PRX1/YBL064C Protein Information

Standard Name	Prx1p 1
Systematic Name	Ybl064cp
ORF Classification	Verified
Description	Mitochondrial peroxiredoxin with thioredoxin peroxidase activity; has a role in reduction of hydroperoxides; reactivation requires Trr2p and glutathione; induced during respiratory growth and oxidative stress; phosphorylated; protein abundance increases in response to DNA replication stress (1, 2, 3, 4, 5)
Name Description	PeroxiRedoXin 1

Experimental Data
Molecules/cell	4510 6

Predicted Sequence	Formatted Sequence or sequence in FASTA format
Length (a.a.)	261
Molecular Weight (Da)	29,496
Isoelectric Point (pI)	9.47

Click on image for expanded interactive view

Post-translational Modifications	PhosphoGRID \| PhosphoPep Database
Domains/motifs	See the graphical view and list of proteins that share domains/motifs in common with Prx1p (InterPro)
Physical Interactions	There are 23 total physical interactions (BioGRID)
Homologs	PDB Homologs \| BLASTP \| BLASTP v. fungi \| Fungal Alignment \| Synteny Viewer
External Sequence Databases	EBI: UPI000004F8CE \| P34227 MIPS: YBL064C NCBI: 313735 \| 465521 \| 536101 \| 6319407 \| NP_009489.1 GenBank/EMBL/DDBJ: DAA07056.1 \| Z23261 \| Z35825
External Classifications	EC: 1.11.1.15 [Peroxiredoxin]

Amino Acid Sequence (or in FASTA format)
1 MFSRICSAQL KRTAWTLPKQ AHLQSQTIKT FATAPILCKQ FKQSDQPRLR 51 INSDAPNFDA DTTVGKINFY DYLGDSWGVL FSHPADFTPV CTTEVSAFAK 101 LKPEFDKRNV KLIGLSVEDV ESHEKWIQDI KEIAKVKNVG FPIIGDTFRN 151 VAFLYDMVDA EGFKNINDGS LKTVRSVFVI DPKKKIRLIF TYPSTVGRNT 201 SEVLRVIDAL QLTDKEGVVT PINWQPADDV IIPPSVSNDE AKAKFGQFNE 251 IKPYLRFTKS K*

Amino Acid Sequence (or in FASTA format)

       1  MFSRICSAQL KRTAWTLPKQ AHLQSQTIKT FATAPILCKQ FKQSDQPRLR
      51  INSDAPNFDA DTTVGKINFY DYLGDSWGVL FSHPADFTPV CTTEVSAFAK
     101  LKPEFDKRNV KLIGLSVEDV ESHEKWIQDI KEIAKVKNVG FPIIGDTFRN
     151  VAFLYDMVDA EGFKNINDGS LKTVRSVFVI DPKKKIRLIF TYPSTVGRNT
     201  SEVLRVIDAL QLTDKEGVVT PINWQPADDV IIPPSVSNDE AKAKFGQFNE
     251  IKPYLRFTKS K*

external links for Prx1p

Homologs	Interaction Resources	Protein databases/Other	Localization Resources
BLASTP (NCBI)	BioGRID	SCOP Superfamily	Organelle DB
Ashbya (AGD)	BOND	GPMdb (Mass Spec.)	YPL+
Aspergillus (AspGD)	BioPIXIE	MIPS	YeastGFP
Candida (CGD)	CYC2008 (complexes)	Pfam domains	YeastRC Public Image Repository
Candida (CandidaDB)	Complexome	YeastRC Structure Prediction (Seattle)
YGOB	DIP
YOGY	GeneMANIA

References cited on this page View Complete Literature Guide for Prx1p

1)	Pedrajas JR, et al. (2000) Mitochondria of Saccharomyces cerevisiae contain one-conserved cysteine type peroxiredoxin with thioredoxin peroxidase activity. J Biol Chem 275(21):16296-301
2)	Grant CM (2001) Role of the glutathione/glutaredoxin and thioredoxin systems in yeast growth and response to stress conditions. Mol Microbiol 39(3):533-41
3)	Reinders J, et al. (2007) Profiling phosphoproteins of yeast mitochondria reveals a role of phosphorylation in assembly of the ATP synthase. Mol Cell Proteomics 6(11):1896-906
4)	Greetham D and Grant CM (2009) Antioxidant activity of the yeast mitochondrial one-Cys peroxiredoxin is dependent on thioredoxin reductase and glutathione in vivo. Mol Cell Biol 29(11):3229-40
5)	Tkach JM, et al. (2012) Dissecting DNA damage response pathways by analysing protein localization and abundance changes during DNA replication stress. Nat Cell Biol 14(9):966-76
6)	Ghaemmaghami S, et al. (2003) Global analysis of protein expression in yeast. Nature 425(6959):737-41