ID   CATT_YEAS7              Reviewed;         562 AA.
AC   A6ZV70;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 2.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=Catalase T;
DE            EC=1.11.1.6;
GN   Name=CTT1; ORFNames=SCY_2303;
OS   Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=307796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YJM789;
RX   PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA   Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA   Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA   Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA   Steinmetz L.M.;
RT   "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT   strain YJM789.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007).
CC   -!- FUNCTION: Occurs in almost all aerobically respiring organisms and
CC       serves to protect cells from the toxic effects of hydrogen peroxide.
CC       {ECO:0000250}.
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; Evidence={ECO:0000250};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- MISCELLANEOUS: This is one of two catalases in S.cerevisiae; the other
CC       is catalase A, which is the peroxisomal form.
CC   -!- SIMILARITY: Belongs to the catalase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EDN61678.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AAFW02000102; EDN61678.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; A6ZV70; -.
DR   SMR; A6ZV70; -.
DR   PRIDE; A6ZV70; -.
DR   EnsemblFungi; EDN61678; EDN61678; SCY_2303.
DR   HOGENOM; CLU_010645_2_0_1; -.
DR   Proteomes; UP000007060; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004096; F:catalase activity; IEA:UniProtKB-EC.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
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   3: Inferred from homology;
KW   Cytoplasm; Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase;
KW   Peroxidase.
FT   CHAIN           1..562
FT                   /note="Catalase T"
FT                   /id="PRO_0000330223"
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"
SQ   SEQUENCE   562 AA;  64567 MW;  E9A38D5572DAE104 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 DYNQTKLFTQ 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 DLGKVIAEGL
     GVPWEPVDLE GYAKTWSIAS AN