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P09850 (XYNA_BACCI) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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

Short name=Xylanase
EC=3.2.1.8
Alternative name(s):
1,4-beta-D-xylan xylanohydrolase
Gene names
Name:xlnA
OrganismBacillus circulans
Taxonomic identifier1397 [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
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 Ref.1
PRO_0000007996

Sites

Active site1061Nucleophile Ref.2
Active site2001Proton donor Ref.2

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P09850 [UniParc].

Last modified July 1, 1989. Version 1.
Checksum: 4BA0A35238CC0135

FASTA21323,359
        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 TITFTNHVNA 

       190        200        210 
WKSHGMNLGS NWAYQVMATE GYQSSGSSNV TVW 

« Hide

References

[1]"Nucleotide sequence of a Bacillus circulans xylanase gene."
Yang R.C.A., MacKenzie C.R., Narang S.A.
Nucleic Acids Res. 16:7187-7187(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Mutational and crystallographic analyses of the active site residues of the Bacillus circulans xylanase."
Wakarchuk W.W., Campbell R.L., Sung W.L., Davoodi J., Yaguchi M.
Protein Sci. 3:467-475(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), MUTAGENESIS.
[3]"The pKa of the general acid/base carboxyl group of a glycosidase cycles during catalysis: a 13C-NMR study of Bacillus circulans xylanase."
McIntosh L.P., Hand G., Johnson P.E., Joshi M.D., Koerner M., Plesniak L.A., Ziser L., Wakarchuk W.W., Withers S.G.
Biochemistry 35:9958-9966(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X07723 Genomic DNA. Translation: CAA30553.1.
PIRS01734.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BCXX-ray1.81A29-213[»]
1BVVX-ray1.80A29-213[»]
1C5HX-ray1.55A29-213[»]
1C5IX-ray1.80A29-213[»]
1HV0X-ray1.60A29-213[»]
1HV1X-ray1.80A29-213[»]
1XNBX-ray1.49A29-213[»]
1XNCX-ray1.60A29-213[»]
2BVVX-ray1.50A29-213[»]
3LB9X-ray3.00A/B/C29-213[»]
3VZJX-ray2.41A/B/C/D29-213[»]
3VZKX-ray1.55A/B29-213[»]
3VZLX-ray2.00A/B/C/D29-213[»]
3VZMX-ray1.86A29-213[»]
3VZNX-ray1.67A/B29-213[»]
3VZOX-ray1.73A29-213[»]
ProteinModelPortalP09850.
SMRP09850. Positions 29-213.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH11. Glycoside Hydrolase Family 11.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKP09850.
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

EvolutionaryTraceP09850.

Entry information

Entry nameXYNA_BACCI
AccessionPrimary (citable) accession number: P09850
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: July 9, 2014
This is version 91 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