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   16-JUN-2009, entry version 37.
DE   RecName: Full=Peroxisomal catalase;
DE            EC=1.11.1.6;
GN   Name=CTA1;
OS   Candida boidinii (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; mitosporic Saccharomycetales;
OC   Candida.
OX   NCBI_TaxID=5477;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SUBCELLULAR LOCATION.
RC   STRAIN=S2;
RX   MEDLINE=21475782; PubMed=11591682;
RX   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
CC       peroxide.
CC   -!- CATALYTIC ACTIVITY: 2 H(2)O(2) = O(2) + 2 H(2)O.
CC   -!- COFACTOR: Heme group.
CC   -!- SUBCELLULAR LOCATION: Peroxisome. Note=Bimodally distributed
CC       between the cytosol and peroxisomes in methanol-grown cells but is
CC       localized exclusively in peroxisomes in oleate- and D-alanine-
CC       grown cells.
CC   -!- SIMILARITY: Belongs to the catalase family.
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DR   EMBL; AB064338; BAB69893.1; -; Genomic_DNA.
DR   HSSP; P15202; 1A4E.
DR   PeroxiBase; 5262; CboiKat01.
DR   BioCyc; MetaCyc:MON-13166; -.
DR   BRENDA; 1.11.1.6; 675.
DR   GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR   GO; GO:0004096; F:catalase activity; IEA:EC.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR002226; Catalase.
DR   InterPro; IPR010582; Catalase-rel_immune_responsive.
DR   InterPro; IPR011614; Catalase_N.
DR   InterPro; IPR018028; Catalase_rel_subgroup.
DR   Gene3D; G3DSA:2.40.180.10; Catalase_N; 1.
DR   PANTHER; PTHR11465; Catalase; 1.
DR   Pfam; PF00199; Catalase; 1.
DR   Pfam; PF06628; Catalase-rel; 1.
DR   PRINTS; PR00067; CATALASE.
DR   ProDom; PD000510; Catalase; 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;
KW   Peroxidase; Peroxisome.
FT   CHAIN         1    504       Peroxisomal catalase.
FT                                /FTId=PRO_0000084919.
FT   MOTIF       502    504       Microbody targeting signal.
FT   ACT_SITE     63     63       By similarity.
FT   ACT_SITE    136    136       By similarity.
FT   METAL       345    345       Iron (heme axial ligand) (By similarity).
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
//