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Catalase (EC 1.11.1.6)

 CATA_CANLF              Reviewed;         527 AA.
O97492; Q9GKY3;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
25-OCT-2017, entry version 113.
RecName: Full=Catalase;
EC=1.11.1.6;
Name=CAT;
Canis lupus familiaris (Dog) (Canis familiaris).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae;
Canis.
NCBI_TaxID=9615;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Beagle; TISSUE=Liver;
PubMed=10524763; DOI=10.3109/10425179809008475;
Nakamura K., Watanabe M., Ikeda T.;
"cDNA and deduced amino acid sequences of dog catalase.";
DNA Seq. 9:347-352(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ACATALASEMIA THR-327.
STRAIN=Beagle;
PubMed=11137458; DOI=10.1016/S1357-2725(00)00057-1;
Nakamura K., Watanabe M., Takanaka K., Sasaki Y., Ikeda T.;
"cDNA cloning of mutant catalase in acatalasemic beagle dog: single
nucleotide substitution leading to thermal-instability and enhanced
proteolysis of mutant enzyme.";
Int. J. Biochem. Cell Biol. 32:1183-1193(2000).
-!- FUNCTION: Occurs in almost all aerobically respiring organisms and
serves to protect cells from the toxic effects of hydrogen
peroxide. Promotes growth of cells.
-!- CATALYTIC ACTIVITY: 2 H(2)O(2) = O(2) + 2 H(2)O.
{ECO:0000255|PROSITE-ProRule:PRU10013}.
-!- COFACTOR:
Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
-!- COFACTOR:
Name=NADP(+); Xref=ChEBI:CHEBI:58349; Evidence={ECO:0000250};
-!- SUBUNIT: Homotetramer. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000250}.
-!- DISEASE: Note=Defects in CAT are the cause of acatalasia; also
known as acatalasemia. This disease is characterized by absence of
catalase activity. {ECO:0000269|PubMed:11137458}.
-!- SIMILARITY: Belongs to the catalase family. {ECO:0000305}.
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EMBL; AB012918; BAA36420.1; -; mRNA.
EMBL; AB038231; BAB20764.1; -; mRNA.
RefSeq; NP_001002984.1; NM_001002984.1.
UniGene; Cfa.188; -.
ProteinModelPortal; O97492; -.
SMR; O97492; -.
STRING; 9615.ENSCAFP00000010324; -.
PeroxiBase; 5319; CfaKat01.
PaxDb; O97492; -.
PRIDE; O97492; -.
Ensembl; ENSCAFT00000011146; ENSCAFP00000010324; ENSCAFG00000006941.
GeneID; 403474; -.
KEGG; cfa:403474; -.
CTD; 847; -.
eggNOG; KOG0047; Eukaryota.
eggNOG; COG0753; LUCA.
GeneTree; ENSGT00390000018100; -.
HOGENOM; HOG000087852; -.
HOVERGEN; HBG003986; -.
InParanoid; O97492; -.
KO; K03781; -.
OMA; HADFGRM; -.
OrthoDB; EOG091G04V5; -.
TreeFam; TF300540; -.
Reactome; R-CFA-3299685; Detoxification of Reactive Oxygen Species.
Reactome; R-CFA-6798695; Neutrophil degranulation.
Proteomes; UP000002254; Chromosome 18.
Bgee; ENSCAFG00000006941; -.
GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
GO; GO:0005777; C:peroxisome; IBA:GO_Central.
GO; GO:0004096; F:catalase activity; IBA:GO_Central.
GO; GO:0020037; F:heme binding; IBA:GO_Central.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0042744; P:hydrogen peroxide catabolic process; IBA:GO_Central.
GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
GO; GO:0042542; P:response to hydrogen peroxide; IBA:GO_Central.
Gene3D; 2.40.180.10; -; 1.
InterPro; IPR018028; Catalase.
InterPro; IPR024708; Catalase_AS.
InterPro; IPR024711; Catalase_clade1/3.
InterPro; IPR011614; Catalase_core.
InterPro; IPR037060; Catalase_core_sf.
