CATA_BOVIN
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 03-AUG-2022, entry version 177.
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.
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).
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]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
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: Occurs in almost all aerobically respiring organisms and
CC serves to protect cells from the toxic effects of hydrogen peroxide.
CC Promotes growth of cells.
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 ECO:0000269|PubMed:10691967};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC -!- COFACTOR:
CC Name=NADP(+); Xref=ChEBI:CHEBI:58349;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7. {ECO:0000269|PubMed:10691967};
CC -!- SUBUNIT: Homotetramer.
CC -!- SUBCELLULAR LOCATION: Peroxisome.
CC -!- SIMILARITY: Belongs to the catalase family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Worthington enzyme manual;
CC URL="https://www.worthington-biochem.com/CTL/";
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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 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 AlphaFoldDB; P00432; -.
DR SASBDB; P00432; -.
DR SMR; P00432; -.
DR ComplexPortal; CPX-4768; Catalase complex.
DR IntAct; P00432; 1.
DR STRING; 9913.ENSBTAP00000027941; -.
DR BindingDB; P00432; -.
DR ChEMBL; CHEMBL2227489; -.
DR PeroxiBase; 5281; BtKat01.
DR PaxDb; P00432; -.
DR PeptideAtlas; P00432; -.
DR PRIDE; P00432; -.
DR Ensembl; ENSBTAT00000027941; ENSBTAP00000027941; ENSBTAG00000020980.
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; 507937at2759; -.
DR TreeFam; TF300540; -.
DR BRENDA; 1.11.1.6; 908.
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 tissues.
DR ExpressionAtlas; P00432; baseline and differential.
DR GO; GO:0062151; C:catalase complex; IPI:ComplexPortal.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IDA:UniProtKB.
DR GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
DR GO; GO:0042542; P:response to hydrogen peroxide; IBA:GO_Central.
DR CDD; cd08156; catalase_clade_3; 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; 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 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:0000250|UniProtKB:P04040,
FT 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 COMPBIAS 1..21
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 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:7328661"
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 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 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 TURN 305..307
FT /evidence="ECO:0007829|PDB:6PO0"
FT STRAND 311..320
FT /evidence="ECO:0007829|PDB:6PO0"
FT HELIX 325..328
FT /evidence="ECO:0007829|PDB:6PO0"
FT TURN 329..331
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 STRAND 424..431
FT /evidence="ECO:0007829|PDB:6PO0"
FT STRAND 435..437
FT /evidence="ECO:0007829|PDB:4BLC"
FT HELIX 441..448
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
