ID   CATA_CANTR              Reviewed;         485 AA.
AC   P07820;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 4.
DT   16-JUN-2009, entry version 69.
DE   RecName: Full=Peroxisomal catalase;
DE            EC=1.11.1.6;
DE   AltName: Full=PXP-9;
GN   Name=POX9;
OS   Candida tropicalis (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; mitosporic Saccharomycetales;
OC   Candida.
OX   NCBI_TaxID=5482;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=88082804; PubMed=3691514;
RX   DOI=10.1111/j.1432-1033.1987.tb13673.x;
RA   Okada H., Ueda M., Sugaya T., Atomi H., Mozaffar S., Hishida T.,
RA   Teranishi Y., Okazaki K., Takechi T., Kamiryo T., Tanaka A.;
RT   "Catalase gene of the yeast Candida tropicalis. Sequence analysis and
RT   comparison with peroxisomal and cytosolic catalases from other
RT   sources.";
RL   Eur. J. Biochem. 170:105-110(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=ATCC 20336 / pK233 / NCYC 997;
RX   MEDLINE=88185842; PubMed=3446581; DOI=10.1016/0378-1119(87)90202-2;
RA   Murray W.W., Rachubinski R.A.;
RT   "The nucleotide sequence of complementary DNA and the deduced amino
RT   acid sequence of peroxisomal catalase of the yeast Candida tropicalis
RT   pK233.";
RL   Gene 61:401-413(1987).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 20336 / pK233 / NCYC 997;
RX   MEDLINE=89263811; PubMed=2726500; DOI=10.1093/nar/17.9.3600;
RA   Murray W.W., Rachubinski R.A.;
RT   "Nucleotide sequence of peroxisomal catalase from the yeast Candida
RT   tropicalis pK233: identification of an upstream BamHI site
RT   polymorphism.";
RL   Nucleic Acids Res. 17:3600-3600(1989).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 377-385.
RC   STRAIN=ATCC 20336 / pK233 / NCYC 997;
RX   MEDLINE=87214216; PubMed=3580373; DOI=10.1016/0167-4781(87)90044-3;
RA   Rachubinski R.A., Fujiki Y., Lazarow P.B.;
RT   "Isolation of cDNA clones coding for peroxisomal proteins of Candida
RT   tropicalis: identification and sequence of a clone for catalase.";
RL   Biochim. Biophys. Acta 909:35-43(1987).
RN   [5]
RP   NUCLEOTIDE SEQUENCE OF 394-451, AND PARTIAL PROTEIN SEQUENCE.
RX   MEDLINE=87276567; PubMed=2440725; DOI=10.1016/0014-5793(87)80870-0;
RA   Ueda M., Okada H., Hishida T., Teranishi Y., Tanaka A.;
RT   "Isolation of several cDNAs encoding yeast peroxisomal enzymes.";
RL   FEBS Lett. 220:31-35(1987).
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   -!- SUBUNIT: Homotetramer.
CC   -!- SUBCELLULAR LOCATION: Peroxisome.
CC   -!- SIMILARITY: Belongs to the catalase family.
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DR   EMBL; M18832; AAA34327.1; -; mRNA.
DR   EMBL; X05886; CAA29310.1; -; mRNA.
DR   EMBL; X05604; CAA29093.1; -; mRNA.
DR   EMBL; X06660; CAA29859.1; -; Genomic_DNA.
DR   EMBL; X13978; CAA32159.1; -; Genomic_DNA.
DR   PIR; A29629; CSCKPT.
DR   HSSP; P15202; 1A4E.
DR   PeroxiBase; 5256; CtKat01.
DR   BRENDA; 1.11.1.6; 1242.
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   1: Evidence at protein level;
KW   Direct protein sequencing; Heme; Hydrogen peroxide; Iron;
KW   Metal-binding; Oxidoreductase; Peroxidase; Peroxisome.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    485       Peroxisomal catalase.
FT                                /FTId=PRO_0000084920.
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    166    166       T -> S (in Ref. 2; AAA34327).
FT   CONFLICT    377    377       L -> V (in Ref. 4; CAA29093).
FT   CONFLICT    390    390       I -> V (in Ref. 2; AAA34327).
SQ   SEQUENCE   485 AA;  54938 MW;  612629F910FF4E8D CRC64;
     MAPTFTNSNG QPIPEPFATQ RVGQHGPLLL QDFNLIDSLA HFDRERIPER VVHAKGSGAY
     GVFEVTDDIT DVCAAKFLDT VGKKTRIFTR FSTVGGELGS ADTARDPRGF ATKFYTEEGN
     LDLVYNNTPV FFIRDPSKFP HFIHTQKRNP ETHLKDANMF WDYLTTNEES VHQVMVLFSD
     RGTPASYREM NGYSGHTYKW SNNKGEWFYV QVHFISDQGI KTLTNEEAGS LAGSNPDYAQ
     EDLFKNIAAG NYPSWTCYIQ TMTEAQAKEA EFSVFDLTKV WPHGKYPMRR FGKFTLNENP
     KNYFAEVEQA AFSPAHTVPH MEPSADPVLQ SRLFSYADTH RHRLGTNYTQ IPVNCPVTGA
     VFNPHMRDGA MNVNGNLGNH PNYLASDKPI EFKQFSLQED QEVWHGAATP FHWKATPADF
     KQATELWKVL KKYPNQQEHL AHNVAVHASA ADAPIQDRVI AYFTKVHPDL GDLIKKEILE
     LSPRK
//