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P38013 (AHP1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 146. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Peroxiredoxin type-2

EC=1.11.1.15
Alternative name(s):
AHPC1
Cytoplasmic thiol peroxidase 3
Short name=cTPx 3
Peroxiredoxin type II
Peroxisomal alkyl hydroperoxide reductase
TPx type II
Thiol-specific antioxidant II
Short name=TSA II
Thioredoxin peroxidase type II
Thioredoxin reductase type II
Gene names
Name:AHP1
Ordered Locus Names:YLR109W
ORF Names:L2916, L9354.5
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length176 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Thiol-specific antioxidant protein with alkyl hydroperoxidase activity. Involved in osmotic stress resistance and detoxification of the cell. Preferentially eliminates organic peroxides rather than H2O2. Involved in cellular Mn2+ homeostasis.

Catalytic activity

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

Subunit structure

Homodimer; disulfide-linked, upon oxidation. Ref.6

Subcellular location

Cytoplasm Ref.10.

Induction

By H2O2. Ref.10

Post-translational modification

The Cys-62-SH group is the primary site of oxidation by H2O2, and the oxidized Cys-62 (probably Cys-SOH) rapidly reacts with Cys-120-SH of the other subunit to form an intermolecular disulfide. This disulfide is subsequently reduced by thioredoxin to restore the reduced active form of the enzyme.

Conjugated to URM1, a ubiquitin-like protein.

Miscellaneous

Present with 16228 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the peroxiredoxin 2 family.

Contains 1 thioredoxin domain.

Biophysicochemical properties

Kinetic parameters:

KM=150 µM for H2O2 Ref.6

KM=45 µM for cumene hydroperoxide

KM=8 µM for tert-butyl hydroperoxide

KM=3 µM for TRX1

KM=2 µM for TRX2

Vmax=20 µmol/min/mg enzyme for H2O2

Vmax=17 µmol/min/mg enzyme for cumene hydroperoxide

Vmax=14 µmol/min/mg enzyme for tert-butyl hydroperoxide

Vmax=17 µmol/min/mg enzyme for TRX1

Vmax=16 µmol/min/mg enzyme for TRX2

pH dependence:

Optimum pH is 6.5.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.4
Chain2 – 176175Peroxiredoxin type-2
PRO_0000056610

Regions

Domain9 – 176168Thioredoxin

Sites

Active site621Cysteine sulfenic acid (-SOH) intermediate Potential

Amino acid modifications

Modified residue21N-acetylserine Ref.4
Modified residue281Phosphoserine Ref.12
Modified residue591Phosphoserine Ref.11
Modified residue1161Phosphoserine Ref.12
Disulfide bond62Interchain (with C-120); in linked form Ref.6
Disulfide bond120Interchain (with C-62); in linked form Ref.6

Experimental info

Sequence conflict211I → T AA sequence Ref.6
Sequence conflict651S → V AA sequence Ref.6
Sequence conflict871I → E AA sequence Ref.6

Secondary structure

....................................... 176
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P38013 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 11B730781306A015

FASTA17619,115
        10         20         30         40         50         60 
MSDLVNKKFP AGDYKFQYIA ISQSDADSES CKMPQTVEWS KLISENKKVI ITGAPAAFSP 

        70         80         90        100        110        120 
TCTVSHIPGY INYLDELVKE KEVDQVIVVT VDNPFANQAW AKSLGVKDTT HIKFASDPGC 

