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P18429 (XYNA_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 119. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Endo-1,4-beta-xylanase A

Short name=Xylanase A
EC=3.2.1.8
Alternative name(s):
1,4-beta-D-xylan xylanohydrolase A
Gene names
Name:xynA
Ordered Locus Names:BSU18840
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length213 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.

Pathway

Glycan degradation; xylan degradation.

Sequence similarities

Belongs to the glycosyl hydrolase 11 (cellulase G) family.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Polysaccharide degradation
Xylan degradation
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processxylan catabolic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Molecular_functionendo-1,4-beta-xylanase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2828
Chain29 – 213185Endo-1,4-beta-xylanase A
PRO_0000007999

Sites

Active site1061Nucleophile Ref.5
Active site2001Proton donor By similarity

Experimental info

Mutagenesis1061E → S: Drastically reduced activity.
Mutagenesis2001E → S: Drastically reduced activity.

Secondary structure

......................... 213
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P18429 [UniParc].

Last modified November 1, 1990. Version 1.
Checksum: 20CBA35238CC0564

FASTA21323,345
        10         20         30         40         50         60 
MFKFKKNFLV GLSAALMSIS LFSATASAAS TDYWQNWTDG GGIVNAVNGS GGNYSVNWSN 

        70         80         90        100        110        120 
TGNFVVGKGW TTGSPFRTIN YNAGVWAPNG NGYLTLYGWT RSPLIEYYVV DSWGTYRPTG 

       130        140        150        160        170        180 
TYKGTVKSDG GTYDIYTTTR YNAPSIDGDR TTFTQYWSVR QSKRPTGSNA TITFSNHVNA 

       190        200        210 
WKSHGMNLGS NWAYQVMATE GYQSSGSSNV TVW 

« Hide

References

« Hide 'large scale' references
[1]"A xylanase gene from Bacillus subtilis: nucleotide sequence and comparison with B. pumilus gene."
Paice M.G., Bourbonnais R., Desrochers M., Jurasek L., Yaguchi M.
Arch. Microbiol. 144:201-206(1986)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Sequence analysis of the Bacillus subtilis chromosome region between the terC and odhAB loci cloned in a yeast artificial chromosome."
Lapidus A., Galleron N., Sorokin A., Ehrlich S.D.
Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. expand/collapse author list , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.
[4]Wakarchuk W., Methot N., Lanthier P., Sung W., Seligy V., Yaguchi M., To R., Campbell R., Rose D.
(In) Visser J., Beldman G., Kusters-van Someren M.A., Voragen A.G.J. (eds.); Xylans and xylanases, pp.439-442, Elsevier, Amsterdam (1992)
Cited for: MUTAGENESIS.
[5]"Identification of glutamic acid 78 as the active site nucleophile in Bacillus subtilis xylanase using electrospray tandem mass spectrometry."
Miao S., Ziser L., Aebersold R., Withers S.G.
Biochemistry 33:7027-7032(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: ACTIVE SITE GLU-106.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M36648 Genomic DNA. Translation: AAA22897.1.
AF027868 Genomic DNA. Translation: AAB84458.1.
AL009126 Genomic DNA. Translation: CAB13776.1.
PIRI40569.
RefSeqNP_389765.1. NC_000964.3.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AXKX-ray2.10A/B29-213[»]
1XXNX-ray1.70A29-213[»]
2B42X-ray2.50B29-213[»]
2B45X-ray2.00X29-213[»]
2B46X-ray2.21X29-213[»]
2DCYX-ray1.40A/B/C/D/E29-213[»]
2DCZX-ray1.90A/B29-213[»]
2QZ3X-ray1.80A/B29-213[»]
2Z79X-ray1.30A/B29-213[»]
3EXUX-ray1.81A/B29-213[»]
3HD8X-ray2.39B/D29-213[»]
ProteinModelPortalP18429.
SMRP18429. Positions 29-213.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP18429. 2 interactions.
MINTMINT-7101863.
STRING224308.BSU18840.

Protein family/group databases

CAZyGH11. Glycoside Hydrolase Family 11.

Proteomic databases

PaxDbP18429.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB13776; CAB13776; BSU18840.
GeneID939861.
KEGGbsu:BSU18840.
PATRIC18975607. VBIBacSub10457_1994.

Organism-specific databases

GenoListBSU18840. [Micado]

Phylogenomic databases

eggNOGNOG05353.
HOGENOMHOG000179135.
KOK01181.
OMATYDIYTT.
OrthoDBEOG63VBWG.
ProtClustDBCLSK872863.

Enzyme and pathway databases

BioCycBSUB:BSU18840-MONOMER.
BRENDA3.2.1.8. 700.
SABIO-RKP18429.
UniPathwayUPA00114.

Family and domain databases

Gene3D2.60.120.180. 1 hit.
InterProIPR008985. ConA-like_lec_gl_sf.
IPR001137. Glyco_hydro_11.
IPR013319. Glyco_hydro_11/12.
IPR018208. Glyco_hydro_11_AS.
[Graphical view]
PfamPF00457. Glyco_hydro_11. 1 hit.
[Graphical view]
PRINTSPR00911. GLHYDRLASE11.
SUPFAMSSF49899. SSF49899. 1 hit.
PROSITEPS00776. GLYCOSYL_HYDROL_F11_1. 1 hit.
PS00777. GLYCOSYL_HYDROL_F11_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP18429.

Entry information

Entry nameXYNA_BACSU
AccessionPrimary (citable) accession number: P18429
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1990
Last modified: November 13, 2013
This is version 119 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList