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P15202 (CATA_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 114. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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
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)
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length515 AA.
Sequence statusComplete.
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. Ref.5

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

Chain1 – 515515Peroxisomal catalase A
PRO_0000084928

Regions

Motif513 – 5153Microbody targeting signal Potential

Sites

Active site701
Active site1431
Metal binding3551Iron (heme axial ligand)

Experimental info

Sequence conflict1311F → L in AAU09703. Ref.4

Secondary structure

1 .................................................................................. 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: 3046940] [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: 9169867] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204511 / S288c / AB972.
[3]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
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: 17322287] [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: 14562106] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[6]"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: 9931255] [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...

Protein-protein interaction databases

DIPDIP-4320N.
IntActP15202. 7 interactions.
MINTMINT-545033.
STRINGP15202.

Protein family/group databases

PeroxiBase5175. SceKat01.

Proteomic databases

PeptideAtlasP15202.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYDR256C; YDR256C; YDR256C.
GeneID851843.
KEGGsce:YDR256C.
NMPDRfig|4932.3.peg.1300.

Organism-specific databases

CYGDYDR256c.
SGDS000002664. CTA1.

Phylogenomic databases

eggNOGfuNOG05162.
HOGENOMHBG339355.
OMADWVYNNT.
OrthoDBEOG4Z65X1.

Gene expression databases

ArrayExpressP15202.
GenevestigatorP15202.
GermOnlineYDR256C. Saccharomyces cerevisiae.

Family and domain databases

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]
Gene3DG3DSA:2.40.180.10. Catalase_N. 1 hit.
KOK03781.
PANTHERPTHR11465. Catalase. 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. Catalase_N. 1 hit.
PROSITEPS00437. CATALASE_1. 1 hit.
PS00438. CATALASE_2. 1 hit.
PS51402. CATALASE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio969751.

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: January 25, 2012
This is version 114 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents