Peroxiredoxin type-2 - Saccharomyces cerevisiae (Baker's yeast)

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Names and origin

Protein names

Recommended 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

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

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Protein attributes

Sequence length	176 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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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: K_M=150 µM for H₂O₂ K_M=45 µM for cumene hydroperoxide K_M=8 µM for tert-butyl hydroperoxide K_M=3 µM for TRX1 K_M=2 µM for TRX2 V_max=20 µmol/min/mg enzyme for H₂O₂ V_max=17 µmol/min/mg enzyme for cumene hydroperoxide V_max=14 µmol/min/mg enzyme for tert-butyl hydroperoxide V_max=17 µmol/min/mg enzyme for TRX1 V_max=16 µmol/min/mg enzyme for TRX2 pH dependence: Optimum pH is 6.5.

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Ontologies

Keywords
Cellular component	Cytoplasm
Domain	Redox-active center
Molecular function	Antioxidant Oxidoreductase Peroxidase
PTM	Acetylation Disulfide bond Phosphoprotein Ubl conjugation
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	cell redox homeostasis Ref.9 Inferred from direct assay. Source: SGD oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW response to metal ion Inferred from mutant phenotype. Source: SGD response to oxidative stress Inferred from genetic interaction. Source: SGD
Cellular component	cytoplasm Ref.9 Inferred from direct assay. Source: SGD plasma membrane enriched fraction Inferred from direct assay. Source: SGD
Molecular function	protein binding Inferred from physical interaction. Source: IntAct thioredoxin peroxidase activity Ref.9 Inferred from direct assay. Source: SGD
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct	Notes
TRX2	P22803	1	EBI-2382,EBI-19598

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.3

Chain

2 – 176

175

Peroxiredoxin type-2

PRO_0000056610

Regions

Domain

9 – 176

168

Thioredoxin

Sites

Active site

Cysteine sulfenic acid (-SOH) intermediate Potential

Amino acid modifications

Modified residue

N-acetylserine Ref.3 Ref.10

Modified residue

Phosphoserine Ref.10

Modified residue

Phosphoserine Ref.11

Modified residue

Phosphoserine Ref.12

Modified residue

171

Phosphoserine Ref.12

Disulfide bond

Interchain (with C-120); in linked form Ref.5

Disulfide bond

120

Interchain (with C-62); in linked form Ref.5

Experimental info

Sequence conflict

I → T AA sequence Ref.5

Sequence conflict

S → V AA sequence Ref.5

Sequence conflict

I → E AA sequence Ref.5

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Sequences

Sequence

Length

Mass (Da)

Tools

P38013-1 [UniParc].

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

176

19,115

        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

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References

	« Hide 'large scale' referencesShow '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. 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.

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Cross-references

Sequence databases
	X89514 Genomic DNA. Translation: CAA61687.1. Z73281 Genomic DNA. Translation: CAA97676.1. U53878 Genomic DNA. Translation: AAB67554.1.
PIR	S64946.
RefSeq	NP_013210.1.
3D structure databases
HSSP	HSSP built from PDB template 1NM3 based on UniProtKB P44758.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:6375N.
IntAct	P38013. 15 interactions.
2-D gel databases
COMPLUYEAST-2DPAGE	P38013.
Proteomic databases
PeptideAtlas	P38013.
PRIDE	P38013.
Genome annotation databases
Ensembl	YLR109W. Saccharomyces cerevisiae. [Contig view]
GeneID	850799.
GenomeReviews	Gene locus YLR109W in contig Y13138_GR.
KEGG	sce:YLR109W.
NMPDR	fig\|4932.3.peg.4202.
Organism-specific databases
CYGD	YLR109w.
SGD	S000004099. AHP1.
Yeast-GFP	Search...
Phylogenomic databases
HOGENOM	P38013.
OMA	P38013. LPGAYTG.
Enzyme and pathway databases
BRENDA	1.11.1.15. 250.
Gene expression databases
ArrayExpress	P38013.
GermOnline	YLR109W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR013740. Redoxin. IPR017936. Thioredoxin-like. IPR012335. Thioredoxin_fold. [Graphical view]
Gene3D	G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.
Pfam	PF08534. Redoxin. 1 hit. [Graphical view]
PROSITE	PS51352. THIOREDOXIN_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	967020.

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Entry information

Entry name

AHP1_YEAST

Accession

Primary (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 status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)

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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

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

2-D gel databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents