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Catalase (EC 1.11.1.6)

 CATA_BOVIN              Reviewed;         527 AA.
P00432; Q3SZ80;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
12-SEP-2018, entry version 157.
RecName: Full=Catalase;
EC=1.11.1.6;
Name=CAT;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Hereford; TISSUE=Rumen reticulum;
NIH - Mammalian Gene Collection (MGC) project;
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
[2]
PROTEIN SEQUENCE OF 2-507.
TISSUE=Liver;
PubMed=7082009; DOI=10.1016/0003-9861(82)90044-3;
Schroeder W.A., Shelton J.R., Shelton J.B., Robberson B., Apell G.,
Fang R.S., Bonaventura J.;
"The complete amino acid sequence of bovine liver catalase and the
partial sequence of bovine erythrocyte catalase.";
Arch. Biochem. Biophys. 214:397-421(1982).
[3]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
TISSUE=Liver;
PubMed=7328661; DOI=10.1016/0022-2836(81)90254-0;
Murthy M.R.N., Reid T.J. III, Sicignano A., Tanaka N., Rossmann M.G.;
"Structure of beef liver catalase.";
J. Mol. Biol. 152:465-499(1981).
[4]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
TISSUE=Liver;
Fita I., Silva A.M., Murthy M.R.N., Rossmann M.G.;
"The refined structure of beef liver catalase at 2.5-A resolution.";
Acta Crystallogr. B 42:497-515(1986).
[5]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
TISSUE=Liver;
PubMed=10417406; DOI=10.1107/S0907444999007052;
Ko T.P., Day J., Malkin A.J., McPherson A.;
"Structure of orthorhombic crystals of beef liver catalase.";
Acta Crystallogr. D 55:1383-1394(1999).
[6]
SIMILARITY TO P.VITALE CATALASE.
PubMed=3712444; DOI=10.1016/0022-2836(86)90480-8;
Melik-Adamyan W.R., Barynin V.V., Vagin A.A., Borisov V.V.,
Vainshtein B.K., Fita I., Murthy M.R.N., Rossmann M.G.;
"Comparison of beef liver and Penicillium vitale catalases.";
J. Mol. Biol. 188:63-72(1986).
-!- 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;
-!- COFACTOR:
Name=NADP(+); Xref=ChEBI:CHEBI:58349;
-!- SUBUNIT: Homotetramer.
-!- SUBCELLULAR LOCATION: Peroxisome.
-!- SIMILARITY: Belongs to the catalase family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Worthington enzyme manual;
URL="http://www.worthington-biochem.com/CTL/";
-----------------------------------------------------------------------
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EMBL; BC103066; AAI03067.1; -; mRNA.
PIR; A00500; CSBO.
RefSeq; NP_001030463.1; NM_001035386.2.
UniGene; Bt.48925; -.
PDB; 1TGU; X-ray; 2.80 A; A/B/C/D=2-507.
PDB; 1TH2; X-ray; 2.80 A; A/B/C/D=2-507.
PDB; 1TH3; X-ray; 2.80 A; A/B/C/D=2-507.
PDB; 1TH4; X-ray; 2.98 A; A/B/C/D=2-507.
PDB; 3J7B; EM; 3.20 A; A/B/C/D=1-527.
PDB; 3NWL; X-ray; 2.69 A; A/B/C/D=1-527.
PDB; 3RE8; X-ray; 1.90 A; A/B/C/D=4-502.
PDB; 3RGP; X-ray; 1.88 A; A/B/C/D=4-502.
PDB; 3RGS; X-ray; 1.99 A; A/B/C/D=4-502.
PDB; 4BLC; X-ray; 2.30 A; A/B/C/D=2-507.
PDB; 5GKN; EM; 3.20 A; A/B/C/D=1-527.
PDB; 7CAT; X-ray; 2.50 A; A/B=2-507.
PDB; 8CAT; X-ray; 2.50 A; A/B=2-507.
PDBsum; 1TGU; -.
PDBsum; 1TH2; -.
PDBsum; 1TH3; -.
PDBsum; 1TH4; -.
PDBsum; 3J7B; -.
PDBsum; 3NWL; -.
PDBsum; 3RE8; -.
PDBsum; 3RGP; -.
PDBsum; 3RGS; -.
PDBsum; 4BLC; -.
PDBsum; 5GKN; -.
PDBsum; 7CAT; -.
PDBsum; 8CAT; -.
ProteinModelPortal; P00432; -.
SMR; P00432; -.
