GenomeNet

Database: UniProt
Entry: P18429
LinkDB: P18429
Original site: P18429 
ID   XYNA_BACSU              Reviewed;         213 AA.
AC   P18429;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 1.
DT   10-APR-2019, entry version 148.
DE   RecName: Full=Endo-1,4-beta-xylanase A;
DE            Short=Xylanase A;
DE            EC=3.2.1.8;
DE   AltName: Full=1,4-beta-D-xylan xylanohydrolase A;
DE   Flags: Precursor;
GN   Name=xynA; OrderedLocusNames=BSU18840;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Paice M.G., Bourbonnais R., Desrochers M., Jurasek L., Yaguchi M.;
RT   "A xylanase gene from Bacillus subtilis: nucleotide sequence and
RT   comparison with B. pumilus gene.";
RL   Arch. Microbiol. 144:201-206(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Lapidus A., Galleron N., Sorokin A., Ehrlich S.D.;
RT   "Sequence analysis of the Bacillus subtilis chromosome region between
RT   the terC and odhAB loci cloned in a yeast artificial chromosome.";
RL   Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G.,
RA   Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S.,
RA   Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S.,
RA   Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M.,
RA   Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A.,
RA   Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T.,
RA   Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D.,
RA   Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N.,
RA   Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G.,
RA   Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A.,
RA   Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M.,
RA   Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M.,
RA   Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S.,
RA   Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G.,
RA   Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B.,
RA   Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R.,
RA   Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P.,
RA   Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H.,
RA   Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P.,
RA   Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F.,
RA   Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H.,
RA   Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [4]
RP   MUTAGENESIS.
RA   Wakarchuk W., Methot N., Lanthier P., Sung W., Seligy V., Yaguchi M.,
RA   To R., Campbell R., Rose D.;
RL   (In) Visser J., Beldman G., Kusters-van Someren M.A., Voragen A.G.J.
RL   (eds.);
RL   Xylans and xylanases, pp.439-442, Elsevier, Amsterdam (1992).
RN   [5]
RP   ACTIVE SITE GLU-106.
RX   PubMed=7911679; DOI=10.1021/bi00189a002;
RA   Miao S., Ziser L., Aebersold R., Withers S.G.;
RT   "Identification of glutamic acid 78 as the active site nucleophile in
RT   Bacillus subtilis xylanase using electrospray tandem mass
RT   spectrometry.";
RL   Biochemistry 33:7027-7032(1994).
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; M36648; AAA22897.1; -; Genomic_DNA.
DR   EMBL; AF027868; AAB84458.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB13776.1; -; Genomic_DNA.
DR   PIR; I40569; I40569.
DR   RefSeq; NP_389765.1; NC_000964.3.
DR   RefSeq; WP_003231377.1; NZ_JNCM01000036.1.
DR   PDB; 1AXK; X-ray; 2.10 A; A/B=29-213.
DR   PDB; 1XXN; X-ray; 1.70 A; A=29-213.
DR   PDB; 2B42; X-ray; 2.50 A; B=29-213.
DR   PDB; 2B45; X-ray; 2.00 A; X=29-213.
DR   PDB; 2B46; X-ray; 2.21 A; X=29-213.
DR   PDB; 2DCY; X-ray; 1.40 A; A/B/C/D/E=29-213.
DR   PDB; 2DCZ; X-ray; 1.90 A; A/B=29-213.
DR   PDB; 2QZ3; X-ray; 1.80 A; A/B=29-213.
DR   PDB; 2Z79; X-ray; 1.30 A; A/B=29-213.
DR   PDB; 3EXU; X-ray; 1.81 A; A/B=29-213.
DR   PDB; 3HD8; X-ray; 2.39 A; B/D=29-213.
DR   PDB; 5K9Y; X-ray; 2.20 A; A/B=29-213.
DR   PDB; 5TVV; X-ray; 1.79 A; A/B/C=30-213.
DR   PDB; 5TVY; X-ray; 1.00 A; A/B=30-213.
DR   PDB; 5TZO; X-ray; 1.67 A; A/B/C=30-213.
DR   PDBsum; 1AXK; -.
DR   PDBsum; 1XXN; -.
DR   PDBsum; 2B42; -.
DR   PDBsum; 2B45; -.
DR   PDBsum; 2B46; -.
DR   PDBsum; 2DCY; -.
DR   PDBsum; 2DCZ; -.
DR   PDBsum; 2QZ3; -.
