ID   CATA_CANBO              Reviewed;         504 AA.
AC   Q96VB8;
DT   23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=Peroxisomal catalase;
DE            EC=1.11.1.6;
GN   Name=CTA1;
OS   Candida boidinii (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Pichiaceae; Ogataea; Ogataea/Candida clade.
OX   NCBI_TaxID=5477;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SUBCELLULAR LOCATION.
RC   STRAIN=S2;
RX   PubMed=11591682; DOI=10.1128/jb.183.21.6372-6383.2001;
RA   Horiguchi H., Yurimoto H., Goh T.K., Nakagawa T., Kato N., Sakai Y.;
RT   "Peroxisomal catalase in the methylotrophic yeast Candida boidinii:
RT   transport efficiency and metabolic significance.";
RL   J. Bacteriol. 183:6372-6383(2001).
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   -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:11591682}.
CC       Note=Bimodally distributed between the cytosol and peroxisomes in
CC       methanol-grown cells but is localized exclusively in peroxisomes in
CC       oleate- and D-alanine-grown cells.
CC   -!- SIMILARITY: Belongs to the catalase family. {ECO:0000305}.
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DR   EMBL; AB064338; BAB69893.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q96VB8; -.
DR   SMR; Q96VB8; -.
DR   PeroxiBase; 5262; CboiKat01.
DR   PRIDE; Q96VB8; -.
DR   BioCyc; MetaCyc:MON-13166; -.
DR   GO; GO:0005777; C:peroxisome; 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   Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase;
KW   Peroxisome.
FT   CHAIN           1..504
FT                   /note="Peroxisomal catalase"
FT                   /id="PRO_0000084919"
FT   MOTIF           502..504
FT                   /note="Microbody targeting signal"
FT   ACT_SITE        63
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10013"
FT   ACT_SITE        136
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10013"
FT   BINDING         345
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   504 AA;  57095 MW;  CCF63C4FA752DC3B CRC64;
     MSNPPTYTTS QGCPVSDAFS TQRISGTKIS IKTPVGPLLL QDFKFLDSLA HFDRERIPER
     VVHAKGAGAY GVFEVTEDIS DICSAKFLDT VGKKTKIFTR FSTVGGEKGS SDSARDPRGF
     ATKFYTEEGN LDLVYNNTPI FFIRDPTKFP HFIHTQKRNP ATNCKDANMF WDYLTNNPES
     LHQIMYLFSN RGTPTSYRKM NGYSGHSYKW YNAKGEWVSS VHFISNQGVH NMTDEEAGDL
     SGKDPDFQTM DLYKAIEQGD YPSWECYVQT MTLEEAKKQP FSVYDLTKVW PHKDFPLRHF
     GKFTLNENAQ NYFAEVEQAA FSPSHTVPGM EPSNDPVLQS RLFSYPDTHR HRLGVNYSQI
     PVNCPMRAVF APQIRDGSMM VNGNLGGTPN YAGAYNCPVQ YQAPIKASSK TPEEQYEGET
     LSYDWTEVNE YDFYQPGRFW EVLGKTKGEQ EALVHNVANH VSGADEFIQD RVFAYFSKAN
     PVIGDLIRKE VLKKSPRGAS KNKF