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Database: UniProt
Entry: P06115
LinkDB: P06115
Original site: P06115 
ID   CATT_YEAST              Reviewed;         562 AA.
AC   P06115; D6VUM0;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 3.
DT   27-MAR-2024, entry version 206.
DE   RecName: Full=Catalase T;
DE            EC=1.11.1.6;
GN   Name=CTT1; OrderedLocusNames=YGR088W;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3536508; DOI=10.1111/j.1432-1033.1986.tb10065.x;
RA   Hartig A., Ruis H.;
RT   "Nucleotide sequence of the Saccharomyces cerevisiae CTT1 gene and deduced
RT   amino-acid sequence of yeast catalase T.";
RL   Eur. J. Biochem. 160:487-490(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169869;
RA   Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA   Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA   Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA   Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA   Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA   Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA   Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA   Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA   Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA   Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA   Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA   Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA   Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA   Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA   Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA   Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA   Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA   Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA   Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA   Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA   Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA   Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL   Nature 387:81-84(1997).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-63.
RX   PubMed=2423850; DOI=10.1007/bf00330386;
RA   Spevak W., Hartig A., Meindl P., Ruis H.;
RT   "Heme control region of the catalase T gene of the yeast Saccharomyces
RT   cerevisiae.";
RL   Mol. Gen. Genet. 203:73-78(1986).
RN   [5]
RP   PROTEIN SEQUENCE OF 394-398.
RC   STRAIN=ATCC 44827 / SKQ2N;
RX   PubMed=9038161; DOI=10.1074/jbc.272.9.5544;
RA   Norbeck J., Blomberg A.;
RT   "Metabolic and regulatory changes associated with growth of Saccharomyces
RT   cerevisiae in 1.4 M NaCl. Evidence for osmotic induction of glycerol
RT   dissimilation via the dihydroxyacetone pathway.";
RL   J. Biol. Chem. 272:5544-5554(1997).
RN   [6]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=14562095; DOI=10.1038/nature02026;
RA   Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA   Weissman J.S., O'Shea E.K.;
RT   "Global analysis of protein localization in budding yeast.";
RL   Nature 425:686-691(2003).
RN   [7]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [8]
RP   IDENTIFICATION OF PROBABLE INITIATION SITE.
RX   PubMed=15905473; DOI=10.1093/nar/gki583;
RA   Zhang Z., Dietrich F.S.;
RT   "Mapping of transcription start sites in Saccharomyces cerevisiae using 5'
RT   SAGE.";
RL   Nucleic Acids Res. 33:2838-2851(2005).
CC   -!- FUNCTION: Occurs in almost all aerobically respiring organisms and
CC       serves to protect cells from the toxic effects of hydrogen peroxide.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 H2O2 = 2 H2O + O2; Xref=Rhea:RHEA:20309, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:16240; EC=1.11.1.6;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU10013};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC   -!- SUBUNIT: Homotetramer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC   -!- MISCELLANEOUS: This is one of two catalases in S.cerevisiae; the other
CC       is catalase A, which is the peroxisomal form.
CC   -!- MISCELLANEOUS: Present with 319 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the catalase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA34540.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=CAA97090.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; X04625; CAA28298.1; -; Genomic_DNA.
DR   EMBL; Z72873; CAA97090.1; ALT_INIT; Genomic_DNA.
DR   EMBL; M30256; AAA34540.1; ALT_INIT; Genomic_DNA.
DR   EMBL; BK006941; DAA08181.1; -; Genomic_DNA.
DR   PIR; S64383; CSBYT.
DR   RefSeq; NP_011602.2; NM_001181217.1.
DR   AlphaFoldDB; P06115; -.
DR   SMR; P06115; -.
DR   BioGRID; 33330; 70.
DR   DIP; DIP-4310N; -.
DR   IntAct; P06115; 4.
DR   STRING; 4932.YGR088W; -.
DR   PeroxiBase; 5176; SceKat02.
DR   iPTMnet; P06115; -.
DR   MaxQB; P06115; -.
DR   PaxDb; 4932-YGR088W; -.
DR   PeptideAtlas; P06115; -.
DR   EnsemblFungi; YGR088W_mRNA; YGR088W; YGR088W.
DR   GeneID; 852979; -.
DR   KEGG; sce:YGR088W; -.
DR   AGR; SGD:S000003320; -.
DR   SGD; S000003320; CTT1.
DR   VEuPathDB; FungiDB:YGR088W; -.
