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P15202 (CATA_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 134. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Peroxisomal catalase A

EC=1.11.1.6
Gene names
Name:CTA1
Ordered Locus Names:YDR256C
ORF Names:YD9320A.06C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length515 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide.

Catalytic activity

2 H2O2 = O2 + 2 H2O.

Cofactor

Heme group.

Subunit structure

Homotetramer.

Subcellular location

Peroxisome.

Miscellaneous

This is one of two catalases in S.cerevisiae; the other is catalase T, which is the cytoplasmic form.

Present with 623 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the catalase family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

RSP5P399402EBI-4061,EBI-16219

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.6
Chain2 – 515514Peroxisomal catalase A
PRO_0000084928

Regions

Motif513 – 5153Microbody targeting signal Potential

Sites

Active site701
Active site1431
Metal binding3551Iron (heme axial ligand)

Amino acid modifications

Modified residue21N-acetylserine Ref.6

Experimental info

Sequence conflict1311F → L in AAU09703. Ref.4

Secondary structure

.................................................................................. 515
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P15202 [UniParc].

Last modified April 1, 1990. Version 1.
Checksum: 22DFCC599D79801F

FASTA51558,555
        10         20         30         40         50         60 
MSKLGQEKNE VNYSDVREDR VVTNSTGNPI NEPFVTQRIG EHGPLLLQDY NLIDSLAHFN 

        70         80         90        100        110        120 
RENIPQRNPH AHGSGAFGYF EVTDDITDIC GSAMFSKIGK RTKCLTRFST VGGDKGSADT 

       130        140        150        160        170        180 
VRDPRGFATK FYTEEGNLDW VYNNTPVFFI RDPSKFPHFI HTQKRNPQTN LRDADMFWDF 

       190        200        210        220        230        240 
LTTPENQVAI HQVMILFSDR GTPANYRSMH GYSGHTYKWS NKNGDWHYVQ VHIKTDQGIK 

       250        260        270        280        290        300 
NLTIEEATKI AGSNPDYCQQ DLFEAIQNGN YPSWTVYIQT MTERDAKKLP FSVFDLTKVW 

       310        320        330        340        350        360 
PQGQFPLRRV GKIVLNENPL NFFAQVEQAA FAPSTTVPYQ EASADPVLQA RLFSYADAHR 

       370        380        390        400        410        420 
YRLGPNFHQI PVNCPYASKF FNPAIRDGPM NVNGNFGSEP TYLANDKSYT YIQQDRPIQQ 

       430        440        450        460        470        480 
HQEVWNGPAI PYHWATSPGD VDFVQARNLY RVLGKQPGQQ KNLAYNIGIH VEGACPQIQQ 

       490        500        510 
RVYDMFARVD KGLSEAIKKV AEAKHASELS SNSKF 

« Hide

References

« Hide 'large scale' references
[1]"Sequence of the Saccharomyces cerevisiae CTA1 gene and amino acid sequence of catalase A derived from it."
Cohen G., Rapatz W., Ruis H.
Eur. J. Biochem. 176:159-163(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T. expand/collapse author list , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae."
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. expand/collapse author list , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.
Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[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] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[6]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[7]"Structure of catalase-A from Saccharomyces cerevisiae."
Mate M.J., Zamocky M., Nykyri L.M., Herzog C., Alzari P.M., Betzel C., Koller F., Fita I.
J. Mol. Biol. 286:135-149(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X13028 Genomic DNA. Translation: CAA31443.1.
Z68329 Genomic DNA. Translation: CAA92713.1.
Z70202 Genomic DNA. Translation: CAA94095.1.
AY723786 Genomic DNA. Translation: AAU09703.1.
BK006938 Genomic DNA. Translation: DAA12096.1.
PIRCSBYP. S07868.
RefSeqNP_010542.1. NM_001180564.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1A4EX-ray2.40A/B/C/D15-502[»]
ProteinModelPortalP15202.
SMRP15202. Positions 15-502.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid32306. 37 interactions.
DIPDIP-4320N.
IntActP15202. 7 interactions.
MINTMINT-545033.
STRING4932.YDR256C.

Protein family/group databases

PeroxiBase5175. SceKat01.

Proteomic databases

PaxDbP15202.
PeptideAtlasP15202.
PRIDEP15202.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYDR256C; YDR256C; YDR256C.
GeneID851843.
KEGGsce:YDR256C.

Organism-specific databases

CYGDYDR256c.
SGDS000002664. CTA1.

Phylogenomic databases

eggNOGCOG0753.
GeneTreeENSGT00390000018100.
HOGENOMHOG000087852.
KOK03781.
OMAEATTMIM.
OrthoDBEOG7K9KBN.

Enzyme and pathway databases

BioCycYEAST:YDR256C-MONOMER.

Gene expression databases

GenevestigatorP15202.

Family and domain databases

Gene3D2.40.180.10. 1 hit.
InterProIPR018028. Catalase.
IPR020835. Catalase-like_dom.
IPR024708. Catalase_AS.
IPR024711. Catalase_clade1/3.
IPR011614. Catalase_core.
IPR002226. Catalase_haem_BS.
IPR010582. Catalase_immune_responsive.
[Graphical view]
PANTHERPTHR11465. PTHR11465. 1 hit.
PfamPF00199. Catalase. 1 hit.
PF06628. Catalase-rel. 1 hit.
[Graphical view]
PIRSFPIRSF038928. Catalase_clade1-3. 1 hit.
PRINTSPR00067. CATALASE.
SMARTSM01060. Catalase. 1 hit.
[Graphical view]
SUPFAMSSF56634. SSF56634. 1 hit.
PROSITEPS00437. CATALASE_1. 1 hit.
PS00438. CATALASE_2. 1 hit.
PS51402. CATALASE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP15202.
NextBio969751.
PROP15202.

Entry information

Entry nameCATA_YEAST
AccessionPrimary (citable) accession number: P15202
Secondary accession number(s): D6VSN6, E9P947
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: June 11, 2014
This is version 134 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome IV

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

Yeast

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

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references