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Reviewed, UniProtKB/Swiss-Prot P00694 (XYNA_BACPU)

Last modified June 16, 2009. Version 69. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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
OrganismBacillus pumilus (Bacillus mesentericus)
Taxonomic identifier1408 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillus

Protein attributes

Sequence length228 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 processXylan degradation
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
Gene Ontology (GO)
   Biological processxylan catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionendo-1,4-beta-xylanase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2727
Chain28 – 228201Endo-1,4-beta-xylanase A
PRO_0000007997

Sites

Active site1201Nucleophile By similarity
Active site2091Proton donor By similarity

Experimental info

Mutagenesis1201E → S: Loss of activity.
Mutagenesis2091E → D: Loss of activity.

Sequences

Sequence LengthMass (Da)Tools
P00694-1 [UniParc].

Last modified February 1, 1996. Version 2.
Checksum: 32EF9833E7B5E503

FASTA22825,491
        10         20         30         40         50         60 
MNLRKLRLLF VMCIGLTLIL TAVPAHARTI TNNEMGNHSG YDYELWKDYG NTSMTLNNGG 

        70         80         90        100        110        120 
AFSAGWNNIG NALFRKGKKF DSTRTHHQLG NISINYNASF NPGGNSYLCV YGWTQSPLAE 

       130        140        150        160        170        180 
YYIVDSWGTY RPTGAYKGSF YADGGTYDIY ETTRVNQPSI IGIATFKQYW SVRQTKRTSG 

       190        200        210        220 
TVSVSAHFRK WESLGMPMGK MYETAFTVEG YQSSGSANVM TNQLFIGN 

« Hide

References

[1]"The complete nucleotide sequence of the xylanase gene (xynA) of Bacillus pumilus."
Fukusaki E., Panbangred W., Shinmyo A., Okada H.
FEBS Lett. 171:197-201(1984)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: IPO.
[2]Urabe I.
Submitted (FEB-1991) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION TO 103.
[3]"Site-directed mutagenesis at aspartate and glutamate residues of xylanase from Bacillus pumilus."
Ko E.P., Akatsuka H., Moriyama H., Shinmyo A., Hata Y., Katsube Y., Urabe I., Okada H.
Biochem. J. 288:117-121(1992) [PubMed: 1359880] [Abstract]
Cited for: MUTAGENESIS, ACTIVE SITES.

Cross-references

Sequence databases

X00660 Genomic DNA. Translation: CAA25278.1.
PIRWWBSXP. A00848.

3D structure databases

HSSPHSSP built from PDB template 1F5J based on UniProtKB P77853.
SMRP00694. Positions 27-227.
ModBaseSearch...

Protein family/group databases

CAZyGH11. Glycoside Hydrolase Family 11.

Enzyme and pathway databases

BRENDA3.2.1.8. 1189.

Family and domain databases

InterProIPR001137. Glyco_hydro_11.
IPR013319. Glyco_hydro_11/12_cat.
IPR018208. Glyco_hydro_11_AS.
[Graphical view]
Gene3DG3DSA:2.60.120.180. Glyco_hydro_11/12_cat. 1 hit.
PfamPF00457. Glyco_hydro_11. 1 hit.
[Graphical view]
PRINTSPR00911. GLHYDRLASE11.
PROSITEPS00776. GLYCOSYL_HYDROL_F11_1. 1 hit.
PS00777. GLYCOSYL_HYDROL_F11_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameXYNA_BACPU
AccessionPrimary (citable) accession number: P00694
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: February 1, 1996
Last modified: June 16, 2009
This is version 69 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents