Detail Information for IndEnz0007000013
IED ID IndEnz0007000013
Enzyme Type ID catalase000013
Protein Name Catalase
EC 1.11.1.6
Gene Name CAT
Organism Homo sapiens (Human)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human)
Enzyme Sequence MADSRDPASDQMQHWKEQRAAQKADVLTTGAGNPVGDKLNVITVGPRGPLLVQDVVFTDEMAHFDRERIPERVVHAKGAGAFGYFEVTHDITKYSKAKVFEHIGKKTPIAVRFSTVAGESGSADTVRDPRGFAVKFYTEDGNWDLVGNNTPIFFIRDPILFPSFIHSQKRNPQTHLKDPDMVWDFWSLRPESLHQVSFLFSDRGIPDGHRHMNGYGSHTFKLVNANGEAVYCKFHYKTDQGIKNLSVEDAARLSQEDPDYGIRDLFNAIATGKYPSWTFYIQVMTFNQAETFPFNPFDLTKVWPHKDYPLIPVGKLVLNRNPVNYFAEVEQIAFDPSNMPPGIEASPDKMLQGRLFAYPDTHRHRLGPNYLHIPVNCPYRARVANYQRDGPMCMQDNQGGAPNYYPNSFGAPEQQPSALEHSIQYSGEVRRFNTANDDNVTQVRAFYVNVLNEEQRKRLCENIAGHLKDAQIFIQKKAVKNFTEVHPDYGSHIQALLDKYNAEKPKNAIHTFVQSGSHLAAREKANL
Enzyme Length 527
Uniprot Accession Number P04040
Absorption
Active Site ACT_SITE 75; ACT_SITE 148
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=2 H2O2 = 2 H2O + O2; Xref=Rhea:RHEA:20309, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240; EC=1.11.1.6; Evidence={ECO:0000255|PROSITE-ProRule:PRU10013, ECO:0000269|PubMed:7882369};
DNA Binding
EC Number 1.11.1.6
Enzyme Function FUNCTION: Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide. Promotes growth of cells including T-cells, B-cells, myeloid leukemia cells, melanoma cells, mastocytoma cells and normal and transformed fibroblast cells. {ECO:0000269|PubMed:7882369}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (2); Beta strand (18); Chain (1); Helix (21); Initiator methionine (1); Metal binding (1); Modified residue (14); Sequence conflict (9); Turn (7)
Keywords 3D-structure;Acetylation;Direct protein sequencing;Heme;Hydrogen peroxide;Iron;Metal-binding;Mitogen;NADP;Oxidoreductase;Peroxidase;Peroxisome;Phosphoprotein;Reference proteome
Interact With Itself
Induction
Subcellular Location SUBCELLULAR LOCATION: Peroxisome.
Modified Residue MOD_RES 2; /note="N-acetylalanine"; /evidence="ECO:0007744|PubMed:25944712"; MOD_RES 9; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:24275569"; MOD_RES 221; /note="N6-succinyllysine"; /evidence="ECO:0000250|UniProtKB:P24270"; MOD_RES 233; /note="N6-acetyllysine"; /evidence="ECO:0000250|UniProtKB:P24270"; MOD_RES 306; /note="N6-acetyllysine; alternate"; /evidence="ECO:0000250|UniProtKB:P24270"; MOD_RES 306; /note="N6-succinyllysine; alternate"; /evidence="ECO:0000250|UniProtKB:P24270"; MOD_RES 417; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:P24270"; MOD_RES 422; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:24275569"; MOD_RES 480; /note="N6-acetyllysine; alternate"; /evidence="ECO:0000250|UniProtKB:P24270"; MOD_RES 480; /note="N6-succinyllysine; alternate"; /evidence="ECO:0000250|UniProtKB:P24270"; MOD_RES 499; /note="N6-acetyllysine"; /evidence="ECO:0000250|UniProtKB:P24270"; MOD_RES 511; /note="Phosphothreonine"; /evidence="ECO:0007744|PubMed:24275569"; MOD_RES 515; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"; MOD_RES 517; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:24275569"
Post Translational Modification PTM: The N-terminus is blocked.