InterPro; IPR002226; Catalase_haem_BS.
InterPro; IPR010582; Catalase_immune_responsive.
InterPro; IPR020835; Catalase_sf.
PANTHER; PTHR11465; PTHR11465; 1.
Pfam; PF00199; Catalase; 1.
Pfam; PF06628; Catalase-rel; 1.
PIRSF; PIRSF038928; Catalase_clade1-3; 1.
PRINTS; PR00067; CATALASE.
SMART; SM01060; Catalase; 1.
SUPFAM; SSF56634; SSF56634; 1.
PROSITE; PS00437; CATALASE_1; 1.
PROSITE; PS00438; CATALASE_2; 1.
PROSITE; PS51402; CATALASE_3; 1.
1: Evidence at protein level;
Acetylation; Complete proteome; Disease mutation; Heme;
Hydrogen peroxide; Iron; Metal-binding; Mitogen; NADP; Oxidoreductase;
Peroxidase; Peroxisome; Phosphoprotein; Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P04040}.
CHAIN 2 527 Catalase.
/FTId=PRO_0000084899.
ACT_SITE 75 75 {ECO:0000255|PROSITE-ProRule:PRU10013}.
ACT_SITE 148 148 {ECO:0000255|PROSITE-ProRule:PRU10013}.
METAL 358 358 Iron (heme axial ligand). {ECO:0000250}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000250|UniProtKB:P04040}.
MOD_RES 9 9 Phosphoserine.
{ECO:0000250|UniProtKB:P04040}.
MOD_RES 13 13 N6-succinyllysine.
{ECO:0000250|UniProtKB:P24270}.
MOD_RES 221 221 N6-succinyllysine.
{ECO:0000250|UniProtKB:P24270}.
MOD_RES 233 233 N6-acetyllysine.
{ECO:0000250|UniProtKB:P24270}.
MOD_RES 422 422 Phosphoserine.
{ECO:0000250|UniProtKB:P04040}.
MOD_RES 434 434 Phosphoserine.
{ECO:0000250|UniProtKB:P24270}.
MOD_RES 449 449 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P24270}.
MOD_RES 449 449 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P24270}.
MOD_RES 480 480 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P24270}.
MOD_RES 480 480 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P24270}.
MOD_RES 499 499 N6-acetyllysine.
{ECO:0000250|UniProtKB:P24270}.
MOD_RES 511 511 Phosphothreonine.
{ECO:0000250|UniProtKB:P04040}.
MOD_RES 517 517 Phosphoserine.
{ECO:0000250|UniProtKB:P04040}.
VARIANT 327 327 A -> T (in acatalasemia; heat-labile).
{ECO:0000269|PubMed:11137458}.
SEQUENCE 527 AA; 59797 MW; CC0BC7F88FE2C2AC CRC64;
MADSRDPASD QMKLWKEQRA AQKPDVLTTG GGNPIGDKLN VMTAGPRGPL LVQDVVFTDE
MAHFDRERIP ERVVHAKGAG AFGYFEVTHD ITKYSKAKVF EHIGKRTPIA VRFSTVAGES
GSADTVRDPR GFAVKFYTED GNWDLVGNNT PIFFIRDAIL FPSFIHSQKR NPQTHLKDPD
MVWDFWSLRP ESLHQVSFLF SDRGIPDGHR HMNGYGSHTF KLVNAAGEAV YCKFHYKTDQ
GIKNLSVEDA ARLSHEDPDY GLRDLFNAIA TGNYPSWTFY IQVMTFSQAE TFPFNPFDLT
KIWPHQDYPL IPVGKLVLNR NPVNYFAEVE QMAFDPSNMP PGIEPSPDKM LQGRLFAYPD
THRHRLGPNY LQIPVNCPFR ARVANYQRDG PMCMLDNQGG APNYYPNSFS APEQQRCVLE
HSSQCSPDVQ RFNSANEDNV TQVRTFYLKV LGEEERKRLC ENIAGHLKDA QLFIQKKAVK
NFSDVHPDYG ARIQALLDKY NAEKPKNAIH TFMQHGSHLA AREKANL


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