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Protein

Peroxisomal catalase A

Gene

CTA1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

2 H2O2 = O2 + 2 H2O.PROSITE-ProRule annotation

Cofactori

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei70 – 701
Active sitei143 – 1431
Metal bindingi355 – 3551Iron (heme axial ligand)

GO - Molecular functioni

  • catalase activity Source: SGD
  • heme binding Source: InterPro
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • age-dependent response to reactive oxygen species Source: SGD
  • hydrogen peroxide catabolic process Source: SGD
  • response to reactive oxygen species Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase, Peroxidase

Keywords - Biological processi

Hydrogen peroxide

Keywords - Ligandi

Heme, Iron, Metal-binding

Enzyme and pathway databases

BioCyciYEAST:YDR256C-MONOMER.
ReactomeiREACT_310793. Detoxification of Reactive Oxygen Species.
REACT_353691. Purine catabolism.

Protein family/group databases

PeroxiBasei5175. SceKat01.

Names & Taxonomyi

Protein namesi
Recommended name:
Peroxisomal catalase A (EC:1.11.1.6)
Gene namesi
Name:CTA1
Ordered Locus Names:YDR256C
ORF Names:YD9320A.06C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome IV

Organism-specific databases

CYGDiYDR256c.
EuPathDBiFungiDB:YDR256C.
SGDiS000002664. CTA1.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial matrix Source: SGD
  • peroxisomal matrix Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Peroxisome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 515514Peroxisomal catalase APRO_0000084928Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP15202.
PeptideAtlasiP15202.
PRIDEiP15202.

Interactioni

Subunit structurei

Homotetramer.

Binary interactionsi

WithEntry#Exp.IntActNotes
RSP5P399402EBI-4061,EBI-16219

Protein-protein interaction databases

BioGridi32306. 36 interactions.
DIPiDIP-4320N.
IntActiP15202. 7 interactions.
MINTiMINT-545033.

Structurei

Secondary structure

1
515
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi31 – 344Combined sources
Beta strandi36 – 394Combined sources
Turni40 – 423Combined sources
Helixi50 – 5910Combined sources
Beta strandi72 – 8211Combined sources
Turni87 – 893Combined sources
Helixi93 – 953Combined sources
Beta strandi101 – 1099Combined sources
Beta strandi111 – 1133Combined sources
Beta strandi119 – 1235Combined sources
Beta strandi126 – 1338Combined sources
Beta strandi136 – 14712Combined sources
Helixi155 – 1639Combined sources
Turni167 – 1693Combined sources
Helixi174 – 1818Combined sources
Helixi184 – 1896Combined sources
Helixi190 – 1978Combined sources
Helixi199 – 2013Combined sources
Beta strandi202 – 2043Combined sources
Helixi206 – 2083Combined sources
Beta strandi217 – 2204Combined sources
Beta strandi226 – 23712Combined sources
Helixi244 – 25310Combined sources
Helixi257 – 26711Combined sources
Beta strandi273 – 2819Combined sources
Helixi283 – 2875Combined sources
Beta strandi289 – 2913Combined sources
Turni302 – 3043Combined sources
Beta strandi308 – 31710Combined sources
Helixi322 – 3254Combined sources
Turni326 – 3283Combined sources
Beta strandi340 – 3423Combined sources
Helixi346 – 36217Combined sources
Helixi367 – 3693Combined sources
Helixi371 – 3733Combined sources
Turni395 – 3984Combined sources
Beta strandi425 – 4273Combined sources
Beta strandi429 – 4324Combined sources
Beta strandi438 – 4403Combined sources
Helixi441 – 45414Combined sources
Helixi459 – 47113Combined sources
Helixi476 – 48712Combined sources
Helixi491 – 50111Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A4EX-ray2.40A/B/C/D15-502[»]
ProteinModelPortaliP15202.
SMRiP15202. Positions 15-502.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP15202.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi513 – 5153Microbody targeting signalSequence Analysis

Sequence similaritiesi

Belongs to the catalase family.Curated

Phylogenomic databases

eggNOGiCOG0753.
GeneTreeiENSGT00390000018100.
HOGENOMiHOG000087852.
InParanoidiP15202.
KOiK03781.
OMAiHIQERMI.
OrthoDBiEOG7K9KBN.