Signal Peptide
Structure 3D X-ray crystallography (6); Electron microscopy (2)
Cross Reference PDB 1DGB; 1DGF; 1DGG; 1DGH; 1F4J; 1QQW; 7P8W; 7VD9;
Mapped Pubmed ID 10022913; 10567208; 11101887; 11182520; 11350569; 11479740; 11837458; 11907164; 12032677; 12110367; 12165738; 12231449; 12372460; 12447480; 12456682; 12468545; 12469627; 12487379; 12516882; 12559034; 12578380; 12603857; 12606529; 12730222; 12777400; 12824748; 12838770; 12885776; 12950161; 14580687; 14710363; 14962975; 15125229; 15131792; 15133753; 15182856; 15203188; 15472150; 15528999; 15556604; 15733034; 15735318; 15774926; 15800961; 15870505; 15890005; 15934434; 15988600; 16026777; 16047490; 16076760; 16098030; 16192345; 16204228; 16298864; 16385446; 16387755; 16424062; 16453382; 16467073; 16504657; 16523188; 16586065; 16600249; 16630078; 16644728; 16729966; 16773213; 16775184; 16868544; 16956821; 17005595; 17007944; 17145829; 17171548; 17209132; 17213227; 17264407; 17548672; 17549373; 17566139; 17567676; 17567781; 17577741; 17601350; 17634480; 17646900; 17693525; 17696155; 17850515; 17937824; 18048809; 18171680; 18248894; 18353692; 18368408; 18415766; 18423055; 18469277; 18483329; 18485895; 18606005; 18634817; 18682580; 18712838; 18829504; 18930811; 18936436; 18949620; 18977241; 19050255; 19064360; 19092850; 19124506; 19170196; 19172437; 19197237; 19242068; 19255063; 19274593; 19336475; 19341793; 19373626; 19399816; 19409565; 19424819; 19497990; 19505917; 19538885; 19584060; 19584075; 19615732; 19622717; 19625176; 19632994; 19688952; 19692168; 19705749; 19731237; 19787204; 19855359; 19863340; 19874574; 19896490; 19897513; 19897742; 19902075; 19929244; 19949914; 1999334; 20020532; 20049130; 20078877; 20082261; 20097730; 20105444; 20109103; 20110814; 20178365; 20194081; 20235792; 20301895; 20416077; 20444272; 20485444; 20494887; 20562859; 20613769; 20628086; 20643115; 20649881; 20711500; 20727719; 20732340; 20851292; 20878976; 20923778; 21053180; 21054578; 21069346; 21083503; 21109199; 21131394; 21179281; 21180245; 21191398; 21295602; 21417634; 21689642; 21799178; 21827848; 21829032; 21911577; 21921984; 21947853; 21964540; 21968610; 21976670; 21985133; 21985966; 21988832; 22002062; 22058000; 22089180; 22108257; 22167619; 22242279; 22286031; 22645453; 22736749; 22747494; 22880027; 22907559; 22958044; 22959522; 22970972; 22998821; 23066387; 23098659; 23212700; 23325794; 23333653; 23340375; 23383735; 23390647; 23425094; 23461612; 23606334; 23641975; 23650620; 23701472; 23746122; 23771908; 23773345; 23827365; 23828460; 23868633; 23911407; 23961996; 23963456; 24057136; 24189400; 24211614; 24215654; 24235149; 24305782; 24456074; 24517502; 24583396; 24602691; 24630930; 24817970; 24824229; 24825136; 24915010; 25007762; 25033027; 25085901; 25086217; 25139332; 25154023; 25248722; 25307973; 25484013; 25514903; 25576221; 25609649; 25667417; 25697005; 25739358; 25772105; 25786472; 25818327; 25837760; 25837767; 25854684; 25866291; 25894370; 26045794; 26074427; 26117330; 26125826; 26130326; 26198800; 26220973; 26342455; 26496610; 26523980; 26674569; 26787049; 26817806; 26970563; 27206672; 27206673; 27225276; 27225983; 27302388; 27449288; 27515707; 27534583; 27591797; 27704307; 27706591; 27731402; 27735913; 27751366; 27848965; 27914828; 28058676; 28141554; 28167245; 28206724; 28222320; 28397206; 28436704; 28512644; 28547970; 28554099; 28652427; 28655148; 28711952; 28749186; 28760655; 28765278; 28787099; 28829657; 29028686; 29421935; 29467184; 29496557; 29535798; 29753736; 29782990; 29859283; 29924645; 29953407; 30191955; 30225256; 30326254; 30422963; 30574618; 30600457; 30680511; 31120146; 31617239; 31646444; 31947722; 32203639; 33009206; 33359244; 33425072; 33708335; 33710662; 34001853; 34420848; 34427017; 34530960; 34907237; 35275189; 7719337; 7790377; 8824437; 8858165; 9653144; 9668159; 9837948;
Motif
Gene Encoded By
Mass 59,756
Kinetics
Metal Binding METAL 358; /note=Iron (heme axial ligand)
Rhea ID RHEA:20309
Cross Reference Brenda 1.11.1.6;