       130        140        150        160        170 
AFTKSIGFEL AVGDGVYWSG RWAMVVENGI VTYAAKETNP GTDVTVSSVE SVLAHL 

« Hide

References

« Hide 'large scale' references
[1]"Sequence analysis of a 37.6 kbp cosmid clone from the right arm of Saccharomyces cerevisiae chromosome XII, carrying YAP3, HOG1, SNR6, tRNA-Arg3 and 23 new open reading frames, among which several homologies to proteins involved in cell division control and to mammalian growth factors and other animal proteins are found."
Verhasselt P., Volckaert G.
Yeast 13:241-250(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 90840 / EAY235 / FY23.
[2]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."
Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H. expand/collapse author list , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D.
Nature 387:87-90(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]Bienvenut W.V., Peters C.
Submitted (MAY-2005) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-8; 16-48; 80-102 AND 114-176, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY.
[5]"Attachment of the ubiquitin-related protein Urm1p to the antioxidant protein Ahp1p."
Goehring A.S., Rivers D.M., Sprague G.F. Jr.
Eukaryot. Cell 2:930-936(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 8-15; 33-41; 80-102 AND 125-176, CONJUGATION TO URM1.
[6]"Purification and characterization of a second type thioredoxin peroxidase (type II TPx) from Saccharomyces cerevisiae."
Jeong J.S., Kwon S.J., Kang S.W., Rhee S.G., Kim K.
Biochemistry 38:776-783(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 16-41; 49-68; 82-96; 114-123 AND 142-150, POST-TRANSLATIONAL MODIFICATION, DISULFIDE BONDS, BIOPHYSICOCHEMICAL PROPERTIES.
[7]"Protein identifications for a Saccharomyces cerevisiae protein database."
Garrels J.I., Futcher B., Kobayashi R., Latter G.I., Schwender B., Volpe T., Warner J.R., McLaughlin C.S.
Electrophoresis 15:1466-1486(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 82-99.
Strain: ATCC 204508 / S288c.
[8]"A new antioxidant with alkyl hydroperoxide defense properties in yeast."
Lee J., Spector D., Godon C., Labarre J., Toledano M.B.
J. Biol. Chem. 274:4537-4544(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[9]"Involvement of thioredoxin peroxidase type II (Ahp1p) of Saccharomyces cerevisiae in Mn2+ homeostasis."
Farcasanu I.C., Hirata D., Tsuchiya E., Mizuta K., Miyakawa T.
Biosci. Biotechnol. Biochem. 63:1871-1881(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[10]"Distinct physiological functions of thiol peroxidase isoenzymes in Saccharomyces cerevisiae."
Park S.G., Cha M.-K., Jeong W., Kim I.-H.
J. Biol. Chem. 275:5723-5732(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION, INDUCTION, SUBCELLULAR LOCATION.
[11]"A multidimensional chromatography technology for in-depth phosphoproteome analysis."
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-59, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28 AND SER-116, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"Sites of ubiquitin attachment in Saccharomyces cerevisiae."
Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"Characterization of the yeast peroxiredoxin Ahp1 in its reduced active and overoxidized inactive forms using NMR."
Trivelli X., Krimm I., Ebel C., Verdoucq L., Prouzet-Mauleon V., Chartier Y., Tsan P., Lauquin G., Meyer Y., Lancelin J.-M.
Biochemistry 42:14139-14149(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: 3D-STRUCTURE MODELING, STRUCTURE BY NMR.
[15]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X89514 Genomic DNA. Translation: CAA61687.1.
Z73281 Genomic DNA. Translation: CAA97676.1.
U53878 Genomic DNA. Translation: AAB67554.1.
BK006945 Genomic DNA. Translation: DAA09425.1.
PIRS64946.
RefSeqNP_013210.1. NM_001181996.1.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalP38013.
SMRP38013. Positions 1-176.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid31382. 57 interactions.
DIPDIP-6375N.
IntActP38013. 4 interactions.
MINTMINT-705985.
STRING4932.YLR109W.

2D gel databases

COMPLUYEAST-2DPAGEP38013.

Proteomic databases

PaxDbP38013.
PeptideAtlasP38013.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYLR109W; YLR109W; YLR109W.
GeneID850799.
KEGGsce:YLR109W.

Organism-specific databases

SGDS000004099. AHP1.

Phylogenomic databases

eggNOGCOG0678.
GeneTreeENSGT00390000018173.
HOGENOMHOG000255884.
KOK14171.
OMAAEILCIS.
OrthoDBEOG7X3R3F.

Enzyme and pathway databases

BioCycYEAST:YLR109W-MONOMER.

Gene expression databases

GenevestigatorP38013.

Family and domain databases

Gene3D3.40.30.10. 1 hit.
InterProIPR013740. Redoxin.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamPF08534. Redoxin. 1 hit.
[Graphical view]
SUPFAMSSF52833. SSF52833. 1 hit.
PROSITEPS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio967020.
PROP38013.

Entry information

Entry nameAHP1_YEAST
AccessionPrimary (citable) accession number: P38013
Secondary accession number(s): D6VYA9
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 146 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XII

Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references