ID CATA_BOVIN Reviewed; 527 AA. AC P00432; Q3SZ80; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 02-SEP-2026, entry version 193. DE RecName: Full=Catalase; DE EC=1.11.1.6 {ECO:0000255|PROSITE-ProRule:PRU10013, ECO:0000269|PubMed:10691967}; GN Name=CAT; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae; OC Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Hereford; TISSUE=Rumen reticulum; RG NIH - Mammalian Gene Collection (MGC) project; RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases. RN [2] RP PROTEIN SEQUENCE OF 2-507, AND SUBCELLULAR LOCATION. RC TISSUE=Liver; RX PubMed=7082009; DOI=10.1016/0003-9861(82)90044-3; RA Schroeder W.A., Shelton J.R., Shelton J.B., Robberson B., Apell G., RA Fang R.S., Bonaventura J.; RT "The complete amino acid sequence of bovine liver catalase and the partial RT sequence of bovine erythrocyte catalase."; RL Arch. Biochem. Biophys. 214:397-421(1982). RN [3] RP CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=10691967; DOI=10.1046/j.1432-1327.2000.01091.x; RA Togo S.H., Maebuchi M., Yokota S., Bun-Ya M., Kawahara A., Kamiryo T.; RT "Immunological detection of alkaline-diaminobenzidine-negative peroxisomes RT of the nematode Caenorhabditis elegans. Purification and unique pH optima RT of peroxisomal catalase."; RL Eur. J. Biochem. 267:1307-1312(2000). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), AND ACTIVE SITE. RC TISSUE=Liver; RX PubMed=7328661; DOI=10.1016/0022-2836(81)90254-0; RA Murthy M.R.N., Reid T.J. III, Sicignano A., Tanaka N., Rossmann M.G.; RT "Structure of beef liver catalase."; RL J. Mol. Biol. 152:465-499(1981). RN [5] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS). RC TISSUE=Liver; RA Fita I., Silva A.M., Murthy M.R.N., Rossmann M.G.; RT "The refined structure of beef liver catalase at 2.5-A resolution."; RL Acta Crystallogr. B 42:497-515(1986). RN [6] {ECO:0007744|PDB:4BLC} RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH NADPH AND HEME, RP COFACTOR, AND SUBUNIT. RC TISSUE=Liver; RX PubMed=10417406; DOI=10.1107/s0907444999007052; RA Ko T.P., Day J., Malkin A.J., McPherson A.; RT "Structure of orthorhombic crystals of beef liver catalase."; RL Acta Crystallogr. D 55:1383-1394(1999). RN [7] RP SIMILARITY TO P.VITALE CATALASE. RX PubMed=3712444; DOI=10.1016/0022-2836(86)90480-8; RA Melik-Adamyan W.R., Barynin V.V., Vagin A.A., Borisov V.V., RA Vainshtein B.K., Fita I., Murthy M.R.N., Rossmann M.G.; RT "Comparison of beef liver and Penicillium vitale catalases."; RL J. Mol. Biol. 188:63-72(1986). CC -!- FUNCTION: Catalyzes the degradation of hydrogen peroxide (H(2)O(2)) CC generated by peroxisomal oxidases to water and oxygen, thereby CC protecting cells from the toxic effects of hydrogen peroxide CC (PubMed:10691967). Promotes growth of cells including T-cells, B-cells, CC myeloid leukemia cells, melanoma cells, mastocytoma cells and normal CC and transformed fibroblast cells (PubMed:10691967). CC {ECO:0000269|PubMed:10691967}. CC -!- CATALYTIC ACTIVITY: CC Reaction=2 H2O2 = O2 + 2 H2O; 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 ECO:0000269|PubMed:10691967}; CC -!- COFACTOR: CC Name=heme; Xref=ChEBI:CHEBI:30413; CC Evidence={ECO:0000269|PubMed:10417406}; CC -!- COFACTOR: CC Name=NADP(+); Xref=ChEBI:CHEBI:58349; CC Evidence={ECO:0000269|PubMed:10417406}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC pH dependence: CC Optimum pH is 7. {ECO:0000269|PubMed:10691967}; CC -!