Reviewed,
UniProtKB/Swiss-Prot P36917 (XYNA_THESA)
Last modified
June 16, 2009.
Version 68.
History...
Clusters with 100%,
90%,
50% identity |
Documents (3) |
Third-party data |
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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 | Thermoanaerobacter saccharolyticum | ||
| Taxonomic identifier | 28896 [NCBI] | ||
| Taxonomic lineage | Bacteria › Firmicutes › Clostridia › Thermoanaerobacterales › Thermoanaerobacterales Family III. Incertae Sedis › Thermoanaerobacterium |
Protein attributes
| Sequence length | 1157 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)
| Function | Endo-acting enzyme that randomly cleaves the internal xylosidic linkages of the xylan backbone, yielding xylooligosaccharides of various lengths which are further hydrolyzed to xylose molecules by beta-xylosidase (EC 3.2.1.37). Requires at least three xylose residues for catalytic activity. Does not have activity against xylobiose. |
| Catalytic activity | Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans. |
| Pathway | |
| Induction | By xylan and xylose. |
| Sequence similarities | Belongs to the glycosyl hydrolase 10 (cellulase F) family. Contains 2 CBM-cenC (cenC-type cellulose-binding) domains. Contains 2 SLH (S-layer homology) domains. |
| biophysicochemical properties | pH dependence: Optimum pH is 5.5. Temperature dependence: Optimum temperature is 70 degrees Celsius. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Xylan degradation |
| Domain | Repeat Signal |
| Molecular function | Glycosidase Hydrolase |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | carbohydrate catabolic process Inferred from electronic annotation. Source: InterPro xylan catabolic processInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | carbohydrate binding Inferred from electronic annotation. Source: InterPro cation bindingInferred from electronic annotation. Source: InterPro endo-1,4-beta-xylanase activityInferred 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 – 33 | 33 | Ref.1 | ||||||
| Chain | 34 – 1157 | 1124 | Endo-1,4-beta-xylanase A | PRO_0000007980 | |||||
Regions | |||||||||
| Domain | 38 – 189 | 152 | CBM-cenC 1 | ||||||
| Domain | 195 – 343 | 149 | CBM-cenC 2 | ||||||
| Domain | 1051 – 1114 | 64 | SLH 1 | ||||||
| Domain | 1115 – 1157 | 43 | SLH 2 | ||||||
| Region | 413 – 649 | 237 | Catalytic Potential | ||||||
Sites | |||||||||
| Active site | 495 | 1 | Proton donor By similarity | ||||||
| Active site | 537 | 1 | Ref.2 | ||||||
| Active site | 600 | 1 | Nucleophile Ref.2 | ||||||
Experimental info | |||||||||
| Mutagenesis | 537 | 1 | D → N: Loss of activity. | ||||||
| Mutagenesis | 600 | 1 | E → Q: Loss of activity. | ||||||
| Mutagenesis | 602 | 1 | D → N: Loss of activity. | ||||||
Sequences
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References
| [1] | "Gene cloning, sequencing, and biochemical characterization of endoxylanase from Thermoanaerobacterium saccharolyticum B6A-RI." Lee Y.-E., Lowe S.E., Zeikus J.G. Appl. Environ. Microbiol. 59:3134-3137(1993) [PubMed: 8215382] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 34-41. Strain: B6A-RI. |
| [2] | "Characterization of the active site and thermostability regions of endoxylanase from Thermoanaerobacterium saccharolyticum B6A-RI." Lee Y.-E., Lowe S.E., Henrissat B., Zeikus J.G. J. Bacteriol. 175:5890-5898(1993) [PubMed: 8376336] [Abstract] Cited for: ACTIVE SITE, MUTAGENESIS. |
Cross-references
Sequence databases | |
|---|---|
| M97882 Genomic DNA. Translation: AAA21812.1. Sequence problems. | |
| PIR | A48490. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1I8A based on UniProtKB Q60037. |
| ModBase | Search... |
Protein family/group databases | |
| CAZy | CBM22. Carbohydrate-Binding Module Family 22. CBM9. Carbohydrate-Binding Module Family 9. GH10. Glycoside Hydrolase Family 10. |
Family and domain databases | |
| InterPro | IPR010502. Carb-bd_9. IPR015922. Carb-bd_9-like. IPR003305. CenC_carb_bd. IPR001000. Glyco_hydro_10. IPR018087. Glyco_hydro_5_CS. IPR013781. Glyco_hydro_sg_catalytic. IPR001119. SLH. [Graphical view] |
| Gene3D | G3DSA:2.60.40.1190. CBD9. 1 hit. G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit. |
| Pfam | PF02018. CBM_4_9. 2 hits. PF06452. DUF1083. 2 hits. PF00331. Glyco_hydro_10. 1 hit. PF00395. SLH. 2 hits. [Graphical view] |
| PRINTS | PR00134. GLHYDRLASE10. |
| SMART | SM00633. Glyco_10. 1 hit. [Graphical view] |
| PROSITE | PS00591. GLYCOSYL_HYDROL_F10. 1 hit. PS00659. GLYCOSYL_HYDROL_F5. 1 hit. PS51272. SLH. 2 hits. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | XYNA_THESA | ||||||||
| Accession | Primary (citable) accession number: P36917 | ||||||||
| 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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