {ECO:0000244|PDB:1XNB}.
FT   STRAND       42     48       {ECO:0000244|PDB:1XNB}.
FT   STRAND       53     60       {ECO:0000244|PDB:1XNB}.
FT   STRAND       62     72       {ECO:0000244|PDB:1XNB}.
FT   STRAND       78    101       {ECO:0000244|PDB:1XNB}.
FT   TURN        102    104       {ECO:0000244|PDB:1XNB}.
FT   STRAND      105    115       {ECO:0000244|PDB:1XNB}.
FT   STRAND      121    128       {ECO:0000244|PDB:1XNB}.
FT   STRAND      131    144       {ECO:0000244|PDB:1XNB}.
FT   STRAND      148    162       {ECO:0000244|PDB:1XNB}.
FT   STRAND      166    168       {ECO:0000244|PDB:1XNB}.
FT   STRAND      170    173       {ECO:0000244|PDB:1XNB}.
FT   HELIX       174    183       {ECO:0000244|PDB:1XNB}.
FT   STRAND      190    203       {ECO:0000244|PDB:1XNB}.
FT   STRAND      205    213       {ECO:0000244|PDB:1XNB}.
SQ   SEQUENCE   213 AA;  23359 MW;  4BA0A35238CC0135 CRC64;
     MFKFKKNFLV GLSAALMSIS LFSATASAAS TDYWQNWTDG GGIVNAVNGS GGNYSVNWSN
     TGNFVVGKGW TTGSPFRTIN YNAGVWAPNG NGYLTLYGWT RSPLIEYYVV DSWGTYRPTG
     TYKGTVKSDG GTYDIYTTTR YNAPSIDGDR TTFTQYWSVR QSKRPTGSNA TITFTNHVNA
     WKSHGMNLGS NWAYQVMATE GYQSSGSSNV TVW
//
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