IntAct; P00432; 1.
STRING; 9913.ENSBTAP00000027941; -.
ChEMBL; CHEMBL2227489; -.
PeroxiBase; 5281; BtKat01.
PaxDb; P00432; -.
PeptideAtlas; P00432; -.
PRIDE; P00432; -.
Ensembl; ENSBTAT00000027941; ENSBTAP00000027941; ENSBTAG00000020980.
GeneID; 531682; -.
KEGG; bta:531682; -.
CTD; 847; -.
VGNC; VGNC:26792; CAT.
eggNOG; KOG0047; Eukaryota.
eggNOG; COG0753; LUCA.
GeneTree; ENSGT00390000018100; -.
HOGENOM; HOG000087852; -.
HOVERGEN; HBG003986; -.
InParanoid; P00432; -.
KO; K03781; -.
OMA; HADFGRM; -.
OrthoDB; EOG091G04V5; -.
TreeFam; TF300540; -.
BRENDA; 1.11.1.6; 908.
Reactome; R-BTA-3299685; Detoxification of Reactive Oxygen Species.
Reactome; R-BTA-6798695; Neutrophil degranulation.
Reactome; R-BTA-9033241; Peroxisomal protein import.
SABIO-RK; P00432; -.
EvolutionaryTrace; P00432; -.
PRO; PR:P00432; -.
Proteomes; UP000009136; Chromosome 15.
Bgee; ENSBTAG00000020980; Expressed in 9 organ(s), highest expression level in liver.
GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
GO; GO:0005778; C:peroxisomal membrane; IEA:Ensembl.
GO; GO:0005777; C:peroxisome; IBA:GO_Central.
GO; GO:0004046; F:aminoacylase activity; IEA:Ensembl.
GO; GO:0004096; F:catalase activity; IDA:UniProtKB.
GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
GO; GO:0020037; F:heme binding; IBA:GO_Central.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0050661; F:NADP binding; IEA:Ensembl.
GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
GO; GO:0005102; F:signaling receptor binding; IEA:Ensembl.
GO; GO:0009060; P:aerobic respiration; IEA:Ensembl.
GO; GO:0008203; P:cholesterol metabolic process; IEA:Ensembl.
GO; GO:0020027; P:hemoglobin metabolic process; IEA:Ensembl.
GO; GO:0042744; P:hydrogen peroxide catabolic process; IBA:GO_Central.
GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; IEA:Ensembl.
GO; GO:0055114; P:oxidation-reduction process; IDA:UniProtKB.
GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IEA:Ensembl.
GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IEA:Ensembl.
GO; GO:0051289; P:protein homotetramerization; IEA:Ensembl.
GO; GO:0042542; P:response to hydrogen peroxide; IBA:GO_Central.
GO; GO:0006641; P:triglyceride metabolic process; IEA:Ensembl.
GO; GO:0009650; P:UV protection; IEA:Ensembl.
InterPro; IPR018028; Catalase.
InterPro; IPR024708; Catalase_AS.
InterPro; IPR024711; Catalase_clade1/3.
InterPro; IPR011614; Catalase_core.
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;
3D-structure; Acetylation; Complete proteome;
Direct protein sequencing; Heme; Hydrogen peroxide; Iron;
Metal-binding; Mitogen; NADP; Oxidoreductase; Peroxidase; Peroxisome;
Phosphoprotein; Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P04040,
ECO:0000269|PubMed:7082009}.
CHAIN 2 527 Catalase.
/FTId=PRO_0000084898.
ACT_SITE 75 75 {ECO:0000255|PROSITE-ProRule:PRU10013,
ECO:0000269|PubMed:7328661}.
ACT_SITE 148 148
METAL 358 358 Iron (heme axial ligand).
{ECO:0000269|PubMed:7328661}.
MOD_RES 2 2 Blocked amino end (Ala); alternate.
{ECO:0000269|PubMed:7082009}.
MOD_RES 2 2 N-acetylalanine; alternate.
{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 417 417 Phosphoserine.
{ECO:0000250|UniProtKB:P24270}.
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}.
CONFLICT 213 213 N -> D (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 226 226 N -> D (in Ref. 2; AA sequence).
{ECO:0000305}.
TURN 7 10 {ECO:0000244|PDB:3RGP}.
HELIX 11 18 {ECO:0000244|PDB:3RGP}.
TURN 19 21 {ECO:0000244|PDB:3RGP}.
STRAND 38 40 {ECO:0000244|PDB:3RGP}.
