Search by BoMiProt ID - Bomi4508

Primary Information

BoMiProt ID Bomi4508
Protein Name Catalase
Organism Bos taurus
Uniprot IDP00432
Milk FractionExosomes
Ref Sequence ID NP_001030463.1
Aminoacid Length 527
Molecular Weight 59915
FASTA Sequence Download
Gene Name CAT
Gene ID 531682
Protein Existence Status Reviewed

Secondary Information

Presence in other biological fluids/tissue/cells  liver
Protein Function Catalase is a key enzyme in the metabolism of H2O2 and reactive nitrogen species, and its expression and localization is markedly altered in tumors. 
Biochemical Properties Human catalase contains four identical subunits of 62 kDa, each subunit containing four distinct domains and one prosthetic heme group. The four domains include: (1) a N-terminal arm which contains a distal histidine, an essential amino acid for the catalase reaction; (2) a β-barrel domain that contains eight β-barrels arranged in an antiparallel fashion with six α-helical insertions, conferring the hydrophobic core of the protein necessary for the tri-dimensional structure of the enzyme; (3) a connection domain which contains the tyrosine residue that binds the heme group; and finally (4) an α-helical domains, which is important for NADPH binding.
PTMs N6-Acetylation at Lys, Phosphorylation at Ser
Site(s) of PTM(s)

N-glycosylation, O-glycosylation,
SCOP Class : All beta proteins
Fold : Streptavidin-like
Superfamily : Heme-dependent catalase-like
Family : Heme-dependent catalases
Domain Name : 4BLC A:3-501

CATH Matched CATH superfamily
Predicted Disorder Regions NA
DisProt Annotation
TM Helix Prediction No TM helices
PDB ID 1TGU, 1TH2, 1TH3, 1TH4, 3J7B, 3NWL, 3RE8, 3RGP, 3RGS, 4BLC, 5GKN, 6JNT, 6JNU, 6PM7, 6PO0, 7CAT, 7DI8, 8CAT,
Bibliography 1.Glorieux C, Calderon PB. Catalase, a remarkable enzyme: targeting the oldest antioxidant enzyme to find a new cancer treatment approach. Biol Chem. 2017 Sep 26;398(10):1095-1108. doi: 10.1515/hsz-2017-0131. PMID: 28384098. 2.Nagem, R.A., Martins, E.A., Goncalves, V.M., Aparicio, R., and Polikarpov, I. (1999). Crystallization and preliminary X-ray diffraction studies of human catalase. Acta Crystallogr. D Biol. Crystallogr. 55, 1614–1615.10.1107/S0907444999009695. 3.Zamocky, M. and Koller, F. (1999). Understanding the structure and function of catalases: clues from molecular evolution and in vitro mutagenesis. Prog. Biophys. Mol. Biol. 72, 19–66.10.1016/S0079-6107(98)00058-3. 4.Putnam, C.D., Arvai, A.S., Bourne, Y., and Tainer, J.A. (2000). Active and inhibited human catalase structures: ligand and NADPH binding and catalytic mechanism. J. Mol. Biol. 296, 295–309.10.1006/jmbi.1999.3458.