Reviewed, UniProtKB/Swiss-Prot P34227 (PRX1_YEAST)

Names and origin

Protein names

Recommended name:
    Mitochondrial peroxiredoxin PRX1
    EC=1.11.1.15
Alternative name(s):
    Thioredoxin reductase
    1-Cys PRX
    Mitochondrial thiol peroxidase
      Short name=mTPx

Gene names

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

Organism

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

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	261 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Has a thioredoxin peroxidase activity with a role in reduction of hydroperoxides. Ref.4
Catalytic activity	2 R'-SH + ROOH = R'-S-S-R' + H2O + ROH.
Subcellular location	Mitochondrion.
Miscellaneous	Present with 4510 molecules/cell in log phase SD medium. Ref.5
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
Gene Ontology (GO)
Biological process	cell redox homeostasis Ref.3 Inferred from direct assay. Source: SGD oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW response to cadmium ion Inferred from mutant phenotype. Source: SGD response to oxidative stress Inferred from genetic interaction. Source: SGD
Cellular component	mitochondrion Ref.3 Ref.4 Ref.6 Inferred from direct assay. Source: SGD
Molecular function	thioredoxin peroxidase activity Ref.3 Ref.4 Inferred from direct assay. 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.7
Experimental info
	Mutagenesis	91	1	C → S: No activity. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	P34227-1 [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]	"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.
[4]	"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.
[5]	"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].
[6]	"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.
[7]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	Z23261 Genomic DNA. Translation: CAA80784.1. Z35825 Genomic DNA. Translation: CAA84884.1.
PIR	S39825.
RefSeq	NP_009489.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:6412N.
STRING	P34227.
Proteomic databases
PeptideAtlas	P34227.
Genome annotation databases
Ensembl	YBL064C; YBL064C; YBL064C; Saccharomyces cerevisiae. [Genome view]
GeneID	852215.
KEGG	sce:YBL064C.
NMPDR	fig|4932.3.peg.178.
Organism-specific databases
CYGD	YBL064c.
SGD	S000000160. PRX1.
Phylogenomic databases
HOGENOM	P34227.
OMA	HPNANDT
OrthoDB	EOG9X3JHG
Enzyme and pathway databases
BRENDA	1.11.1.15. 250.
Gene expression databases
ArrayExpress	P34227.
Genevestigator	P34227.
GermOnline	YBL064C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR000866. Alkyl_hydroperoxide_Rdtase. IPR019479. Peroxiredoxin_C. IPR017936. Thioredoxin-like. IPR012336. Thioredoxin-like_fold. IPR012335. Thioredoxin_fold. [Graphical view]
Gene3D	G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.
Pfam	PF10417. 1-cysPrx_C. 1 hit. PF00578. AhpC-TSA. 1 hit. [Graphical view]
PROSITE	PS51352. THIOREDOXIN_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	970724.

Entry information

Entry name

PRX1_YEAST

Accession

Primary (citable) accession number: P34227

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
Last sequence update:	February 1, 1994
Last modified:	November 24, 2009
This is version 79 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)