Reviewed,
UniProtKB/Swiss-Prot P00694 (XYNA_BACPU)
Last modified
November 4, 2008.
Version 65.
History...
Clusters with 100%,
90%,
50% identity |
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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents
Names and origin
| Protein names | Recommended 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 |
| ||
| Organism | Bacillus pumilus (Bacillus mesentericus) | ||
| Taxonomic identifier | 1408 [NCBI] | ||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus |
Protein attributes
| Sequence length | 228 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Catalytic activity | Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans. |
| Pathway | |
| Sequence similarities | Belongs to the glycosyl hydrolase 11 (cellulase G) family. |
Ontologies
Keywords | |
|---|---|
| Biological process | Xylan degradation |
| Domain | Signal |
| Molecular function | Glycosidase Hydrolase |
Gene Ontology (GO) | |
| Biological process | xylan catabolic process Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | endo-1,4-beta-xylanase activity Inferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 27 | 27 | |||||||
| Chain | 28 – 228 | 201 | Endo-1,4-beta-xylanase A | PRO_0000007997 | |||||
Sites | |||||||||
| Active site | 120 | 1 | Nucleophile By similarity | ||||||
| Active site | 209 | 1 | Proton donor By similarity | ||||||
Experimental info | |||||||||
| Mutagenesis | 120 | 1 | E → S: Loss of activity | ||||||
| Mutagenesis | 209 | 1 | E → D: Loss of activity | ||||||
Sequences
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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. | |
| PIR | WWBSXP. A00848. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1F5J based on UniProtKB P77853. |
| SMR | P00694. Positions 27-227. |
| ModBase | Search... |
Family and domain databases | |
| InterPro | IPR001137. Glyco_hydro_11. IPR013319. Glyco_hydro_11/12_cat. [Graphical view] |
| Gene3D | G3DSA:2.60.120.180. Glyco_hydro_11/12_cat. 1 hit. |
| Pfam | PF00457. Glyco_hydro_11. 1 hit. [Graphical view] |
| PRINTS | PR00911. GLHYDRLASE11. |
| PROSITE | PS00776. GLYCOSYL_HYDROL_F11_1. 1 hit. PS00777. GLYCOSYL_HYDROL_F11_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| LinkHub | P00694. |
Entry information
| Entry name | XYNA_BACPU | ||||||||
| Accession | Primary (citable) accession number: P00694 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (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 |

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