DR   PDBsum; 2Z79; -.
DR   PDBsum; 3EXU; -.
DR   PDBsum; 3HD8; -.
DR   PDBsum; 5K9Y; -.
DR   PDBsum; 5TVV; -.
DR   PDBsum; 5TVY; -.
DR   PDBsum; 5TZO; -.
DR   ProteinModelPortal; P18429; -.
DR   SMR; P18429; -.
DR   IntAct; P18429; 2.
DR   MINT; P18429; -.
DR   STRING; 224308.BSU18840; -.
DR   CAZy; GH11; Glycoside Hydrolase Family 11.
DR   mycoCLAP; XYN11C_BACSU; -.
DR   PaxDb; P18429; -.
DR   PRIDE; P18429; -.
DR   EnsemblBacteria; CAB13776; CAB13776; BSU18840.
DR   GeneID; 939861; -.
DR   KEGG; bsu:BSU18840; -.
DR   PATRIC; fig|224308.179.peg.2054; -.
DR   eggNOG; ENOG4107T94; Bacteria.
DR   eggNOG; ENOG410YH6C; LUCA.
DR   HOGENOM; HOG000179135; -.
DR   InParanoid; P18429; -.
DR   KO; K01181; -.
DR   OMA; IEYYVVD; -.
DR   PhylomeDB; P18429; -.
DR   BioCyc; BSUB:BSU18840-MONOMER; -.
DR   BRENDA; 3.2.1.8; 658.
DR   SABIO-RK; P18429; -.
DR   UniPathway; UPA00114; -.
DR   EvolutionaryTrace; P18429; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0031176; F:endo-1,4-beta-xylanase activity; IBA:GO_Central.
DR   GO; GO:0045493; P:xylan catabolic process; IBA:GO_Central.
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; Complete proteome; Glycosidase;
KW   Hydrolase; Polysaccharide degradation; Reference proteome; Signal;
KW   Xylan degradation.
FT   SIGNAL        1     28
FT   CHAIN        29    213       Endo-1,4-beta-xylanase A.
FT                                /FTId=PRO_0000007999.
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:7911679}.
FT   ACT_SITE    200    200       Proton donor. {ECO:0000255|PROSITE-
FT                                ProRule:PRU10063}.
FT   MUTAGEN     106    106       E->S: Drastically reduced activity.
FT                                {ECO:0000269|Ref.4}.
FT   MUTAGEN     200    200       E->S: Drastically reduced activity.
FT                                {ECO:0000269|Ref.4}.
FT   STRAND       33     38       {ECO:0000244|PDB:5TVY}.
FT   STRAND       42     48       {ECO:0000244|PDB:5TVY}.
FT   STRAND       53     60       {ECO:0000244|PDB:5TVY}.
FT   STRAND       62     72       {ECO:0000244|PDB:5TVY}.
FT   STRAND       78     88       {ECO:0000244|PDB:5TVY}.
FT   STRAND       90    101       {ECO:0000244|PDB:5TVY}.
FT   TURN        102    104       {ECO:0000244|PDB:5TVY}.
FT   STRAND      105    116       {ECO:0000244|PDB:5TVY}.
FT   STRAND      121    128       {ECO:0000244|PDB:5TVY}.
FT   STRAND      131    145       {ECO:0000244|PDB:5TVY}.
FT   STRAND      148    162       {ECO:0000244|PDB:5TVY}.
FT   STRAND      170    173       {ECO:0000244|PDB:5TVY}.
FT   HELIX       174    183       {ECO:0000244|PDB:5TVY}.
FT   STRAND      190    203       {ECO:0000244|PDB:5TVY}.
FT   STRAND      206    213       {ECO:0000244|PDB:5TVY}.
SQ   SEQUENCE   213 AA;  23345 MW;  20CBA35238CC0564 CRC64;
     MFKFKKNFLV GLSAALMSIS LFSATASAAS TDYWQNWTDG GGIVNAVNGS GGNYSVNWSN
     TGNFVVGKGW TTGSPFRTIN YNAGVWAPNG NGYLTLYGWT RSPLIEYYVV DSWGTYRPTG
     TYKGTVKSDG GTYDIYTTTR YNAPSIDGDR TTFTQYWSVR QSKRPTGSNA TITFSNHVNA
     WKSHGMNLGS NWAYQVMATE GYQSSGSSNV TVW
//
DBGET integrated database retrieval system