P34227 (PRX1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Mitochondrial peroxiredoxin PRX1
EC=1.11.1.15

Alternative name(s):
1-Cys PRX
Mitochondrial thiol peroxidase
Short name=mTPx
Thioredoxin reductase

Gene names

Name:	PRX1
Ordered Locus Names:	YBL064C
ORF Names:	YBL0503, YBL0524

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	261 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Has a thioredoxin peroxidase activity with a role in reduction of hydroperoxides. Ref.5
Catalytic activity	2 R'-SH + ROOH = R'-S-S-R' + H2O + ROH.
Subcellular location	Mitochondrion Ref.5 Ref.7.
Miscellaneous	Present with 4510 molecules/cell in log phase SD medium. Ref.6
Sequence similarities	Belongs to the AhpC/TSA family. Contains 1 thioredoxin domain.
Biophysicochemical properties	pH dependence: Optimum pH is 6.5.

Ontologies

Keywords
Cellular component	Mitochondrion
Domain	Redox-active center
Molecular function	Antioxidant Oxidoreductase Peroxidase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cell redox homeostasis Inferred from mutant phenotype Ref.4. Source: SGD response to cadmium ion Inferred from mutant phenotype. Source: SGD
Cellular component	mitochondrion Inferred from direct assay Ref.4Ref.5Ref.7. Source: SGD
Molecular function	thioredoxin peroxidase activity Inferred from direct assay Ref.5. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 261	261	Mitochondrial peroxiredoxin PRX1		PRO_0000135151
Regions
	Domain	49 – 212	164	Thioredoxin
Sites
	Active site	91	1	By similarity
Amino acid modifications
	Modified residue	53	1	Phosphoserine Ref.8
Experimental info
	Mutagenesis	91	1	C → S: No activity. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	P34227 [UniParc]. Last modified February 1, 1994. Version 1. Checksum: F611A9ED85E4681A	FASTA	261	29,496
	10 20 30 40 50 60 MFSRICSAQL KRTAWTLPKQ AHLQSQTIKT FATAPILCKQ FKQSDQPRLR INSDAPNFDA 70 80 90 100 110 120 DTTVGKINFY DYLGDSWGVL FSHPADFTPV CTTEVSAFAK LKPEFDKRNV KLIGLSVEDV 130 140 150 160 170 180 ESHEKWIQDI KEIAKVKNVG FPIIGDTFRN VAFLYDMVDA EGFKNINDGS LKTVRSVFVI 190 200 210 220 230 240 DPKKKIRLIF TYPSTVGRNT SEVLRVIDAL QLTDKEGVVT PINWQPADDV IIPPSVSNDE 250 260 AKAKFGQFNE IKPYLRFTKS K

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequencing and functional analysis of a 32,560 bp segment on the left arm of yeast chromosome II. Identification of 26 open reading frames, including the KIP1 and SEC17 genes." Scherens B., el Bakkoury M., Vierendeels F., Dubois E., Messenguy F. Yeast 9:1355-1371(1993) [PubMed: 8154187] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[2]	"Complete DNA sequence of yeast chromosome II." Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C. , Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K. EMBO J. 13:5795-5809(1994) [PubMed: 7813418] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[4]	"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, MUTAGENESIS OF CYS-91.
[5]	"Mitochondria of Saccharomyces cerevisiae contain one-conserved cysteine type peroxiredoxin with thioredoxin peroxidase activity." Pedrajas J.R., Miranda-Vizuete A., Javanmardy N., Gustafsson J.A., Spyrou G. J. Biol. Chem. 275:16296-16301(2000) [PubMed: 10821871] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[6]	"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].
[7]	"The proteome of Saccharomyces cerevisiae mitochondria." Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E., Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P., Pfanner N., Meisinger C. Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003) [PubMed: 14576278] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY. Strain: ATCC 76625 / YPH499.
[8]	"Profiling phosphoproteins of yeast mitochondria reveals a role of phosphorylation in assembly of the ATP synthase." Reinders J., Wagner K., Zahedi R.P., Stojanovski D., Eyrich B., van der Laan M., Rehling P., Sickmann A., Pfanner N., Meisinger C. Mol. Cell. Proteomics 6:1896-1906(2007) [PubMed: 17761666] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-53, MASS SPECTROMETRY. Strain: ATCC 76625 / YPH499.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z23261 Genomic DNA. Translation: CAA80784.1. Z35825 Genomic DNA. Translation: CAA84884.1. BK006936 Genomic DNA. Translation: DAA07056.1.
PIR	S39825.
RefSeq	NP_009489.1. NM_001178304.1.
3D structure databases
ProteinModelPortal	P34227.
SMR	P34227. Positions 48-260.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-6412N.
IntAct	P34227. 7 interactions.
MINT	MINT-642862.
STRING	P34227.
2D gel databases
UCD-2DPAGE	P34227.
Proteomic databases
PeptideAtlas	P34227.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YBL064C; YBL064C; YBL064C.
GeneID	852215.
KEGG	sce:YBL064C.
NMPDR	fig|4932.3.peg.178.
Organism-specific databases
CYGD	YBL064c.
SGD	S000000160. PRX1.
Phylogenomic databases
eggNOG	fuNOG07943.
GeneTree	EFGT00050000006473.
HOGENOM	HBG493509.
OMA	NYPILAD.
OrthoDB	EOG4K6KD8.
Gene expression databases
ArrayExpress	P34227.
Genevestigator	P34227.
GermOnline	YBL064C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR000866. AhpC/TSA. IPR024706. Peroxiredoxin_AhpC-typ. IPR019479. Peroxiredoxin_C. IPR012336. Thioredoxin-like_fold. [Graphical view]
Gene3D	G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.
KO	K03386.
Pfam	PF10417. 1-cysPrx_C. 1 hit. PF00578. AhpC-TSA. 1 hit. [Graphical view]
PIRSF	PIRSF000239. AHPC. 1 hit.
SUPFAM	SSF52833. Thiordxn-like_fd. 1 hit.
PROSITE	PS51352. THIOREDOXIN_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	970724.

Entry information

Entry name

PRX1_YEAST

Accession

Primary (citable) accession number: P34227
Secondary accession number(s): D6VPT6

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
Last sequence update:	February 1, 1994
Last modified:	December 14, 2011
This is version 101 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program