CATA_CANTR
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 03-AUG-2022, entry version 111.
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; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=5482;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 20336 / pK233 / NCYC 997;
RX PubMed=3691514; 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 sources.";
RL Eur. J. Biochem. 170:105-110(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=ATCC 20336 / pK233 / NCYC 997;
RX 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 acid
RT sequence of peroxisomal catalase of the yeast Candida tropicalis pK233.";
RL Gene 61:401-413(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 20336 / pK233 / NCYC 997;
RX 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 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 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 [GENOMIC DNA] OF 394-451, AND PROTEIN SEQUENCE OF 2-24;
RP 109-113; 222-236; 302-307; 394-403 AND 422-428.
RC STRAIN=ATCC 20336 / pK233 / NCYC 997;
RX 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 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 -!- SUBUNIT: Homotetramer.
CC -!- SUBCELLULAR LOCATION: Peroxisome.
CC -!- SIMILARITY: Belongs to the catalase family. {ECO:0000305}.
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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 AlphaFoldDB; P07820; -.
DR SMR; P07820; -.
DR PeroxiBase; 5256; CtKat01.
DR VEuPathDB; FungiDB:CTMYA2_025960; -.
DR VEuPathDB; FungiDB:CTRG_04203; -.
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 1: Evidence at protein level;
KW Direct protein sequencing; Heme; Hydrogen peroxide; Iron; Metal-binding;
KW Oxidoreductase; Peroxidase; Peroxisome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2440725"
FT CHAIN 2..485
FT /note="Peroxisomal catalase"
FT /id="PRO_0000084920"
FT ACT_SITE 53
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10013"
FT ACT_SITE 126
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10013"
FT BINDING 336
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"
FT CONFLICT 166
FT /note="T -> S (in Ref. 2; AAA34327)"
FT /evidence="ECO:0000305"
FT CONFLICT 377
FT /note="L -> V (in Ref. 4; CAA29093)"
FT /evidence="ECO:0000305"
FT CONFLICT 390
FT /note="I -> V (in Ref. 2; AAA34327)"
FT /evidence="ECO:0000305"
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
