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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

heme1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei701 Publication1
Active sitei1431 Publication1
Metal bindingi355Iron (heme axial ligand)1 Publication1

GO - Molecular functioni

  • catalase activity Source: SGD
  • heme binding Source: GO_Central
  • 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 hydrogen peroxide Source: GO_Central
  • 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.
ReactomeiR-SCE-3299685. Detoxification of Reactive Oxygen Species.
R-SCE-6798695. Neutrophil degranulation.
R-SCE-74259. 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
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

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)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00000849282 – 515Peroxisomal catalase AAdd BLAST514

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineCombined sources1

Keywords - PTMi

Acetylation

Proteomic databases

PRIDEiP15202.

Interactioni

Subunit structurei

Homotetramer.

Binary interactionsi

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

Protein-protein interaction databases

BioGridi32306. 37 interactors.
DIPiDIP-4320N.
IntActiP15202. 7 interactors.
MINTiMINT-545033.

Structurei

Secondary structure

1515
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi31 – 34Combined sources4
Beta strandi36 – 39Combined sources4
Turni40 – 42Combined sources3
Helixi50 – 59Combined sources10
Beta strandi72 – 82Combined sources11
Turni87 – 89Combined sources3
Helixi93 – 95Combined sources3
Beta strandi101 – 109Combined sources9
Beta strandi111 – 113Combined sources3
Beta strandi119 – 123Combined sources5
Beta strandi126 – 133Combined sources8
Beta strandi136 – 147Combined sources12
Helixi155 – 163Combined sources9
Turni167 – 169Combined sources3
Helixi174 – 181Combined sources8
Helixi184 – 189Combined sources6
Helixi190 – 197Combined sources8
Helixi199 – 201Combined sources3
Beta strandi202 – 204Combined sources3
Helixi206 – 208Combined sources3
Beta strandi217 – 220Combined sources4
Beta strandi226 – 237Combined sources12
Helixi244 – 253Combined sources10
Helixi257 – 267Combined sources11
Beta strandi273 – 281Combined sources9
Helixi283 – 287Combined sources5
Beta strandi289 – 291Combined sources3
Turni302 – 304Combined sources3
Beta strandi308 – 317Combined sources10
Helixi322 – 325Combined sources4
Turni326 – 328Combined sources3
Beta strandi340 – 342Combined sources3
Helixi346 – 362Combined sources17
Helixi367 – 369Combined sources3
Helixi371 – 373Combined sources3
Turni395 – 398Combined sources4
Beta strandi425 – 427Combined sources3
Beta strandi429 – 432Combined sources4
Beta strandi438 – 440Combined sources3
Helixi441 – 454Combined sources14
Helixi459 – 471Combined sources13
Helixi476 – 487Combined sources12
Helixi491 – 501Combined sources11

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP15202.

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi513 – 515Microbody targeting signalSequence analysis3

Sequence similaritiesi

Belongs to the catalase family.Curated

Phylogenomic databases

GeneTreeiENSGT00390000018100.
HOGENOMiHOG000087852.
InParanoidiP15202.
KOiK03781.
OMAiYIQTMTE.
OrthoDBiEOG092C0NOX.

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)DescriptionActionsGraphical viewLength
Sequence conflicti131F → L in AAU09703 (PubMed:17322287).Curated1

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1A4EX-ray2.40A/B/C/D15-502[»]
ProteinModelPortaliP15202.
SMRiP15202.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32306. 37 interactors.
DIPiDIP-4320N.
IntActiP15202. 7 interactors.
MINTiMINT-545033.

Protein family/group databases

PeroxiBasei5175. SceKat01.

Proteomic databases

PRIDEiP15202.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

EuPathDBiFungiDB:YDR256C.
SGDiS000002664. CTA1.

Phylogenomic databases

GeneTreeiENSGT00390000018100.
HOGENOMiHOG000087852.
InParanoidiP15202.
KOiK03781.
OMAiYIQTMTE.
OrthoDBiEOG092C0NOX.

Enzyme and pathway databases

BioCyciYEAST:YDR256C-MONOMER.
ReactomeiR-SCE-3299685. Detoxification of Reactive Oxygen Species.
R-SCE-6798695. Neutrophil degranulation.
R-SCE-74259. Purine catabolism.

Miscellaneous databases

EvolutionaryTraceiP15202.
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...

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: November 30, 2016
This is version 155 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

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 one 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.