Reviewed,
UniProtKB/Swiss-Prot P14293 (PMPB_CANBO)
Last modified
March 3, 2009.
Version 62.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Putative peroxiredoxin-B EC=1.11.1.15 Alternative name(s): Thioredoxin reductase Peroxisomal membrane protein B PMP20 Allergen=Cand b 2 | ||
| Gene names |
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| Organism | Candida boidinii (Yeast) | ||
| Taxonomic identifier | 5477 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › mitosporic Saccharomycetales › Candida |
Protein attributes
| Sequence length | 167 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 | Its function is very likely to be related to the metabolism of methanol. |
| Catalytic activity | 2 R'-SH + ROOH = R'-S-S-R' + H2O + ROH. |
| Subcellular location | |
| Induction | By methanol. |
| Allergenic properties | Causes an allergic reaction in human. Shares common IgE-binding epitopes with allergen Asp f 3 of Aspergillus fumigatus. |
| Sequence similarities | Belongs to the peroxiredoxin 2 family. Contains 1 thioredoxin domain. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Methanol utilization |
| Cellular component | Membrane Peroxisome |
| Disease | Allergen |
| Domain | Redox-active center |
| Molecular function | Oxidoreductase Peroxidase |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | cell redox homeostasis Inferred from electronic annotation. Source: InterPro methanol metabolic processInferred from electronic annotation. Source: UniProtKB-KW oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | peroxisomal membrane Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | peroxiredoxin activity Inferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
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References
| [1] | "Two genes encode the major membrane-associated protein of methanol-induced peroxisomes from Candida boidinii." Garrard L.J., Goodman J.M. J. Biol. Chem. 264:13929-13937(1989) [PubMed: 2760051] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-26. Strain: ATCC 32195. |
| [2] | "Allergens of Aspergillus fumigatus and Candida boidinii share IgE-binding epitopes." Hemmann S., Blaser K., Crameri R. Am. J. Respir. Crit. Care Med. 156:1956-1962(1997) [PubMed: 9412580] [Abstract] Cited for: CROSS-REACTIVITY WITH ASP F 3. |
Cross-references
Sequence databases | |
|---|---|
| J04985 Genomic DNA. Translation: AAA34358.1. | |
| PIR | B32646. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1NM3 based on UniProtKB P44758. |
| ModBase | Search... |
Enzyme and pathway databases | |
| BRENDA | 1.11.1.15. 675. |
Family and domain databases | |
| InterPro | IPR013740. Redoxin. IPR017936. Thioredoxin-like. IPR012335. Thioredoxin_fold. [Graphical view] |
| Gene3D | G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit. |
| Pfam | PF08534. Redoxin. 1 hit. [Graphical view] |
| PROSITE | PS51352. THIOREDOXIN_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | PMPB_CANBO | ||||||||
| Accession | Primary (citable) accession number: P14293 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | FPAP (Fungal Proteome Annotation Project) | ||||||||
Relevant documents
| Allergens Nomenclature of allergens and list of entries |
| SIMILARITY comments Index of protein domains and families |

Clusters with