STRAND 42 45 {ECO:0000244|PDB:3RGP}.
HELIX 55 64 {ECO:0000244|PDB:3RGP}.
STRAND 73 75 {ECO:0000244|PDB:3RGS}.
STRAND 77 87 {ECO:0000244|PDB:3RGP}.
TURN 92 94 {ECO:0000244|PDB:3RGP}.
HELIX 98 100 {ECO:0000244|PDB:3RGP}.
STRAND 106 114 {ECO:0000244|PDB:3RGP}.
STRAND 116 118 {ECO:0000244|PDB:3RGP}.
STRAND 124 128 {ECO:0000244|PDB:3RGP}.
STRAND 131 138 {ECO:0000244|PDB:3RGP}.
STRAND 141 151 {ECO:0000244|PDB:3RGP}.
HELIX 158 160 {ECO:0000244|PDB:3RGP}.
HELIX 161 168 {ECO:0000244|PDB:3RGP}.
TURN 172 174 {ECO:0000244|PDB:3RGP}.
HELIX 179 188 {ECO:0000244|PDB:3RGP}.
HELIX 190 192 {ECO:0000244|PDB:3RGP}.
HELIX 193 199 {ECO:0000244|PDB:3RGP}.
HELIX 202 204 {ECO:0000244|PDB:3RGP}.
STRAND 205 209 {ECO:0000244|PDB:3RGP}.
STRAND 220 223 {ECO:0000244|PDB:3RGP}.
STRAND 229 238 {ECO:0000244|PDB:3RGP}.
HELIX 247 256 {ECO:0000244|PDB:3RGP}.
HELIX 260 270 {ECO:0000244|PDB:3RGP}.
STRAND 276 284 {ECO:0000244|PDB:3RGP}.
HELIX 286 291 {ECO:0000244|PDB:3RGP}.
TURN 305 307 {ECO:0000244|PDB:3RGP}.
STRAND 311 320 {ECO:0000244|PDB:3RGP}.
HELIX 325 328 {ECO:0000244|PDB:3RGP}.
TURN 329 331 {ECO:0000244|PDB:3RGP}.
STRAND 343 345 {ECO:0000244|PDB:3RGP}.
HELIX 349 365 {ECO:0000244|PDB:3RGP}.
HELIX 370 372 {ECO:0000244|PDB:3RGP}.
HELIX 374 376 {ECO:0000244|PDB:3RGP}.
TURN 395 400 {ECO:0000244|PDB:3RGP}.
STRAND 404 406 {ECO:0000244|PDB:3RGP}.
HELIX 416 418 {ECO:0000244|PDB:3RGP}.
STRAND 424 430 {ECO:0000244|PDB:3RGP}.
STRAND 435 437 {ECO:0000244|PDB:4BLC}.
HELIX 441 448 {ECO:0000244|PDB:3RGP}.
HELIX 453 467 {ECO:0000244|PDB:3RGP}.
HELIX 472 485 {ECO:0000244|PDB:3RGP}.
HELIX 487 500 {ECO:0000244|PDB:3RGP}.
SEQUENCE 527 AA; 59915 MW; 2F97E793153D7AF9 CRC64;
MADNRDPASD QMKHWKEQRA AQKPDVLTTG GGNPVGDKLN SLTVGPRGPL LVQDVVFTDE
MAHFDRERIP ERVVHAKGAG AFGYFEVTHD ITRYSKAKVF EHIGKRTPIA VRFSTVAGES
GSADTVRDPR GFAVKFYTED GNWDLVGNNT PIFFIRDALL FPSFIHSQKR NPQTHLKDPD
MVWDFWSLRP ESLHQVSFLF SDRGIPDGHR HMNGYGSHTF KLVNANGEAV YCKFHYKTDQ
GIKNLSVEDA ARLAHEDPDY GLRDLFNAIA TGNYPSWTLY IQVMTFSEAE IFPFNPFDLT
KVWPHGDYPL IPVGKLVLNR NPVNYFAEVE QLAFDPSNMP PGIEPSPDKM LQGRLFAYPD
THRHRLGPNY LQIPVNCPYR ARVANYQRDG PMCMMDNQGG APNYYPNSFS APEHQPSALE
HRTHFSGDVQ RFNSANDDNV TQVRTFYLKV LNEEQRKRLC ENIAGHLKDA QLFIQKKAVK
NFSDVHPEYG SRIQALLDKY NEEKPKNAVH TYVQHGSHLS AREKANL


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