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Protein

Peroxiredoxin AHP1

Gene

AHP1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 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. Preferentially eliminates organic peroxides rather than hydrogen peroxide (PubMed:10391912, PubMed:9988687, PubMed:10681558). Relays alkyl hydroperoxides as a signal to the transcription factor CAD1/YAP2 by inducing the formation of intramolecular disulfide bonds in CAD1, which causes its nuclear accumulation and activation (PubMed:20145245). Involved in cellular Mn2+ homeostasis (PubMed:10635552).5 Publications

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 typical 2-Cys Prx, C(R) is provided by the other dimeric subunit to form an intersubunit disulfide. The disulfide is subsequently reduced by thioredoxin.1 Publication
Present with 16228 molecules/cell in log phase SD medium.1 Publication

Catalytic activityi

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

Kineticsi

  1. KM=150 µM for H2O21 Publication
  2. KM=14 µM for H2O21 Publication
  3. KM=8 µM for cumene hydroperoxide1 Publication
  4. KM=45 µM for tert-butyl hydroperoxide1 Publication
  5. KM=76.9 µM for tert-butyl hydroperoxide1 Publication
  6. KM=3 µM for TRX11 Publication
  7. KM=2 µM for TRX21 Publication
  8. KM=1.3 µM for TRX21 Publication
  1. Vmax=20 µmol/min/mg enzyme for H2O21 Publication
  2. Vmax=14 µmol/min/mg enzyme for cumene hydroperoxide1 Publication
  3. Vmax=17 µmol/min/mg enzyme for tert-butyl hydroperoxide1 Publication
  4. Vmax=17 µmol/min/mg enzyme for TRX11 Publication
  5. Vmax=16 µmol/min/mg enzyme for TRX21 Publication

pH dependencei

Optimum pH is 6.5.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei62Cysteine sulfenic acid (-SOH) intermediate1 Publication1

GO - Molecular functioni

  • thioredoxin peroxidase activity Source: SGD

GO - Biological processi

  • cell redox homeostasis Source: SGD
  • cellular response to oxidative stress Source: SGD
  • response to metal ion Source: SGD

Keywordsi

Molecular functionAntioxidant, Oxidoreductase, Peroxidase

Enzyme and pathway databases

BioCyciYEAST:YLR109W-MONOMER.
ReactomeiR-SCE-3299685. Detoxification of Reactive Oxygen Species.
R-SCE-5628897. TP53 Regulates Metabolic Genes.

Names & Taxonomyi

Protein namesi
Recommended name:
Peroxiredoxin AHP1Curated (EC:1.11.1.152 Publications)
Short name:
Prx
Alternative name(s):
Alkyl hydroperoxide reductase1 Publication
Short name:
AHPC1
Cytoplasmic thiol peroxidase 31 Publication
Short name:
cTPx 31 Publication
Thiol-specific antioxidant II1 Publication
Short name:
TSA II1 Publication
Thioredoxin peroxidase type II1 Publication
Short name:
TPx type II
Gene namesi
Name:AHP11 Publication
Ordered Locus Names:YLR109W
ORF Names:L2916, L9354.5
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XII

Organism-specific databases

EuPathDBiFungiDB:YLR109W.
SGDiS000004099. AHP1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: SGD

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi31C → S: Abolishes catalytic activity. 1 Publication1
Mutagenesisi32K → R: Prevents urmylation of AHP1. 1 Publication1
Mutagenesisi62C → S: Abolishes catalytic activity. 1 Publication1
Mutagenesisi120C → S: No effect on tert-butyl hydroperoxide consumption. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00000566102 – 176Peroxiredoxin AHP1Add BLAST175

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserine1 Publication1
Modified residuei28PhosphoserineCombined sources1
Disulfide bondi31Interchain (with C-31 in TRX2); transient1 Publication
Disulfide bondi31Interchain (with C-62); in linked formCombined sources1 Publication
Cross-linki32Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in URM1)1 Publication
Cross-linki48Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Modified residuei59PhosphoserineCombined sources1
Disulfide bondi62Interchain (with C-31); in linked formCombined sources1 Publication
Cross-linki113Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Modified residuei116PhosphoserineCombined sources1

Post-translational modificationi

Conjugated to URM1, a ubiquitin-like protein.2 Publications

Keywords - PTMi

Acetylation, Disulfide bond, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP38013.
PRIDEiP38013.
TopDownProteomicsiP38013.

