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Protein

Putative peroxiredoxin pmp20

Gene

pmp20

Organism
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

2 R'-SH + ROOH = R'-S-S-R' + H2O + ROH.

GO - Molecular functioni

  • IgE binding Source: ASPGD
  • peroxidase activity Source: UniProtKB-KW
  • peroxiredoxin activity Source: UniProtKB-EC

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase, Peroxidase

Names & Taxonomyi

Protein namesi
Recommended name:
Putative peroxiredoxin pmp20 (EC:1.11.1.15)
Alternative name(s):
Peroxisomal membrane protein pmp20
Thioredoxin reductase
Allergen: Asp f 3
Gene namesi
Name:pmp20
ORF Names:AFUA_6G02280
OrganismiNeosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
Taxonomic identifieri330879 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
Proteomesi
  • UP000002530 Componenti: Chromosome 6

Organism-specific databases

EuPathDBiFungiDB:Afu6g02280.

Subcellular locationi

GO - Cellular componenti

  • intracellular Source: ASPGD
  • peroxisome Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Peroxisome

Pathology & Biotechi

Allergenic propertiesi

Causes an allergic reaction in human. Shares common IgE-binding epitopes with allergen Cand b 2 of Candida boidinii.

Keywords - Diseasei

Allergen

Protein family/group databases

Allergomei3121. Asp f 3.0101.
73. Asp f 3.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000566031 – 168Putative peroxiredoxin pmp20Add BLAST168

Proteomic databases

PRIDEiO43099.

Interactioni

GO - Molecular functioni

  • IgE binding Source: ASPGD

Structurei

Secondary structure

1168
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi15 – 18Combined sources4
Helixi23 – 25Combined sources3
Beta strandi35 – 38Combined sources4
Helixi39 – 42Combined sources4
Turni43 – 45Combined sources3
Beta strandi46 – 52Combined sources7
Helixi59 – 63Combined sources5
Helixi65 – 78Combined sources14
Beta strandi83 – 90Combined sources8
Helixi92 – 101Combined sources10
Beta strandi108 – 113Combined sources6
Helixi115 – 117Combined sources3
Helixi118 – 122Combined sources5
Beta strandi134 – 140Combined sources7
Beta strandi143 – 149Combined sources7
Helixi161 – 165Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5J9BX-ray2.10A/B2-168[»]
5J9CX-ray1.96A/B2-168[»]
ProteinModelPortaliO43099.
SMRiO43099.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini4 – 158ThioredoxinPROSITE-ProRule annotationAdd BLAST155

Sequence similaritiesi

Belongs to the peroxiredoxin 2 family.Curated
Contains 1 thioredoxin domain.PROSITE-ProRule annotation

Keywords - Domaini

Redox-active center

Phylogenomic databases

HOGENOMiHOG000255884.
InParanoidiO43099.
KOiK14171.
OMAiSYIPWSE.
OrthoDBiEOG092C4YDK.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR013740. Redoxin.
IPR012336. Thioredoxin-like_fold.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamiPF08534. Redoxin. 1 hit.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 1 hit.
PROSITEiPS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O43099-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGLKAGDSF PSDVVFSYIP WSEDKGEITA CGIPINYNAS KEWADKKVIL
60 70 80 90 100
FALPGAFTPV CSARHVPEYI EKLPEIRAKG VDVVAVLAYN DAYVMSAWGK
110 120 130 140 150
ANQVTGDDIL FLSDPDARFS KSIGWADEEG RTKRYALVID HGKITYAALE
160
PAKNHLEFSS AETVLKHL
Length:168
Mass (Da):18,453
Last modified:June 1, 1998 - v1
Checksum:iAFFCD72C5A1CCBB2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U58050 mRNA. Translation: AAB95638.1.
AAHF01000012 Genomic DNA. Translation: EAL85811.1.
RefSeqiXP_747849.1. XM_742756.1.

Genome annotation databases

EnsemblFungiiCADAFUAT00000470; CADAFUAP00000470; CADAFUAG00000470.
GeneIDi3505266.
KEGGiafm:AFUA_6G02280.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U58050 mRNA. Translation: AAB95638.1.
AAHF01000012 Genomic DNA. Translation: EAL85811.1.
RefSeqiXP_747849.1. XM_742756.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5J9BX-ray2.10A/B2-168[»]
5J9CX-ray1.96A/B2-168[»]
ProteinModelPortaliO43099.
SMRiO43099.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

Allergomei3121. Asp f 3.0101.
73. Asp f 3.

Proteomic databases

PRIDEiO43099.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCADAFUAT00000470; CADAFUAP00000470; CADAFUAG00000470.
GeneIDi3505266.
KEGGiafm:AFUA_6G02280.

Organism-specific databases

EuPathDBiFungiDB:Afu6g02280.

Phylogenomic databases

HOGENOMiHOG000255884.
InParanoidiO43099.
KOiK14171.
OMAiSYIPWSE.
OrthoDBiEOG092C4YDK.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR013740. Redoxin.
IPR012336. Thioredoxin-like_fold.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamiPF08534. Redoxin. 1 hit.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 1 hit.
PROSITEiPS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPMP20_ASPFU
AccessioniPrimary (citable) accession number: O43099
Secondary accession number(s): Q4WCS7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: June 1, 1998
Last modified: November 30, 2016
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Allergens
    Nomenclature of allergens and list of entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.