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P15202

- CATA_YEAST

UniProt

P15202 - CATA_YEAST

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Protein

Peroxisomal catalase A

Gene

CTA1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - 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

Heme group.

Sites

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

GO - Molecular functioni

  1. catalase activity Source: SGD
  2. heme binding Source: InterPro
  3. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. age-dependent response to reactive oxygen species Source: SGD
  2. hydrogen peroxide catabolic process Source: SGD
  3. 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_191152. Detoxification of Reactive Oxygen Species.

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: Chromosome IV

Organism-specific databases

CYGDiYDR256c.
SGDiS000002664. CTA1.

Subcellular locationi

GO - Cellular componenti

  1. mitochondrial matrix Source: SGD
  2. 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.

Expressioni

Gene expression databases

GenevestigatoriP15202.

Interactioni

Subunit structurei

Homotetramer.

Binary interactionsi

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

Protein-protein interaction databases

BioGridi32306. 37 interactions.
DIPiDIP-4320N.
IntActiP15202. 7 interactions.
MINTiMINT-545033.
STRINGi4932.YDR256C.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.
OMAiEATTMIM.
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:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
PIRi S07868. CSBYP.
RefSeqi NP_010542.1. NM_001180564.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1A4E X-ray 2.40 A/B/C/D 15-502 [» ]
ProteinModelPortali P15202.
SMRi P15202. Positions 15-502.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 32306. 37 interactions.
DIPi DIP-4320N.
IntActi P15202. 7 interactions.
MINTi MINT-545033.
STRINGi 4932.YDR256C.

Protein family/group databases

PeroxiBasei 5175. SceKat01.

Proteomic databases

PaxDbi P15202.
PeptideAtlasi P15202.
PRIDEi P15202.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YDR256C ; YDR256C ; YDR256C .
GeneIDi 851843.
KEGGi sce:YDR256C.

Organism-specific databases

CYGDi YDR256c.
SGDi S000002664. CTA1.

Phylogenomic databases

eggNOGi COG0753.
GeneTreei ENSGT00390000018100.
HOGENOMi HOG000087852.
InParanoidi P15202.
KOi K03781.
OMAi EATTMIM.
OrthoDBi EOG7K9KBN.

Enzyme and pathway databases

BioCyci YEAST:YDR256C-MONOMER.
Reactomei REACT_191152. Detoxification of Reactive Oxygen Species.

Miscellaneous databases

EvolutionaryTracei P15202.
NextBioi 969751.
PROi P15202.

Gene expression databases

Genevestigatori P15202.

Family and domain databases

Gene3Di 2.40.180.10. 1 hit.
InterProi IPR018028. 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 ]
PANTHERi PTHR11465. PTHR11465. 1 hit.
Pfami PF00199. Catalase. 1 hit.
PF06628. Catalase-rel. 1 hit.
[Graphical view ]
PIRSFi PIRSF038928. Catalase_clade1-3. 1 hit.
PRINTSi PR00067. CATALASE.
SMARTi SM01060. Catalase. 1 hit.
[Graphical view ]
SUPFAMi SSF56634. SSF56634. 1 hit.
PROSITEi PS00437. CATALASE_1. 1 hit.
PS00438. CATALASE_2. 1 hit.
PS51402. CATALASE_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: October 29, 2014
This is version 137 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