- SUBUNIT: Homotetramer (PubMed:10417406). Interacts (via microbody CC targeting signal) with PEX5, monomeric form interacts with PEX5, CC leading to its translocation into peroxisomes (By similarity). CC {ECO:0000250|UniProtKB:P04040, ECO:0000269|PubMed:10417406}. CC -!- SUBCELLULAR LOCATION: Peroxisome matrix {ECO:0000269|PubMed:7082009}. CC -!- SIMILARITY: Belongs to the catalase family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BC103066; AAI03067.1; -; mRNA. DR PIR; A00500; CSBO. DR RefSeq; NP_001030463.1; NM_001035386.2. DR PDB; 1TGU; X-ray; 2.80 A; A/B/C/D=2-507. DR PDB; 1TH2; X-ray; 2.80 A; A/B/C/D=2-507. DR PDB; 1TH3; X-ray; 2.80 A; A/B/C/D=2-507. DR PDB; 1TH4; X-ray; 2.98 A; A/B/C/D=2-507. DR PDB; 3J7B; EM; 3.20 A; A/B/C/D=1-527. DR PDB; 3NWL; X-ray; 2.69 A; A/B/C/D=1-527. DR PDB; 3RE8; X-ray; 1.90 A; A/B/C/D=4-502. DR PDB; 3RGP; X-ray; 1.88 A; A/B/C/D=4-502. DR PDB; 3RGS; X-ray; 1.99 A; A/B/C/D=4-502. DR PDB; 4BLC; X-ray; 2.30 A; A/B/C/D=2-507. DR PDB; 5GKN; EM; 3.20 A; A/B/C/D=1-527. DR PDB; 6JNT; EM; 3.00 A; A/B/C/D=1-527. DR PDB; 6JNU; EM; 3.00 A; A/B/C/D=1-527. DR PDB; 6PM7; X-ray; 1.85 A; A/B=1-527. DR PDB; 6PO0; X-ray; 1.75 A; A/B/C/D=1-527. DR PDB; 7CAT; X-ray; 2.50 A; A/B=2-507. DR PDB; 7DI8; EM; 3.20 A; A/B/C/D=1-527. DR PDB; 8CAT; X-ray; 2.50 A; A/B=2-507. DR PDB; 9BDJ; EM; 4.00 A; A/B/C/D=1-527. DR AlphaFoldDB; P00432; -. DR EMDB; EMD-44453; -. DR EMDB; EMD-6314; -. DR SASBDB; P00432; -. DR SMR; P00432; -. DR BioGRID; 188290; 1. DR ComplexPortal; CPX-4768; Catalase complex. DR FunCoup; P00432; 1470. DR IntAct; P00432; 1. DR STRING; 9913.ENSBTAP00000074355; -. DR BindingDB; P00432; -. DR ChEMBL; CHEMBL2227489; -. DR PeroxiBase; 5281; BtKat01. DR PaxDb; 9913-ENSBTAP00000074355; -. DR PeptideAtlas; P00432; -. DR Ensembl; ENSBTAT00000027941.8; ENSBTAP00000027941.5; ENSBTAG00000020980.8. DR Ensembl; ENSBTAT00085039632; ENSBTAP00085040824; ENSBTAG00085013758. DR Ensembl; ENSBTAT00090039188; ENSBTAP00090020109; ENSBTAG00090019244. DR GeneID; 531682; -. DR KEGG; bta:531682; -. DR CTD; 847; -. DR VEuPathDB; HostDB:ENSBTAG00000020980; -. DR VGNC; VGNC:26792; CAT. DR eggNOG; KOG0047; Eukaryota. DR GeneTree; ENSGT00390000018100; -. DR HOGENOM; CLU_010645_2_0_1; -. DR InParanoid; P00432; -. DR OrthoDB; 6880011at2759; -. DR BRENDA; 1.11.1.6; 908. DR Reactome; R-BTA-3299685; Detoxification of Reactive Oxygen Species. DR Reactome; R-BTA-6798695; Neutrophil degranulation. DR Reactome; R-BTA-9033241; Peroxisomal protein import. DR SABIO-RK; P00432; -. DR EvolutionaryTrace; P00432; -. DR PRO; PR:P00432; -. DR Proteomes; UP000009136; Chromosome 15. DR Bgee; ENSBTAG00000020980; Expressed in liver and 105 other cell types or tissues. DR ExpressionAtlas; P00432; baseline. DR GO; GO:0062151; C:catalase complex; IPI:ComplexPortal. DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central. DR GO; GO:0005782; C:peroxisomal matrix; EXP:UniProtKB. DR GO; GO:0005777; C:peroxisome; IBA:GO_Central. DR GO; GO:0004096; F:catalase activity; IDA:UniProtKB. DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB. DR GO; GO:0020037; F:heme binding; IBA:GO_Central. DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IDA:UniProtKB. DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro. DR CDD; cd08156; catalase_clade_3; 1. DR FunFam; 2.40.180.10:FF:000001; Catalase; 1. DR Gene3D; 2.40.180.10; Catalase core domain; 1. DR InterPro; IPR018028; Catalase. DR InterPro; IPR040333; Catalase_3. 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; CATALASE; 1. DR PANTHER; PTHR11465:SF9; CATALASE; 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; Heme-dependent catalase-like; 1. DR PROSITE; PS00437; CATALASE_1; 1. DR PROSITE; PS00438; CATALASE_2; 1. DR PROSITE; PS51402; CATALASE_3; 1. DR PDBsum; 1TGU; -. DR PDBsum; 1TH2; -. DR PDBsum; 1TH3; -. DR PDBsum; 1TH4; -. DR PDBsum; 3J7B; -. DR PDBsum; 3NWL; -. DR PDBsum; 3RE8; -. DR PDBsum; 3RGP; -. DR PDBsum; 3RGS; -. DR PDBsum; 4BLC; -. DR PDBsum; 5GKN; -. DR PDBsum; 6JNT; -. DR PDBsum; 6JNU; -. DR PDBsum; 6PM7; -. DR PDBsum; 6PO0; -. DR PDBsum; 7CAT; -. DR PDBsum; 7DI8; -. DR PDBsum; 8CAT; -. DR PDBsum; 9BDJ; -. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Direct protein sequencing; Heme; KW Hydrogen peroxide; Iron; Metal-binding; Mitogen; NADP; Oxidoreductase; KW Peroxidase; Peroxisome; Phosphoprotein; Reference proteome. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:7082009" FT CHAIN 2..527 FT /note="Catalase" FT /id="PRO_0000084898" FT REGION 1..42 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 524..527 FT /note="Microbody targeting signal; atypical" FT /evidence="ECO:0000250|UniProtKB:P04040" FT COMPBIAS 1..22 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 75 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10013, FT ECO:0000269|PubMed:7328661" FT ACT_SITE 148 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10013" FT BINDING 194 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000269|PubMed:10417406, FT ECO:0007744|PDB:4BLC" FT BINDING 198 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000269|PubMed:10417406, FT ECO:0007744|PDB:4BLC" FT BINDING 201 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000269|PubMed:10417406, FT ECO:0007744|PDB:4BLC" FT BINDING 203 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000269|PubMed:10417406, FT ECO:0007744|PDB:4BLC" FT BINDING 213 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:P04040" FT BINDING 215 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000269|PubMed:10417406, FT ECO:0007744|PDB:4BLC" FT BINDING 237 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000269|PubMed:10417406, FT ECO:0007744|PDB:4BLC" FT BINDING 303 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000269|PubMed:10417406, FT ECO:0007744|PDB:4BLC" FT BINDING 305 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000269|PubMed:10417406, FT ECO:0007744|PDB:4BLC" FT BINDING 358 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:0000269|PubMed:10417406, FT ECO:0007744|PDB:4BLC" FT BINDING 442 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000269|PubMed:10417406, FT ECO:0007744|PDB:4BLC" FT BINDING 445 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000269|PubMed:10417406, FT ECO:0007744|PDB:4BLC" FT BINDING 446 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000269|PubMed:10417406, FT ECO:0007744|PDB:4BLC" FT MOD_RES 2 FT /note="Blocked amino end (Ala); alternate" FT /evidence="ECO:0000269|PubMed:7082009" FT MOD_RES 2 FT /note="N-acetylalanine; alternate" FT /evidence="ECO:0000250|UniProtKB:P04040" FT MOD_RES 9 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P04040" FT MOD_RES 13 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:P24270" FT MOD_RES 221 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:P24270" FT MOD_RES 233 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P24270" FT MOD_RES 417 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P24270" FT MOD_RES 434 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P24270" FT MOD_RES 