ID   CATA_CANAL              Reviewed;         487 AA.
AC   O13289; O42616; Q5AAT2; Q9URJ7;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 4.
DT   16-JUN-2009, entry version 53.
DE   RecName: Full=Peroxisomal catalase;
DE            EC=1.11.1.6;
GN   Name=CTA1; Synonyms=CAT1; ORFNames=CaO19.6229, CaO19.13609;
OS   Candida albicans (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; mitosporic Saccharomycetales;
OC   Candida.
OX   NCBI_TaxID=5476;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 10261 / CBS 2718 / IFO 1061;
RX   MEDLINE=98234019; PubMed=9573075;
RA   Wysong D.R., Christin L., Sugar A.M., Robbins P.W., Diamond R.D.;
RT   "Cloning and sequencing of a Candida albicans catalase gene and
RT   effects of disruption of this gene.";
RL   Infect. Immun. 66:1953-1961(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND FUNCTION.
RC   STRAIN=FC18;
RX   PubMed=18352908; DOI=10.1111/j.1348-0421.2008.00006.x;
RA   Nakagawa Y.;
RT   "Catalase gene disruptant of the human pathogenic yeast Candida
RT   albicans is defective in hyphal growth, and a catalase-specific
RT   inhibitor can suppress hyphal growth of wild-type cells.";
RL   Microbiol. Immunol. 52:16-24(2008).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC5314;
RX   PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA   Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S.,
RA   Magee B.B., Newport G., Thorstenson Y.R., Agabian N., Magee P.T.,
RA   Davis R.W., Scherer S.;
RT   "The diploid genome sequence of Candida albicans.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
CC   -!- FUNCTION: Occurs in almost all aerobically respiring organisms and
CC       serves to protect cells from the toxic effects of hydrogen
CC       peroxide. Required for hyphal growth.
CC   -!- CATALYTIC ACTIVITY: 2 H(2)O(2) = O(2) + 2 H(2)O.
CC   -!- COFACTOR: Heme group.
CC   -!- SUBUNIT: Homotetramer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Peroxisome (By similarity).
CC   -!- SIMILARITY: Belongs to the catalase family.
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DR   EMBL; U40704; AAC39448.1; -; Genomic_DNA.
DR   EMBL; AB006327; BAA21767.1; -; mRNA.
DR   EMBL; AB006328; BAA21768.1; -; Genomic_DNA.
DR   EMBL; AACQ01000038; EAK99824.1; -; Genomic_DNA.
DR   EMBL; AACQ01000037; EAK99912.1; -; Genomic_DNA.
DR   RefSeq; XP_718734.1; -.
DR   RefSeq; XP_718818.1; -.
DR   HSSP; P15202; 1A4E.
DR   GeneID; 3639495; -.
DR   GeneID; 3639575; -.
DR   BRENDA; 1.11.1.6; 1124.
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   2: Evidence at transcript level;
KW   Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase;
KW   Peroxidase; Peroxisome.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    487       Peroxisomal catalase.
FT                                /FTId=PRO_0000084918.
FT   ACT_SITE     53     53       By similarity.
FT   ACT_SITE    126    126       By similarity.
FT   METAL       336    336       Iron (heme axial ligand) (By similarity).
FT   CONFLICT    114    114       I -> F (in Ref. 2; BAA21767 and 3;
FT                                EAK99824/EAK99912).
FT   CONFLICT    224    224       N -> T (in Ref. 2; BAA21767 and 3;
FT                                EAK99824/EAK99912).
FT   CONFLICT    284    284       R -> K (in Ref. 2; BAA21767 and 3;
FT                                EAK99824/EAK99912).
FT   CONFLICT    288    288       M -> L (in Ref. 2; BAA21767 and 3;
FT                                EAK99824/EAK99912).
FT   CONFLICT    301    301       E -> K (in Ref. 2; BAA21767 and 3;
FT                                EAK99824/EAK99912).
FT   CONFLICT    342    342       Missing (in Ref. 2; BAA21767 and 3;
FT                                EAK99824/EAK99912).
FT   CONFLICT    367    367       S -> M (in Ref. 2; BAA21767 and 3;
FT                                EAK99824/EAK99912).
FT   CONFLICT    398    399       SF -> L (in Ref. 2; BAA21767 and 3;
FT                                EAK99824/EAK99912).
SQ   SEQUENCE   487 AA;  55063 MW;  16C1A0EA163C658C CRC64;
     MAPTFTNSNG QPIPEPFATQ RVGQHGPLLL QDFNLIDSLA HFDRERIPER VVHAKGSGAY
     GVFEVTDDIT DICAAKFLDT VGKKTRIFTR FSTVGGELGS ADTARDPRGF ATKIYTEEGN
     LDLVYNNTPV FFIRDPSKFP HFIHTQKRNP ETHLKDANMF WDYLTSNEES IHQVMVLFSD
     RGTPASYREM NGYSGHTYKW SNKKGEWFYV QVHFISDQGI KTLNNEEAGA LAGSNPDYAQ
     EDLFKNIAAG NYPSWTAYIQ TMTEAEAKEA EFSVFDLTKV WPHRKYPMRR FGKFTLNENP
     ENYFAEVEQA AFSPAHTVPY MEPSADPVLQ SRLFSYADTH RPHRLGTNYT QIPVNCPVTG
     AVFNPHSRDG AMTVNGNLGS HPNYLASDKP VEFKQFSSFQ EDQEVWNGAA TPFHWKATPA
     DFKQAQELWK VLKRYPNQQE HLAHNIAVHA AGADAAIQDR VFAYFGKVSQ DLADAIKKEV
     LELSPRK
//