Peroxiredoxin type-2 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P38013 (AHP1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 139. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

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

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

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, an 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: K_M=150 µM for H₂O₂ Ref.6 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.

Ontologies

Keywords
Cellular component	Cytoplasm
Domain	Redox-active center
Molecular function	Antioxidant Oxidoreductase Peroxidase
PTM	Acetylation Disulfide bond Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cell redox homeostasis Inferred from mutant phenotype Ref.10. Source: SGD cellular response to oxidative stress Inferred from genetic interaction PubMed 15051715. Source: SGD response to metal ion Inferred from mutant phenotype PubMed 12270680. Source: SGD
Cellular_component	cytoplasm Inferred from direct assay Ref.10. Source: SGD plasma membrane Inferred from direct assay PubMed 16622836. Source: SGD
Molecular_function	thioredoxin peroxidase activity Inferred from direct assay Ref.10. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.4

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.4 Ref.11

Modified residue

Phosphoserine Ref.11

Modified residue

Phosphoserine Ref.12

Modified residue

Phosphoserine Ref.13

Modified residue

171

Phosphoserine Ref.13

Disulfide bond

Interchain (with C-120); in linked form Ref.6

Disulfide bond

120

Interchain (with C-62); in linked form Ref.6

Experimental info

Sequence conflict

I → T AA sequence Ref.6

Sequence conflict

S → V AA sequence Ref.6

Sequence conflict

I → E AA sequence Ref.6

Secondary structure

176

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P38013 [UniParc].

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

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

« Hide

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] [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. Hoheisel J.D. Nature 387:87-90(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[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, 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]	"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] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION AT SER-2, MASS SPECTROMETRY. Strain: YAL6B.
[12]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22, MASS SPECTROMETRY.
[13]	"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 AND SER-171, MASS SPECTROMETRY.
[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.

PIR

S64946.

RefSeq

NP_013210.1. NM_001181996.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
4DSQ	X-ray	2.40	A/B/C/D	1-176	[»]
4DSR	X-ray	2.91	A/B/C/D	1-176	[»]
4DSS	X-ray	2.10	A	1-176	[»]
4H86	X-ray	2.00	A	1-176	[»]

ProteinModelPortal

P38013.

SMR

P38013. Positions 1-176.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-6375N.

IntAct

P38013. 15 interactions.

MINT

MINT-705985.

STRING

4932.YLR109W.

2D gel databases

COMPLUYEAST-2DPAGE

P38013.

Proteomic databases

PaxDb

P38013.

PeptideAtlas

P38013.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YLR109W; YLR109W; YLR109W.

GeneID

850799.

KEGG

sce:YLR109W.

Organism-specific databases

SGD

S000004099. AHP1.

Phylogenomic databases

eggNOG

COG0678.

GeneTree

ENSGT00390000018173.

HOGENOM

HOG000255884.

K14171.

OMA

CSNQHVP.

OrthoDB

EOG4H75N5.

Enzyme and pathway databases

BioCyc

YEAST:YLR109W-MONOMER.

Gene expression databases

Genevestigator

P38013.

GermOnline

YLR109W. Saccharomyces cerevisiae.

Family and domain databases

Gene3D

3.40.30.10. 1 hit.

InterPro

IPR013740. Redoxin.
IPR012336. Thioredoxin-like_fold.
[Graphical view]

Pfam

PF08534. Redoxin. 1 hit.
[Graphical view]

SUPFAM

SSF52833. Thiordxn-like_fd. 1 hit.

PROSITE

PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

967020.

Entry information

Entry name

AHP1_YEAST

Accession

Primary (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:	May 29, 2013
This is version 139 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

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

Yeast chromosome XII

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents