| IED ID | IndEnz0007000657 |
| Enzyme Type ID | catalase000657 |
| Protein Name |
NAD-dependent protein deacetylase sirtuin-3 EC 2.3.1.286 Regulatory protein SIR2 homolog 3 SIR2-like protein 3 mSIR2L3 |
| Gene Name | Sirt3 Sir2l3 |
| Organism | Mus musculus (Mouse) |
| 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 Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Mus Mus Mus musculus (Mouse) |
| Enzyme Sequence | MALDPLGAVVLQSIMALSGRLALAALRLWGPGGGRRPISLCVGASGGFGGGGSSEKKFSLQDVAELLRTRACSRVVVMVGAGISTPSGIPDFRSPGSGLYSNLQQYDIPYPEAIFELGFFFHNPKPFFMLAKELYPGHYRPNVTHYFLRLLHDKELLLRLYTQNIDGLERASGIPASKLVEAHGTFVTATCTVCRRSFPGEDIWADVMADRVPRCPVCTGVVKPDIVFFGEQLPARFLLHMADFALADLLLILGTSLEVEPFASLSEAVQKSVPRLLINRDLVGPFVLSPRRKDVVQLGDVVHGVERLVDLLGWTQELLDLMQRERGKLDGQDR |
| Enzyme Length | 334 |
| Uniprot Accession Number | Q8R104 |
| Absorption | |
| Active Site | ACT_SITE 183; /note=Proton acceptor; /evidence=ECO:0000255|PROSITE-ProRule:PRU00236 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=H2O + N(6)-acetyl-L-lysyl-[protein] + NAD(+) = 2''-O-acetyl-ADP-D-ribose + L-lysyl-[protein] + nicotinamide; Xref=Rhea:RHEA:43636, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15377, ChEBI:CHEBI:17154, ChEBI:CHEBI:29969, ChEBI:CHEBI:57540, ChEBI:CHEBI:61930, ChEBI:CHEBI:83767; EC=2.3.1.286; Evidence={ECO:0000255|PROSITE-ProRule:PRU00236, ECO:0000269|PubMed:21858060, ECO:0000269|PubMed:26620563, ECO:0000305|PubMed:17923681, ECO:0000305|PubMed:18794531, ECO:0000305|PubMed:21172655, ECO:0000305|PubMed:23835326}; |
| DNA Binding | |
| EC Number | 2.3.1.286 |
| Enzyme Function | FUNCTION: NAD-dependent protein deacetylase (PubMed:23835326, PubMed:17923681, PubMed:18794531, PubMed:21172655, PubMed:26620563). Activates or deactivates mitochondrial target proteins by deacetylating key lysine residues (PubMed:23835326, PubMed:17923681, PubMed:18794531, PubMed:21172655). Known targets include ACSS1, IDH, GDH, PDHA1, SOD2, LCAD, SDHA and the ATP synthase subunit ATP5PO (PubMed:16790548, PubMed:18794531, PubMed:21172655). Contributes to the regulation of the cellular energy metabolism (PubMed:23835326). Important for regulating tissue-specific ATP levels (PubMed:18794531, PubMed:24252090). In response to metabolic stress, deacetylates transcription factor FOXO3 and recruits FOXO3 and mitochondrial RNA polymerase POLRMT to mtDNA to promote mtDNA transcription (PubMed:23283301). Acts as a regulator of ceramide metabolism by mediating deacetylation of ceramide synthases CERS1, CERS2 and CERS6, thereby increasing their activity and promoting mitochondrial ceramide accumulation (PubMed:26620563). {ECO:0000269|PubMed:16790548, ECO:0000269|PubMed:17923681, ECO:0000269|PubMed:18794531, ECO:0000269|PubMed:21172655, ECO:0000269|PubMed:21858060, ECO:0000269|PubMed:23283301, ECO:0000269|PubMed:23835326, ECO:0000269|PubMed:24252090, ECO:0000269|PubMed:26620563}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | NP_BIND 80..100; /note=NAD; /evidence=ECO:0000250|UniProtKB:Q9NTG7; NP_BIND 163..166; /note=NAD; /evidence=ECO:0000250|UniProtKB:Q9NTG7; NP_BIND 254..256; /note=NAD; /evidence=ECO:0000250|UniProtKB:Q9NTG7; NP_BIND 279..281; /note=NAD; /evidence=ECO:0000250|UniProtKB:Q9NTG7 |
| Features | Active site (1); Alternative sequence (1); Chain (1); Domain (1); Metal binding (4); Modified residue (1); Nucleotide binding (4); Sequence conflict (4); Transit peptide (1) |
| Keywords | Alternative splicing;Cytoplasm;Metal-binding;Mitochondrion;NAD;Reference proteome;Transferase;Transit peptide;Zinc |
| Interact With | P47738 |
| Induction | INDUCTION: Sirt3 expression decreases by 50% in skeletal muscle upon fasting. {ECO:0000269|PubMed:23835326}. |
