XYNA_BACSU
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 03-AUG-2022, entry version 162.
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 comparison
RT 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 the
RT 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., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., 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., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., 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 spectrometry.";
RL Biochemistry 33:7027-7032(1994).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.;
CC EC=3.2.1.8;
CC -!- PATHWAY: Glycan degradation; xylan degradation.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 11 (cellulase G) family.
CC {ECO:0000305}.
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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 AlphaFoldDB; P18429; -.
DR BMRB; P18429; -.
DR SMR; P18429; -.
DR IntAct; P18429; 2.
DR MINT; P18429; -.
DR STRING; 224308.BSU18840; -.
DR CAZy; GH11; Glycoside Hydrolase Family 11.
DR CLAE; XYN11C_BACSU; -.
DR PaxDb; P18429; -.
DR EnsemblBacteria; CAB13776; CAB13776; BSU_18840.
DR GeneID; 939861; -.
DR KEGG; bsu:BSU18840; -.
DR PATRIC; fig|224308.179.peg.2054; -.
DR eggNOG; COG0726; Bacteria.
DR InParanoid; P18429; -.
DR OMA; DYWQNWT; -.
DR PhylomeDB; P18429; -.
DR BioCyc; BSUB:BSU18840-MON; -.
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; IEA:UniProtKB-EC.
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; Glycosidase; Hydrolase;
KW Polysaccharide degradation; Reference proteome; Signal; Xylan degradation.
FT SIGNAL 1..28
FT CHAIN 29..213
FT /note="Endo-1,4-beta-xylanase A"
FT /id="PRO_0000007999"
FT DOMAIN 29..213
FT /note="GH11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01097"
FT ACT_SITE 106
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10062,
FT ECO:0000269|PubMed:7911679"
FT ACT_SITE 200
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10063"
FT MUTAGEN 106
FT /note="E->S: Drastically reduced activity."
FT /evidence="ECO:0000269|Ref.4"
FT MUTAGEN 200
FT /note="E->S: Drastically reduced activity."
FT /evidence="ECO:0000269|Ref.4"
FT STRAND 33..38
FT /evidence="ECO:0007829|PDB:5TVY"
FT STRAND 42..48
FT /evidence="ECO:0007829|PDB:5TVY"
FT STRAND 53..60
FT /evidence="ECO:0007829|PDB:5TVY"
FT STRAND 62..72
FT /evidence="ECO:0007829|PDB:5TVY"
FT STRAND 78..88
FT /evidence="ECO:0007829|PDB:5TVY"
FT STRAND 90..101
FT /evidence="ECO:0007829|PDB:5TVY"
FT TURN 102..104
FT /evidence="ECO:0007829|PDB:5TVY"
FT STRAND 105..116
FT /evidence="ECO:0007829|PDB:5TVY"
FT STRAND 121..128
FT /evidence="ECO:0007829|PDB:5TVY"
FT STRAND 131..145
FT /evidence="ECO:0007829|PDB:5TVY"
FT STRAND 148..162
FT /evidence="ECO:0007829|PDB:5TVY"
FT STRAND 170..173
FT /evidence="ECO:0007829|PDB:5TVY"
FT HELIX 174..183
FT /evidence="ECO:0007829|PDB:5TVY"
FT STRAND 190..203
FT /evidence="ECO:0007829|PDB:5TVY"
FT STRAND 206..213
FT /evidence="ECO:0007829|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