Family and domain databases

Gene3Di2.40.180.10. 1 hit.
InterProiIPR018028. 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]
PANTHERiPTHR11465. PTHR11465. 1 hit.
PfamiPF00199. Catalase. 1 hit.
PF06628. Catalase-rel. 1 hit.
[Graphical view]
PIRSFiPIRSF038928. Catalase_clade1-3. 1 hit.
PRINTSiPR00067. CATALASE.
SMARTiSM01060. Catalase. 1 hit.
[Graphical view]
SUPFAMiSSF56634. SSF56634. 1 hit.
PROSITEiPS00437. CATALASE_1. 1 hit.
PS00438. CATALASE_2. 1 hit.
PS51402. CATALASE_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P15202-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKLGQEKNE VNYSDVREDR VVTNSTGNPI NEPFVTQRIG EHGPLLLQDY
60 70 80 90 100
NLIDSLAHFN RENIPQRNPH AHGSGAFGYF EVTDDITDIC GSAMFSKIGK
110 120 130 140 150
RTKCLTRFST VGGDKGSADT VRDPRGFATK FYTEEGNLDW VYNNTPVFFI
160 170 180 190 200
RDPSKFPHFI HTQKRNPQTN LRDADMFWDF LTTPENQVAI HQVMILFSDR
210 220 230 240 250
GTPANYRSMH GYSGHTYKWS NKNGDWHYVQ VHIKTDQGIK NLTIEEATKI
260 270 280 290 300
AGSNPDYCQQ DLFEAIQNGN YPSWTVYIQT MTERDAKKLP FSVFDLTKVW
310 320 330 340 350
PQGQFPLRRV GKIVLNENPL NFFAQVEQAA FAPSTTVPYQ EASADPVLQA
360 370 380 390 400
RLFSYADAHR YRLGPNFHQI PVNCPYASKF FNPAIRDGPM NVNGNFGSEP
410 420 430 440 450
TYLANDKSYT YIQQDRPIQQ HQEVWNGPAI PYHWATSPGD VDFVQARNLY
460 470 480 490 500
RVLGKQPGQQ KNLAYNIGIH VEGACPQIQQ RVYDMFARVD KGLSEAIKKV
510
AEAKHASELS SNSKF
Length:515
Mass (Da):58,555
Last modified:April 1, 1990 - v1
Checksum:i22DFCC599D79801F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti131 – 1311F → L in AAU09703 (PubMed:17322287).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiS07868. CSBYP.
RefSeqiNP_010542.1. NM_001180564.1.

Genome annotation databases

EnsemblFungiiYDR256C; YDR256C; YDR256C.
GeneIDi851843.
KEGGisce:YDR256C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiS07868. CSBYP.
RefSeqiNP_010542.1. NM_001180564.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A4EX-ray2.40A/B/C/D15-502[»]
ProteinModelPortaliP15202.
SMRiP15202. Positions 15-502.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32306. 36 interactions.
DIPiDIP-4320N.
IntActiP15202. 7 interactions.
MINTiMINT-545033.

Protein family/group databases

PeroxiBasei5175. SceKat01.

Proteomic databases

PaxDbiP15202.
PeptideAtlasiP15202.
PRIDEiP15202.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDR256C; YDR256C; YDR256C.
GeneIDi851843.
KEGGisce:YDR256C.

Organism-specific databases

CYGDiYDR256c.
EuPathDBiFungiDB:YDR256C.
SGDiS000002664. CTA1.

Phylogenomic databases

eggNOGiCOG0753.
GeneTreeiENSGT00390000018100.
HOGENOMiHOG000087852.
InParanoidiP15202.
KOiK03781.
OMAiHIQERMI.
OrthoDBiEOG7K9KBN.

Enzyme and pathway databases

BioCyciYEAST:YDR256C-MONOMER.
ReactomeiREACT_310793. Detoxification of Reactive Oxygen Species.
REACT_353691. Purine catabolism.

Miscellaneous databases

EvolutionaryTraceiP15202.
NextBioi969751.
PROiP15202.

Family and domain databases

Gene3Di2.40.180.10. 1 hit.
InterProiIPR018028. 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]
PANTHERiPTHR11465. PTHR11465. 1 hit.
PfamiPF00199. Catalase. 1 hit.
PF06628. Catalase-rel. 1 hit.
[Graphical view]
PIRSFiPIRSF038928. Catalase_clade1-3. 1 hit.
PRINTSiPR00067. CATALASE.
SMARTiSM01060. Catalase. 1 hit.
[Graphical view]
SUPFAMiSSF56634. SSF56634. 1 hit.
PROSITEiPS00437. CATALASE_1. 1 hit.
PS00438. CATALASE_2. 1 hit.
PS51402. CATALASE_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  6. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  7. Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).

Entry informationi

Entry nameiCATA_YEAST
AccessioniPrimary (citable) accession number: P15202
Secondary accession number(s): D6VSN6, E9P947
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: July 22, 2015
This is version 144 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

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.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, 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 IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.