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Reviewed, UniProtKB/Swiss-Prot P38013 (AHP1_YEAST)

Last modified June 16, 2009. Version 99. 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 · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Peroxiredoxin type-2
    EC=1.11.1.15
Alternative name(s):
    Peroxiredoxin type II
    Peroxisomal alkyl hydroperoxide reductase
    Thioredoxin peroxidase type II
    Thioredoxin reductase type II
    TPx type II
    Cytoplasmic thiol peroxidase 3
      Short name=cTPx 3
    Thiol-specific antioxidant II
      Short name=TSA II
    AHPC1
Gene names
Name: AHP1
Ordered Locus Names: YLR109W
ORF Names: L2916, L9354.5
OrganismSaccharomyces cerevisiae (Baker's yeast) [Complete proteome]
Taxonomic identifier4932 [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.5

Subcellular location

Cytoplasm. Ref.9

Induction

By H2O2. Ref.9

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, an ubiquitin-like protein.

Miscellaneous

Present with 16228 molecules/cell in log phase SD medium. Ref.14

Sequence similarities

Belongs to the peroxiredoxin 2 family.

Contains 1 thioredoxin domain.

Biophysicochemical properties

Kinetic parameters:

KM=150 µM for H2O2

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.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

TRX2P228031EBI-2382,EBI-19598

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.3
Chain2 – 176175Peroxiredoxin type-2
PRO_0000056610

Regions

Domain9 – 176168Thioredoxin

Sites

Active site621Cysteine sulfenic acid (-SOH) intermediate Potential

Amino acid modifications

Modified residue21N-acetylserine Ref.3 Ref.10
Modified residue21Phosphoserine Ref.10
Modified residue221Phosphoserine Ref.11
Modified residue591Phosphoserine Ref.12
Modified residue1711Phosphoserine Ref.12
Disulfide bond62Interchain (with C-120); in linked form Ref.5
Disulfide bond120Interchain (with C-62); in linked form Ref.5

Experimental info

Sequence conflict211I → T AA sequence Ref.5
Sequence conflict651S → V AA sequence Ref.5
Sequence conflict871I → E AA sequence Ref.5

Sequences

Sequence LengthMass (Da)Tools
P38013-1 [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: 9090053] [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: 9169871] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204511 / S288c / AB972.
[3]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, MASS SPECTROMETRY.
[4]"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: 14555475] [Abstract]
Cited for: PROTEIN SEQUENCE OF 8-15; 33-41; 80-102 AND 125-176, CONJUGATION TO URM1.
[5]"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: 9888818] [Abstract]
Cited for: PROTEIN SEQUENCE OF 16-41; 49-68; 82-96; 114-123 AND 142-150, POST-TRANSLATIONAL MODIFICATION, DISULFIDE BONDS, BIOPHYSICOCHEMICAL PROPERTIES.
[6]"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: 7895733] [Abstract]
Cited for: PROTEIN SEQUENCE OF 82-99.
Strain: ATCC 204508 / S288c.
[7]"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: 9988687] [Abstract]
Cited for: CHARACTERIZATION.
[8]"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: 10635552] [Abstract]
Cited for: CHARACTERIZATION.
[9]"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: 10681558] [Abstract]
Cited for: CHARACTERIZATION, INDUCTION, SUBCELLULAR LOCATION.
[10]"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway."
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N.
Mol. Cell. Proteomics 4:310-327(2005) [PubMed: 15665377] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION AT SER-2, MASS SPECTROMETRY.
[11]"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed: 17287358] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22, MASS SPECTROMETRY.
[12]"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: 18407956] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-59 AND SER-171, MASS SPECTROMETRY.
[13]"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: 14640681] [Abstract]
Cited for: 3D-STRUCTURE MODELING, STRUCTURE BY NMR.
[14]"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: 14562106] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

X89514 Genomic DNA. Translation: CAA61687.1.
Z73281 Genomic DNA. Translation: CAA97676.1.
U53878 Genomic DNA. Translation: AAB67554.1.
PIRS64946.
RefSeqNP_013210.1.

3D structure databases

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

Protein-protein interaction databases

DIPDIP:6375N.
IntActP38013. 15 interactions.

2-D gel databases

COMPLUYEAST-2DPAGEP38013.

Proteomic databases

PeptideAtlasP38013.
PRIDEP38013.

Genome annotation databases

EnsemblYLR109W. Saccharomyces cerevisiae. [Contig view]
GeneID850799.
GenomeReviewsGene locus YLR109W in contig Y13138_GR.
KEGGsce:YLR109W.
NMPDRfig|4932.3.peg.4202.

Organism-specific databases

CYGDYLR109w.
SGDS000004099. AHP1.
Yeast-GFPSearch...

Phylogenomic databases

HOGENOMP38013.
OMAP38013. LPGAYTG.

Enzyme and pathway databases

BRENDA1.11.1.15. 250.

Gene expression databases

ArrayExpressP38013.
GermOnlineYLR109W. Saccharomyces cerevisiae.

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...

Other Resources

NextBio967020.

Entry information

Entry nameAHP1_YEAST
AccessionPrimary (citable) accession number: P38013
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: January 23, 2007
Last modified: June 16, 2009
This is version 99 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Yeast

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

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents