CATT_YEAST
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 03-AUG-2022, entry version 199.
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; 65.
DR DIP; DIP-4310N; -.
DR IntAct; P06115; 4.
DR STRING; 4932.YGR088W; -.
DR PeroxiBase; 5176; SceKat02.
DR iPTMnet; P06115; -.
DR MaxQB; P06115; -.
DR PaxDb; P06115; -.
DR PRIDE; P06115; -.
DR EnsemblFungi; YGR088W_mRNA; YGR088W; YGR088W.
DR GeneID; 852979; -.
DR KEGG; sce:YGR088W; -.
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; WDYLTQN; -.
DR BioCyc; YEAST:YGR088W-MON; -.
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 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; PTHR11465; 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; SSF56634; 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