DR   eggNOG; KOG0047; Eukaryota.
DR   GeneTree; ENSGT00390000018100; -.
DR   HOGENOM; CLU_010645_2_0_1; -.
DR   InParanoid; P06115; -.
DR   OMA; FRYSVND; -.
DR   OrthoDB; 3198922at2759; -.
DR   BioCyc; YEAST:YGR088W-MONOMER; -.
DR   BioGRID-ORCS; 852979; 0 hits in 10 CRISPR screens.
DR   PRO; PR:P06115; -.
DR   Proteomes; UP000002311; Chromosome VII.
DR   RNAct; P06115; Protein.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0005777; C:peroxisome; IBA:GO_Central.
DR   GO; GO:0004096; F:catalase activity; IDA:SGD.
DR   GO; GO:0020037; F:heme binding; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0042744; P:hydrogen peroxide catabolic process; IBA:GO_Central.
DR   GO; GO:0042542; P:response to hydrogen peroxide; IBA:GO_Central.
DR   GO; GO:0000302; P:response to reactive oxygen species; IMP:SGD.
DR   CDD; cd08157; catalase_fungal; 1.
DR   Gene3D; 2.40.180.10; Catalase core domain; 1.
DR   InterPro; IPR018028; Catalase.
DR   InterPro; IPR024708; Catalase_AS.
DR   InterPro; IPR024711; Catalase_clade1/3.
DR   InterPro; IPR011614; Catalase_core.
DR   InterPro; IPR002226; Catalase_haem_BS.
DR   InterPro; IPR010582; Catalase_immune_responsive.
DR   InterPro; IPR020835; Catalase_sf.
DR   PANTHER; PTHR11465; CATALASE; 1.
DR   PANTHER; PTHR11465:SF62; CATALASE T; 1.
DR   Pfam; PF00199; Catalase; 1.
DR   Pfam; PF06628; Catalase-rel; 1.
DR   PIRSF; PIRSF038928; Catalase_clade1-3; 1.
DR   PRINTS; PR00067; CATALASE.
DR   SMART; SM01060; Catalase; 1.
DR   SUPFAM; SSF56634; Heme-dependent catalase-like; 1.
DR   PROSITE; PS00437; CATALASE_1; 1.
DR   PROSITE; PS00438; CATALASE_2; 1.
DR   PROSITE; PS51402; CATALASE_3; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Direct protein sequencing; Heme; Hydrogen peroxide; Iron;
KW   Metal-binding; Oxidoreductase; Peroxidase; Reference proteome.
FT   CHAIN           1..562
FT                   /note="Catalase T"
FT                   /id="PRO_0000084929"
FT   ACT_SITE        64
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10013"
FT   ACT_SITE        137
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10013"
FT   BINDING         351
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        429
FT                   /note="D -> V (in Ref. 1; CAA28298)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        539
FT                   /note="C -> G (in Ref. 1; CAA28298)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   562 AA;  64583 MW;  1197842ADEAAE7D0 CRC64;
     MNVFGKKEEK QEKVYSLQNG FPYSHHPYAS QYSRPDGPIL LQDFHLLENI ASFDRERVPE
     RVVHAKGGGC RLEFELTDSL SDITYAAPYQ NVGYKCPGLV RFSTVGGESG TPDTARDPRG
     VSFKFYTEWG NHDWVFNNTP VFFLRDAIKF PVFIHSQKRD PQSHLNQFQD TTIYWDYLTL
     NPESIHQITY MFGDRGTPAS WASMNAYSGH SFIMVNKEGK DTYVQFHVLS DTGFETLTGD
     KAAELSGSHP DYNQAKLFTQ LQNGEKPKFN CYVQTMTPEQ ATKFRYSVND LTKIWPHKEF
     PLRKFGTITL TENVDNYFQE IEQVAFSPTN TCIPGIKPSN DSVLQARLFS YPDTQRHRLG
     ANYQQLPVNR PRNLGCPYSK GDSQYTAEQC PFKAVNFQRD GPMSYYNFGP EPNYISSLPN
     QTLKFKNEDN DEVSDKFKGI VLDEVTEVSV RKQEQDQIRN EHIVDAKINQ YYYVYGISPL
     DFEQPRALYE KVYNDEQKKL FVHNVVCHAC KIKDPKVKKR VTQYFGLLNE DLGKVIAECL
     GVPWEPVDLE GYAKTWSIAS AN
//
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