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P38013

- AHP1_YEAST

UniProt

P38013 - AHP1_YEAST

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Protein
Peroxiredoxin type-2
Gene
AHP1, YLR109W, L2916, L9354.5
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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 activityi

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

Kineticsi

  1. KM=150 µM for H2O21 Publication
  2. KM=45 µM for cumene hydroperoxide
  3. KM=8 µM for tert-butyl hydroperoxide
  4. KM=3 µM for TRX1
  5. 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 dependencei

Optimum pH is 6.5.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei62 – 621Cysteine sulfenic acid (-SOH) intermediate Reviewed prediction

GO - Molecular functioni

  1. thioredoxin peroxidase activity Source: SGD
Complete GO annotation...

GO - Biological processi

  1. cell redox homeostasis Source: SGD
  2. cellular response to oxidative stress Source: SGD
  3. response to metal ion Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Antioxidant, Oxidoreductase, Peroxidase

Enzyme and pathway databases

BioCyciYEAST:YLR109W-MONOMER.

Names & Taxonomyi

Protein namesi
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 namesi
Name:AHP1
Ordered Locus Names:YLR109W
ORF Names:L2916, L9354.5
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome XII

Organism-specific databases

SGDiS000004099. AHP1.

Subcellular locationi

Cytoplasm 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 176175Peroxiredoxin type-2
PRO_0000056610Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Modified residuei28 – 281Phosphoserine1 Publication
Modified residuei59 – 591Phosphoserine1 Publication
Disulfide bondi62 – 62Interchain (with C-120); in linked form1 Publication
Modified residuei116 – 1161Phosphoserine1 Publication
Disulfide bondi120 – 120Interchain (with C-62); in linked form1 Publication

Post-translational modificationi

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.

Keywords - PTMi

Acetylation, Disulfide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP38013.
PaxDbiP38013.
PeptideAtlasiP38013.

2D gel databases

COMPLUYEAST-2DPAGEP38013.

Expressioni

Inductioni

By H2O2.1 Publication

Gene expression databases

GenevestigatoriP38013.

Interactioni

Subunit structurei

Homodimer; disulfide-linked, upon oxidation.1 Publication

Protein-protein interaction databases

BioGridi31382. 58 interactions.
DIPiDIP-6375N.
IntActiP38013. 4 interactions.
MINTiMINT-705985.
STRINGi4932.YLR109W.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni3 – 64
Beta strandi15 – 184
Beta strandi23 – 253
Helixi29 – 313
Beta strandi35 – 384
Helixi39 – 457
Beta strandi47 – 537
Helixi60 – 645
Helixi67 – 8014
Beta strandi85 – 928
Helixi94 – 10310
Beta strandi110 – 1167
Helixi118 – 1203
Helixi121 – 1255
Beta strandi129 – 1335
Beta strandi136 – 1394
Beta strandi141 – 1477
Beta strandi150 – 1567
Turni160 – 1623
Helixi169 – 1735

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliP38013.
SMRiP38013. Positions 1-176.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini9 – 176168Thioredoxin
Add
BLAST

Sequence similaritiesi

Belongs to the peroxiredoxin 2 family.
Contains 1 thioredoxin domain.

Keywords - Domaini

Redox-active center

Phylogenomic databases

eggNOGiCOG0678.
GeneTreeiENSGT00390000018173.
HOGENOMiHOG000255884.
KOiK14171.
OMAiCHANHAP.
OrthoDBiEOG7X3R3F.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR013740. Redoxin.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF08534. Redoxin. 1 hit.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 1 hit.
PROSITEiPS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P38013-1 [UniParc]FASTAAdd to Basket

« Hide

MSDLVNKKFP AGDYKFQYIA ISQSDADSES CKMPQTVEWS KLISENKKVI    50
ITGAPAAFSP TCTVSHIPGY INYLDELVKE KEVDQVIVVT VDNPFANQAW 100
AKSLGVKDTT HIKFASDPGC AFTKSIGFEL AVGDGVYWSG RWAMVVENGI 150
VTYAAKETNP GTDVTVSSVE SVLAHL 176
Length:176
Mass (Da):19,115
Last modified:January 23, 2007 - v4
Checksum:i11B730781306A015
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti21 – 211I → T AA sequence 1 Publication
Sequence conflicti65 – 651S → V AA sequence 1 Publication
Sequence conflicti87 – 871I → E AA sequence 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
PIRi S64946.
RefSeqi NP_013210.1. NM_001181996.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
ProteinModelPortali P38013.
SMRi P38013. Positions 1-176.
ModBasei Search...

Protein-protein interaction databases

BioGridi 31382. 58 interactions.
DIPi DIP-6375N.
IntActi P38013. 4 interactions.
MINTi MINT-705985.
STRINGi 4932.YLR109W.

2D gel databases

COMPLUYEAST-2DPAGE P38013.

Proteomic databases

MaxQBi P38013.
PaxDbi P38013.
PeptideAtlasi P38013.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YLR109W ; YLR109W ; YLR109W .
GeneIDi 850799.
KEGGi sce:YLR109W.

Organism-specific databases

SGDi S000004099. AHP1.

Phylogenomic databases

eggNOGi COG0678.
GeneTreei ENSGT00390000018173.
HOGENOMi HOG000255884.
KOi K14171.
OMAi CHANHAP.
OrthoDBi EOG7X3R3F.

Enzyme and pathway databases

BioCyci YEAST:YLR109W-MONOMER.

Miscellaneous databases

NextBioi 967020.
PROi P38013.

Gene expression databases

Genevestigatori P38013.

Family and domain databases

Gene3Di 3.40.30.10. 1 hit.
InterProi IPR013740. Redoxin.
IPR012336. Thioredoxin-like_fold.
[Graphical view ]
Pfami PF08534. Redoxin. 1 hit.
[Graphical view ]
SUPFAMi SSF52833. SSF52833. 1 hit.
PROSITEi PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. 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. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiAHP1_YEAST
AccessioniPrimary (citable) accession number: P38013
Secondary accession number(s): D6VYA9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: January 23, 2007
Last modified: May 14, 2014
This is version 147 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

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

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

External Data

Dasty 3

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