P06115 (CATT_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Catalase T
EC=1.11.1.6

Gene names

Name:	CTT1
Ordered Locus Names:	YGR088W

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	562 AA.
Sequence status	Complete.
Protein existence	Evidence 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	Cytoplasm Ref.6.
Miscellaneous	This is one of two catalases in S.cerevisiae; the other is catalase A, which is the peroxisomal form. Present with 319 molecules/cell in log phase SD medium. Ref.7
Sequence similarities	Belongs to the catalase family.
Sequence caution	The sequence AAA34540.1 differs from that shown. Reason: Erroneous initiation. The sequence CAA97090.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Hydrogen peroxide
Cellular component	Cytoplasm
Ligand	Heme Iron Metal-binding
Molecular function	Oxidoreductase Peroxidase
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	cellular response to water deprivation Inferred from mutant phenotype. Source: SGD hydrogen peroxide catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Traceable author statement. Source: SGD
Molecular function	catalase activity Inferred from electronic annotation. Source: EC heme binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 562	562	Catalase T		PRO_0000084929
Sites
	Active site	64	1	By similarity
	Active site	137	1	By similarity
	Metal binding	351	1	Iron (heme axial ligand) By similarity
Amino acid modifications
	Modified residue	52	1	Phosphoserine Ref.9
	Modified residue	417	1	Phosphoserine Ref.9
Experimental info
	Sequence conflict	429	1	D → V in CAA28298. Ref.1
	Sequence conflict	539	1	C → G in CAA28298. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P06115 [UniParc]. Last modified April 29, 2008. Version 3. Checksum: 1197842ADEAAE7D0	FASTA	562	64,583
	10 20 30 40 50 60 MNVFGKKEEK QEKVYSLQNG FPYSHHPYAS QYSRPDGPIL LQDFHLLENI ASFDRERVPE 70 80 90 100 110 120 RVVHAKGGGC RLEFELTDSL SDITYAAPYQ NVGYKCPGLV RFSTVGGESG TPDTARDPRG 130 140 150 160 170 180 VSFKFYTEWG NHDWVFNNTP VFFLRDAIKF PVFIHSQKRD PQSHLNQFQD TTIYWDYLTL 190 200 210 220 230 240 NPESIHQITY MFGDRGTPAS WASMNAYSGH SFIMVNKEGK DTYVQFHVLS DTGFETLTGD 250 260 270 280 290 300 KAAELSGSHP DYNQAKLFTQ LQNGEKPKFN CYVQTMTPEQ ATKFRYSVND LTKIWPHKEF 310 320 330 340 350 360 PLRKFGTITL TENVDNYFQE IEQVAFSPTN TCIPGIKPSN DSVLQARLFS YPDTQRHRLG 370 380 390 400 410 420 ANYQQLPVNR PRNLGCPYSK GDSQYTAEQC PFKAVNFQRD GPMSYYNFGP EPNYISSLPN 430 440 450 460 470 480 QTLKFKNEDN DEVSDKFKGI VLDEVTEVSV RKQEQDQIRN EHIVDAKINQ YYYVYGISPL 490 500 510 520 530 540 DFEQPRALYE KVYNDEQKKL FVHNVVCHAC KIKDPKVKKR VTQYFGLLNE DLGKVIAECL 550 560 GVPWEPVDLE GYAKTWSIAS AN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence of the Saccharomyces cerevisiae CTT1 gene and deduced amino-acid sequence of yeast catalase T." Hartig A., Ruis H. Eur. J. Biochem. 160:487-490(1986) [PubMed: 3536508] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome VII." Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E. , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K. Nature 387:81-84(1997) [PubMed: 9169869] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[4]	"Heme control region of the catalase T gene of the yeast Saccharomyces cerevisiae." Spevak W., Hartig A., Meindl P., Ruis H. Mol. Gen. Genet. 203:73-78(1986) [PubMed: 2423850] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-63.
[5]	"Metabolic and regulatory changes associated with growth of Saccharomyces cerevisiae in 1.4 M NaCl. Evidence for osmotic induction of glycerol dissimilation via the dihydroxyacetone pathway." Norbeck J., Blomberg A. J. Biol. Chem. 272:5544-5554(1997) [PubMed: 9038161] [Abstract] Cited for: PROTEIN SEQUENCE OF 394-398. Strain: ATCC 44827 / SKQ2N.
[6]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed: 14562095] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[7]	"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].
[8]	"Mapping of transcription start sites in Saccharomyces cerevisiae using 5' SAGE." Zhang Z., Dietrich F.S. Nucleic Acids Res. 33:2838-2851(2005) [PubMed: 15905473] [Abstract] Cited for: IDENTIFICATION OF PROBABLE INITIATION SITE.
[9]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52 AND SER-417, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X04625 Genomic DNA. Translation: CAA28298.1. Z72873 Genomic DNA. Translation: CAA97090.1. Different initiation. M30256 Genomic DNA. Translation: AAA34540.1. Different initiation. BK006941 Genomic DNA. Translation: DAA08181.1.
PIR	CSBYT. S64383.
RefSeq	NP_011602.2. NM_001181217.1.
3D structure databases
ProteinModelPortal	P06115.
SMR	P06115. Positions 11-542.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-4310N.
IntAct	P06115. 8 interactions.
MINT	MINT-522531.
STRING	P06115.
Protein family/group databases
PeroxiBase	5176. SceKat02.
Proteomic databases
PeptideAtlas	P06115.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YGR088W; YGR088W; YGR088W.
GeneID	852979.
KEGG	sce:YGR088W.
NMPDR	fig|4932.3.peg.2719.
Organism-specific databases
SGD	S000003320. CTT1.
Phylogenomic databases
eggNOG	fuNOG05162.
GeneTree	EFGT00050000004867.
HOGENOM	HBG339355.
OMA	FRYSIND.
OrthoDB	EOG4Z65X1.
Gene expression databases
ArrayExpress	P06115.
Genevestigator	P06115.
GermOnline	YGR088W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	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]
Gene3D	G3DSA:2.40.180.10. Catalase_N. 1 hit.
KO	K03781.
PANTHER	PTHR11465. Catalase. 1 hit.
Pfam	PF00199. Catalase. 1 hit. PF06628. Catalase-rel. 1 hit. [Graphical view]
PIRSF	PIRSF038928. Catalase_clade1-3. 1 hit.
PRINTS	PR00067. CATALASE.
SMART	SM01060. Catalase. 1 hit. [Graphical view]
SUPFAM	SSF56634. Catalase_N. 1 hit.
PROSITE	PS00437. CATALASE_1. 1 hit. PS00438. CATALASE_2. 1 hit. PS51402. CATALASE_3. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	972783.

Entry information

Entry name

CATT_YEAST

Accession

Primary (citable) accession number: P06115
Secondary accession number(s): D6VUM0

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1988
Last sequence update:	April 29, 2008
Last modified:	January 25, 2012
This is version 120 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program