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Reviewed, UniProtKB/Swiss-Prot P14293 (PMPB_CANBO)

Last modified March 3, 2009. Version 62. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
    Putative peroxiredoxin-B
    EC=1.11.1.15
Alternative name(s):
    Thioredoxin reductase
    Peroxisomal membrane protein B
    PMP20
    Allergen=Cand b 2
Gene names
Name: PMPB
OrganismCandida boidinii (Yeast)
Taxonomic identifier5477 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesmitosporic SaccharomycetalesCandida

Protein attributes

Sequence length167 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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

Peroxisome membrane; Peripheral membrane protein.

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 processMethanol utilization
   Cellular componentMembrane
Peroxisome
   DiseaseAllergen
   DomainRedox-active center
   Molecular functionOxidoreductase
Peroxidase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processcell redox homeostasis

Inferred from electronic annotation. Source: InterPro

methanol metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentperoxisomal membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionperoxiredoxin activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.1
Chain2 – 167166Putative peroxiredoxin-B
PRO_0000056605

Regions

Domain4 – 167164Thioredoxin
Motif165 – 1673Microbody targeting signal

Sequences

Sequence LengthMass (Da)Tools
P14293-1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: A3909D7C6ACFBFD0

FASTA16718,056
        10         20         30         40         50         60 
MAPIKRGDRF PTTDDVYYIP PEGGEPGAFE LSKFVKTKKF VVVSVPGAFT PPCTEQHLPG 

        70         80         90        100        110        120 
YIKNLPRILS KGVDFVLVIT QNDPFVLKGW KKELGAADAK KLIFVSDPNL KLTKKLGSTI 

       130        140        150        160 
DLSSIGLGTR SGRLALIVNR SGIVEYAAIE NGGEVDVSTA QKIIAKL 

« Hide

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.
PIRB32646.

3D structure databases

HSSPHSSP built from PDB template 1NM3 based on UniProtKB P44758.
ModBaseSearch...

Enzyme and pathway databases

BRENDA1.11.1.15. 675.

Family and domain databases

InterProIPR013740. Redoxin.
IPR017936. Thioredoxin-like.
IPR012335. Thioredoxin_fold.
[Graphical view]
Gene3DG3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.
PfamPF08534. Redoxin. 1 hit.
[Graphical view]
PROSITEPS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePMPB_CANBO
AccessionPrimary (citable) accession number: P14293
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 23, 2007
Last modified: March 3, 2009
This is version 62 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

Allergens

Nomenclature of allergens and list of entries

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