| Subcellular Location | SUBCELLULAR LOCATION: [Isoform L]: Mitochondrion matrix {ECO:0000269|PubMed:19241369, ECO:0000269|PubMed:19333382, ECO:0000269|PubMed:23283301}.; SUBCELLULAR LOCATION: [Isoform S]: Cytoplasm {ECO:0000269|PubMed:11056054}. |
| Modified Residue | MOD_RES 57; /note=N6-succinyllysine; /evidence=ECO:0007744|PubMed:23806337 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 11217851; 12466851; 14610273; 15653680; 16602821; 18054327; 18363549; 18614015; 18710944; 18719589; 18799693; 18824292; 19410549; 19652361; 19940131; 20000467; 20042612; 20059953; 20129246; 20157566; 20203611; 20235147; 20644252; 20661474; 20677216; 21044047; 21094524; 21109197; 21109198; 21165558; 21212461; 21255725; 21390294; 21397863; 21449565; 21454513; 21664458; 21677750; 21720390; 21840382; 21856199; 21873205; 22394676; 22416140; 22645641; 22956852; 23139766; 23201123; 23236377; 23375372; 23396452; 23397292; 23508103; 23576753; 23643077; 23767918; 24039710; 24047466; 24051248; 24073283; 24121500; 24194600; 24344202; 24363305; 24370889; 24454908; 24748594; 24909164; 24966184; 25090966; 25192254; 25284742; 25384422; 25404738; 25470550; 25489948; 25505263; 25555707; 25566066; 25607838; 25681462; 25748450; 25757953; 25759382; 25782072; 25790176; 25811481; 25830335; 25863253; 25948682; 25962702; 26121691; 26319214; 26358839; 26403315; 26464666; 26472659; 26523980; 26524632; 26667039; 26698917; 26767982; 26769382; 26789108; 26868537; 26873966; 26928655; 27000941; 27021965; 27040510; 27047337; 27052737; 27128560; 27295248; 27304511; 27423420; 27540894; 27613967; 27620507; 27626380; 27681422; 27794418; 27815257; 27880725; 27881304; 28236057; 28255277; 28258190; 28286268; 28296029; 28369333; 28375738; 28396567; 28437863; 28449871; 28465484; 28480597; 28500761; 28579116; 28584055; 28603486; 28662362; 28673962; 28684630; 28687409; 28724806; 28808064; 28862956; 28878358; 28911171; 28914882; 28935506; 29031725; 29076061; 29130578; 29198988; 29236713; 29277324; 29302794; 29330215; 29363727; 29444200; 29466723; 29574628; 29589261; 29634313; 29650970; 29674007; 29689547; 29721150; 29765980; 29777578; 29915018; 29958828; 29972782; 30056271; 30171880; 30219671; 30250024; 30362958; 30368983; 30389773; 30411306; 30445987; 30487750; 30510203; 30525304; 30545041; 30584213; 30726738; 30735837; 30774023; 30794763; 30801823; 30846716; 30848932; 30849386; 30970248; 31015456; 31060926; 31085231; 31160717; 31185214; 31201798; 31208274; 31269804; 31302001; 31340681; 31409767; 31632409; 31641228; 31652451; 31712596; 31773668; 31818974; 31849939; 31852393; 31858519; 31876685; 31936019; 31936371; 31991048; 32026628; 32119761; 32212196; 32296036; 32439965; 32447338; 32463172; 32468895; 32485218; 32500353; 32524313; 32526680; 32658908; 32721927; 32722183; 32726464; 32770173; 32835604; 32898015; 32912335; 32933152; 32951306; 33002579; 33006225; 33049518; 33107080; 33131100; 33327751; 33359008; 33371209; 33385630; 33448325; 33531400; 33541361; 33586458; 33664465; 33665656; 33690226; 33744652; 33770326; 33789208; 33805532; 33823364; 33878033; 33900547; 33973685; 34119577; 34122726; 34180125; 34181898; 34202229; 34272364; 34370691; 34405591; 3444409; 34478012; 34571997; 34591326; 34606850; 34624325; 34630854; 34644302; 34695364; 34780879; 34807408; 34849375; 34880332; 35011652; 35234263; |
| Motif | |
| Gene Encoded By | |
| Mass | 36,615 |
| Kinetics | |
| Metal Binding | METAL 191; /note=Zinc; /evidence=ECO:0000255|PROSITE-ProRule:PRU00236; METAL 194; /note=Zinc; /evidence=ECO:0000255|PROSITE-ProRule:PRU00236; METAL 215; /note=Zinc; /evidence=ECO:0000255|PROSITE-ProRule:PRU00236; METAL 218; /note=Zinc; /evidence=ECO:0000255|PROSITE-ProRule:PRU00236 |
| Rhea ID | RHEA:43636 |
| Cross Reference Brenda | 2.3.1.286; |