Reviewed,
UniProtKB/Swiss-Prot O59893 (AXE2_PENPU)
Last modified
June 16, 2009.
Version 43.
History...
Clusters with 100%,
90%,
50% identity |
Documents (3) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Acetylxylan esterase 2 EC=3.1.1.72 Alternative name(s): AXE II | ||||
| Gene names |
| ||||
| Organism | Penicillium purpurogenum | ||||
| Taxonomic identifier | 28575 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Penicillium |
Protein attributes
| Sequence length | 234 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 | Degrades acetylated xylans by cleaving acetyl side groups from the hetero-xylan backbone. Ref.2 |
| Catalytic activity | Deacetylation of xylans and xylo-oligosaccharides. |
| Pathway | |
| Subunit structure | Monomer. |
| Subcellular location | |
| Induction | Induced by xylan and repressed by glucose. Expressed at neutral pH, but not under alkaline or acidic condtions. Ref.3 |
| Sequence similarities | Belongs to the cutinase family. Acetylxylan esterase subfamily. |
| biophysicochemical properties | pH dependence: Optimum pH is 6. Temperature dependence: Optimum temperature is 60 degrees Celsius. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Carbohydrate metabolism Cellulose degradation Polysaccharide degradation |
| Cellular component | Secreted |
| Domain | Signal |
| Molecular function | Hydrolase Serine esterase |
| PTM | Cleavage on pair of basic residues Disulfide bond Glycoprotein |
| Technical term | 3D-structure Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | cellulose catabolic process Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | acetylxylan esterase 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 – 17 | 17 | Potential | |||||||||||||||||||||||||||||||||||||
| Propeptide | 18 – 27 | 10 | Ref.2 Ref.1 | PRO_0000234624 | ||||||||||||||||||||||||||||||||||||
| Chain | 28 – 234 | 207 | Acetylxylan esterase 2 | PRO_0000234625 | ||||||||||||||||||||||||||||||||||||
Sites | ||||||||||||||||||||||||||||||||||||||||
| Active site | 117 | 1 | By similarity | |||||||||||||||||||||||||||||||||||||
| Active site | 202 | 1 | By similarity | |||||||||||||||||||||||||||||||||||||
| Active site | 214 | 1 | By similarity | |||||||||||||||||||||||||||||||||||||
Amino acid modifications | ||||||||||||||||||||||||||||||||||||||||
| Glycosylation | 207 | 1 | N-linked (GlcNAc...) Potential | |||||||||||||||||||||||||||||||||||||
| Disulfide bond | 29 ↔ 106 | |||||||||||||||||||||||||||||||||||||||
| Disulfide bond | 73 ↔ 79 | |||||||||||||||||||||||||||||||||||||||
| Disulfide bond | 128 ↔ 188 | |||||||||||||||||||||||||||||||||||||||
| Disulfide bond | 174 ↔ 206 | |||||||||||||||||||||||||||||||||||||||
| Disulfide bond | 198 ↔ 205 | |||||||||||||||||||||||||||||||||||||||
Experimental info | ||||||||||||||||||||||||||||||||||||||||
| Sequence conflict | 57 | 1 | L → I AA sequence Ref.2 | |||||||||||||||||||||||||||||||||||||
Secondary structure | ||||||||||||||||||||||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||||||||||||||||||||||
| Beta strand | 31 – 37 | 7 | ||||||||||||||||||||||||||||||||||||||
| Helix | 47 – 49 | 3 | ||||||||||||||||||||||||||||||||||||||
| Helix | 50 – 59 | 10 | ||||||||||||||||||||||||||||||||||||||
| Beta strand | 64 – 67 | 4 | ||||||||||||||||||||||||||||||||||||||
| Helix | 77 – 79 | 3 | ||||||||||||||||||||||||||||||||||||||
| Helix | 84 – 105 | 22 | ||||||||||||||||||||||||||||||||||||||
| Beta strand | 110 – 116 | 7 | ||||||||||||||||||||||||||||||||||||||