449 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P24270" FT MOD_RES 449 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P24270" FT MOD_RES 480 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P24270" FT MOD_RES 480 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P24270" FT MOD_RES 499 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P24270" FT MOD_RES 511 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P04040" FT MOD_RES 517 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P04040" FT CONFLICT 213 FT /note="N -> D (in Ref. 2; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 226 FT /note="N -> D (in Ref. 2; AA sequence)" FT /evidence="ECO:0000305" FT TURN 7..10 FT /evidence="ECO:0007829|PDB:6PO0" FT HELIX 11..18 FT /evidence="ECO:0007829|PDB:6PO0" FT TURN 19..21 FT /evidence="ECO:0007829|PDB:6PO0" FT HELIX 23..25 FT /evidence="ECO:0007829|PDB:6PO0" FT STRAND 38..40 FT /evidence="ECO:0007829|PDB:6PO0" FT STRAND 42..45 FT /evidence="ECO:0007829|PDB:6PO0" FT STRAND 50..53 FT /evidence="ECO:0007829|PDB:7DI8" FT HELIX 55..64 FT /evidence="ECO:0007829|PDB:6PO0" FT HELIX 70..72 FT /evidence="ECO:0007829|PDB:6PO0" FT STRAND 73..75 FT /evidence="ECO:0007829|PDB:3RGS" FT STRAND 77..87 FT /evidence="ECO:0007829|PDB:6PO0" FT TURN 92..94 FT /evidence="ECO:0007829|PDB:6PO0" FT HELIX 98..100 FT /evidence="ECO:0007829|PDB:6PO0" FT STRAND 106..114 FT /evidence="ECO:0007829|PDB:6PO0" FT STRAND 116..118 FT /evidence="ECO:0007829|PDB:3RGP" FT STRAND 124..128 FT /evidence="ECO:0007829|PDB:6PO0" FT STRAND 131..138 FT /evidence="ECO:0007829|PDB:6PO0" FT STRAND 141..151 FT /evidence="ECO:0007829|PDB:6PO0" FT HELIX 158..160 FT /evidence="ECO:0007829|PDB:6PO0" FT HELIX 161..168 FT /evidence="ECO:0007829|PDB:6PO0" FT TURN 172..174 FT /evidence="ECO:0007829|PDB:6PO0" FT HELIX 179..188 FT /evidence="ECO:0007829|PDB:6PO0" FT HELIX 190..192 FT /evidence="ECO:0007829|PDB:6PO0" FT HELIX 193..199 FT /evidence="ECO:0007829|PDB:6PO0" FT HELIX 202..204 FT /evidence="ECO:0007829|PDB:6PO0" FT STRAND 205..209 FT /evidence="ECO:0007829|PDB:6PO0" FT STRAND 220..223 FT /evidence="ECO:0007829|PDB:6PO0" FT STRAND 229..238 FT /evidence="ECO:0007829|PDB:6PO0" FT HELIX 247..256 FT /evidence="ECO:0007829|PDB:6PO0" FT HELIX 260..270 FT /evidence="ECO:0007829|PDB:6PO0" FT STRAND 276..284 FT /evidence="ECO:0007829|PDB:6PO0" FT HELIX 286..291 FT /evidence="ECO:0007829|PDB:6PO0" FT HELIX 302..304 FT /evidence="ECO:0007829|PDB:7CAT" FT TURN 305..307 FT /evidence="ECO:0007829|PDB:6PO0" FT STRAND 311..320 FT /evidence="ECO:0007829|PDB:6PO0" FT HELIX 326..330 FT /evidence="ECO:0007829|PDB:6PO0" FT STRAND 343..345 FT /evidence="ECO:0007829|PDB:6PO0" FT HELIX 349..365 FT /evidence="ECO:0007829|PDB:6PO0" FT HELIX 370..372 FT /evidence="ECO:0007829|PDB:6PO0" FT HELIX 374..376 FT /evidence="ECO:0007829|PDB:6PO0" FT TURN 395..400 FT /evidence="ECO:0007829|PDB:6PO0" FT STRAND 404..406 FT /evidence="ECO:0007829|PDB:6PO0" FT HELIX 416..418 FT /evidence="ECO:0007829|PDB:6PO0" FT HELIX 419..421 FT /evidence="ECO:0007829|PDB:6PO0" FT STRAND 424..431 FT /evidence="ECO:0007829|PDB:6PO0" FT STRAND 435..437 FT /evidence="ECO:0007829|PDB:4BLC" FT HELIX 441..445 FT /evidence="ECO:0007829|PDB:6PO0" FT HELIX 446..450 FT /evidence="ECO:0007829|PDB:6PO0" FT HELIX 453..467 FT /evidence="ECO:0007829|PDB:6PO0" FT HELIX 472..485 FT /evidence="ECO:0007829|PDB:6PO0" FT HELIX 487..500 FT /evidence="ECO:0007829|PDB:6PO0" SQ 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 //