2D gel databases

COMPLUYEAST-2DPAGEiP38013.

PTM databases

iPTMnetiP38013.

Expressioni

Inductioni

By H2O2.1 Publication

Interactioni

Subunit structurei

Homodimer; disulfide-linked, upon oxidation.4 Publications

Protein-protein interaction databases

BioGridi31382. 101 interactors.
DIPiDIP-6375N.
IntActiP38013. 4 interactors.
MINTiMINT-705985.
STRINGi4932.YLR109W.

Structurei

Secondary structure

1176
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni3 – 6Combined sources4
Beta strandi15 – 18Combined sources4
Beta strandi23 – 25Combined sources3
Beta strandi26 – 28Combined sources3
Helixi29 – 31Combined sources3
Beta strandi35 – 38Combined sources4
Helixi39 – 45Combined sources7
Beta strandi47 – 53Combined sources7
Helixi60 – 64Combined sources5
Helixi67 – 80Combined sources14
Beta strandi85 – 92Combined sources8
Helixi94 – 103Combined sources10
Beta strandi110 – 116Combined sources7
Helixi118 – 120Combined sources3
Helixi121 – 125Combined sources5
Beta strandi129 – 133Combined sources5
Beta strandi136 – 139Combined sources4
Beta strandi141 – 147Combined sources7
Beta strandi150 – 156Combined sources7
Turni160 – 162Combined sources3
Helixi169 – 173Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4DSQX-ray2.40A/B/C/D1-176[»]
4DSRX-ray2.91A/B/C/D1-176[»]
4DSSX-ray2.10A1-176[»]
4H86X-ray2.00A1-176[»]
4OWYX-ray2.20A/B/C/D1-176[»]
ProteinModelPortaliP38013.
SMRiP38013.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini9 – 176ThioredoxinPROSITE-ProRule annotationAdd BLAST168

Sequence similaritiesi

Belongs to the peroxiredoxin family. Prx5 subfamily.Curated

Keywords - Domaini

Redox-active center

Phylogenomic databases

GeneTreeiENSGT00390000018173.
HOGENOMiHOG000255884.
InParanoidiP38013.
KOiK14171.
OMAiQRYAMVV.
OrthoDBiEOG092C4YDK.

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.

P38013-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSDLVNKKFP AGDYKFQYIA ISQSDADSES CKMPQTVEWS KLISENKKVI
60 70 80 90 100
ITGAPAAFSP TCTVSHIPGY INYLDELVKE KEVDQVIVVT VDNPFANQAW
110 120 130 140 150
AKSLGVKDTT HIKFASDPGC AFTKSIGFEL AVGDGVYWSG RWAMVVENGI
160 170
VTYAAKETNP GTDVTVSSVE SVLAHL
Length:176
Mass (Da):19,115
Last modified:January 23, 2007 - v4
Checksum:i11B730781306A015
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti21I → T AA sequence (PubMed:9888818).Curated1
Sequence conflicti65S → V AA sequence (PubMed:9888818).Curated1
Sequence conflicti87I → E AA sequence (PubMed:9888818).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X89514 Genomic DNA. Translation: CAA61687.1.
Z73281 Genomic DNA. Translation: CAA97676.1.
U53878 Genomic DNA. Translation: AAB67554.1.
BK006945 Genomic DNA. Translation: DAA09425.1.
PIRiS64946.
RefSeqiNP_013210.1. NM_001181996.1.

Genome annotation databases

EnsemblFungiiYLR109W; YLR109W; YLR109W.
GeneIDi850799.
KEGGisce:YLR109W.

Similar proteinsi

Entry informationi

Entry nameiAHP1_YEAST
AccessioniPrimary (citable) accession number: P38013
Secondary accession number(s): D6VYA9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: January 23, 2007
Last modified: August 30, 2017
This is version 175 of the entry and version 4 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Caution

Biochemical and mutational analysis assigned Cys-120 as the resolving cysteine (C(R)) (PubMed:9888818). However, crystal structures showed that Cys-120 is deeply buried within the protein and revealed formation of a disulfide bond between the peroxidatic cysteine Cys-62 and the therefore more likely C(R) Cys-31 (PubMed:22474296, Ref. 21).3 Publications

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XII
    Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names