| Helix | 118 – 128 | 11 | ||||||||||||||||||||||||||||||||||||||
| Helix | 133 – 135 | 3 | ||||||||||||||||||||||||||||||||||||||
| Helix | 146 – 151 | 6 | ||||||||||||||||||||||||||||||||||||||
| Beta strand | 152 – 159 | 8 | ||||||||||||||||||||||||||||||||||||||
| Beta strand | 170 – 173 | 4 | ||||||||||||||||||||||||||||||||||||||
| Helix | 191 – 193 | 3 | ||||||||||||||||||||||||||||||||||||||
| Beta strand | 194 – 197 | 4 | ||||||||||||||||||||||||||||||||||||||
| Turn | 203 – 205 | 3 | ||||||||||||||||||||||||||||||||||||||
| Helix | 211 – 214 | 4 | ||||||||||||||||||||||||||||||||||||||
| Helix | 217 – 233 | 17 | ||||||||||||||||||||||||||||||||||||||
Sequences
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References
| [1] | "Acetyl xylan esterase II from Penicillium purpurogenum is similar to an esterase from Trichoderma reesei but lacks a cellulose binding domain." Gutierrez R., Cederlund E., Hjelmqvist L., Peirano A., Herrera F., Ghosh D., Duax W., Joernvall H., Eyzaguirre J. FEBS Lett. 423:35-38(1998) [PubMed: 9506837] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], PROTEIN SEQUENCE OF 28-234. |
| [2] | "Purification and characterization of two acetyl xylan esterases from Penicillium purpurogenum." Egana L., Gutierrez R., Caputo V., Peirano A., Steiner J., Eyzaguirre J. Biotechnol. Appl. Biochem. 24:33-39(1996) [PubMed: 8756392] [Abstract] Cited for: PROTEIN SEQUENCE OF 28-57, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION. |
| [3] | "The acetyl xylan esterase II gene from Penicillium purpurogenum is differentially expressed in several carbon sources, and tightly regulated by pH." Chavez R., Schachter K., Navarro C., Peirano A., Bull P., Eyzaguirre J. Biol. Res. 37:107-113(2004) [PubMed: 15174310] [Abstract] Cited for: INDUCTION. |
| [4] | "Determination of a protein structure by iodination: the structure of iodinated acetylxylan esterase." Ghosh D., Erman M., Sawicki M., Lala P., Weeks D.R., Li N., Pangborn W., Thiel D.J., Joernvall H., Gutierrez R., Eyzaguirre J. Acta Crystallogr. D 55:779-784(1999) [PubMed: 10089308] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.1 ANGSTROMS) OF 28-234. |
| [5] | "Multiple conformations of catalytic serine and histidine in acetylxylan esterase at 0.90 A." Ghosh D., Sawicki M., Lala P., Erman M., Pangborn W., Eyzaguirre J., Gutierrez R., Joernvall H., Thiel D.J. J. Biol. Chem. 276:11159-11166(2001) [PubMed: 11134051] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (0.9 ANGSTROMS) OF 28-234. |
Cross-references
Sequence databases | |||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| AF015285 mRNA. Translation: AAC39371.1. | |||||||||||||||||||||||||
3D structure databases | |||||||||||||||||||||||||
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| ModBase | Search... | ||||||||||||||||||||||||
Enzyme and pathway databases | |||||||||||||||||||||||||
| BRENDA | 3.1.1.72. 15237. | ||||||||||||||||||||||||
Family and domain databases | |||||||||||||||||||||||||
| InterPro | IPR000675. Cutinase. [Graphical view] | ||||||||||||||||||||||||
| Pfam | PF01083. Cutinase. 1 hit. [Graphical view] | ||||||||||||||||||||||||
| ProtoNet | Search... | ||||||||||||||||||||||||
Entry information
| Entry name | AXE2_PENPU | ||||||||
| Accession | Primary (citable) accession number: O59893 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | FPAP (Fungal Proteome Annotation Project) | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with


