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Protein

Putative peroxiredoxin-A

Gene

PMPA

Organism
Candida boidinii (Yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events.By similarity

Miscellaneous

The active site is a conserved redox-active cysteine residue, the peroxidatic cysteine (C(P)), which makes the nucleophilic attack on the peroxide substrate. The peroxide oxidizes the C(P)-SH to cysteine sulfenic acid (C(P)-SOH), which then reacts with another cysteine residue, the resolving cysteine (C(R)), to form a disulfide bridge. The disulfide is subsequently reduced by an appropriate electron donor to complete the catalytic cycle. In this 1-Cys peroxiredoxin, no C(R) is present and C(P) instead forms a disulfide with a cysteine from another protein or with a small thiol molecule.Curated

Catalytic activityi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei53Cysteine sulfenic acid (-SOH) intermediateBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionAntioxidant, Oxidoreductase, Peroxidase
Biological processMethanol utilization

Names & Taxonomyi

Protein namesi
Recommended name:
Putative peroxiredoxin-A (EC:1.11.1.15)
Alternative name(s):
PMP20
Peroxisomal membrane protein A
Thioredoxin reductase
Allergen: Cand b 2
Gene namesi
Name:PMPA
OrganismiCandida boidinii (Yeast)
Taxonomic identifieri5477 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesPichiaceaeOgataeaOgataea/Candida clade

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Membrane, Peroxisome

Pathology & Biotechi

Allergenic propertiesi

Causes an allergic reaction in human. Shares common IgE-binding epitopes with allergen Asp f 3 of Aspergillus fumigatus.1 Publication

Keywords - Diseasei

Allergen

Protein family/group databases

Allergomei178. Cand b 2.
3175. Cand b 2.0101.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00000566042 – 167Putative peroxiredoxin-AAdd BLAST166

Proteomic databases

PRIDEiP14292.

Expressioni

Inductioni

By methanol.1 Publication

Structurei

3D structure databases

ProteinModelPortaliP14292.
SMRiP14292.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini4 – 167ThioredoxinPROSITE-ProRule annotationAdd BLAST164

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi165 – 167Microbody targeting signal3

Sequence similaritiesi

Belongs to the peroxiredoxin family. Prx5 subfamily.Curated

Keywords - Domaini

Redox-active center

Family and domain databases

InterProiView protein in InterPro
IPR013740. Redoxin.
IPR012336. Thioredoxin-like_fold.
IPR013766. Thioredoxin_domain.
PfamiView protein in Pfam
PF08534. Redoxin. 1 hit.
SUPFAMiSSF52833. SSF52833. 1 hit.
PROSITEiView protein in PROSITE
PS51352. THIOREDOXIN_2. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P14292-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAPIKRGDRF PTTDDVYYIP PEGGEPGPLE LSKFVKTKKF VVVSVPGAFT
60 70 80 90 100
PPCTEQHLPG YIKNLPRILS KGVDFVLVIS QNDPFVLKGW KKELGAADAK
110 120 130 140 150
KLVFVSDPNL KLTKKLGSTI DLSAIGLGTR SGRLALIVNR SGIVEYAAIE
160
NGGEVDVSTA QKIIAKL
Length:167
Mass (Da):18,004
Last modified:January 23, 2007 - v3
Checksum:iBB6474B84834D0D5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04984 Genomic DNA. Translation: AAA34357.1.
PIRiA32646.

Similar proteinsi

Entry informationi

Entry nameiPMPA_CANBO
AccessioniPrimary (citable) accession number: P14292
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 23, 2007
Last modified: August 30, 2017
This is version 92 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. Allergens
    Nomenclature of allergens and list of entries
  2. SIMILARITY comments
    Index of protein domains and families