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UniProtKB - Q9WYW0 (NPD_THEMA)
Protein
NAD-dependent protein deacetylase
Gene
cobB
Organism
Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)
Status
Functioni
NAD-dependent protein deacetylase which modulates the activities of several enzymes which are inactive in their acetylated form. Has also depropionylation activity in vitro. Also able to ADP-ribosylate peptide substrates with Arg or Lys in the +2 position. The role of this function in vivo is not clear.
UniRule annotation3 PublicationsCatalytic activityi
- H2O + N6-acetyl-L-lysyl-[protein] + NAD+ = 2''-O-acetyl-ADP-D-ribose + L-lysyl-[protein] + nicotinamideUniRule annotation1 PublicationEC:2.3.1.286UniRule annotation1 Publication
Cofactori
Zn2+UniRule annotation3 PublicationsNote: Binds 1 zinc ion per subunit.UniRule annotation3 Publications
Activity regulationi
Non-competitively inhibited by nicotinamide but not by nicotinic acid.1 Publication
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Active sitei | 116 | Proton acceptorCurated | 1 | |
Metal bindingi | 124 | Zinc | 1 | |
Metal bindingi | 127 | Zinc | 1 | |
Metal bindingi | 148 | Zinc | 1 | |
Metal bindingi | 151 | Zinc | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 21 – 40 | NADAdd BLAST | 20 | |
Nucleotide bindingi | 98 – 101 | NAD | 4 | |
Nucleotide bindingi | 188 – 190 | NAD | 3 | |
Nucleotide bindingi | 214 – 216 | NAD | 3 | |
Nucleotide bindingi | 231 – 232 | NAD | 2 |
GO - Molecular functioni
- NAD+ binding Source: GO_Central
- NAD-dependent histone deacetylase activity Source: GO_Central
- transferase activity Source: UniProtKB-KW
- zinc ion binding Source: UniProtKB-UniRule
Keywordsi
Molecular function | Transferase |
Ligand | Metal-binding, NAD, Zinc |
Enzyme and pathway databases
BRENDAi | 2.3.1.286, 6331 |
Names & Taxonomyi
Protein namesi | Recommended name: NAD-dependent protein deacetylaseUniRule annotation (EC:2.3.1.286UniRule annotation)Alternative name(s): Regulatory protein SIR2 homologUniRule annotation Short name: Sir2Tm |
Gene namesi | Name:cobBUniRule annotation Synonyms:sir2 Ordered Locus Names:TM_0490 |
Organismi | Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) |
Taxonomic identifieri | 243274 [NCBI] |
Taxonomic lineagei | Bacteria › Thermotogae › Thermotogales › Thermotogaceae › Thermotoga › |
Proteomesi |
|
Subcellular locationi
Cytoplasm and Cytosol
- Cytoplasm UniRule annotation
Other locations
- cytoplasm Source: UniProtKB-SubCell
Keywords - Cellular componenti
CytoplasmPathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 33 | F → A: Reduces kcat for NAD(+), greatly increases sensitivity to nicotinamide inhibition. 1 Publication | 1 | |
Mutagenesisi | 101 | D → N: Alters cosubstrate specificity, decreases Km for NAD(+), enzyme unable to discriminate between NAD(+) and nicotinic acid adenine dinucleotide (NAAD). 1 Publication | 1 | |
Mutagenesisi | 116 | H → A: 2-fold decrease in turnover and peptide affinity. 1 Publication | 1 | |
Mutagenesisi | 116 | H → Y: 10-fold decrease in turnover and peptide affinity. 1 Publication | 1 | |
Mutagenesisi | 165 | N → D: Increased affinity for substrate peptides with a lysine or arginine at position -1. 1 Publication | 1 |
Chemistry databases
ChEMBLi | CHEMBL3217404 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000110362 | 1 – 246 | NAD-dependent protein deacetylaseAdd BLAST | 246 |
Proteomic databases
PRIDEi | Q9WYW0 |
Interactioni
Protein-protein interaction databases
DIPi | DIP-29141N |
IntActi | Q9WYW0, 1 interactor |
STRINGi | 243274.THEMA_02220 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | Q9WYW0 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | Q9WYW0 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 4 – 246 | Deacetylase sirtuin-typeUniRule annotationAdd BLAST | 243 |
Sequence similaritiesi
Phylogenomic databases
eggNOGi | COG0846, Bacteria |
InParanoidi | Q9WYW0 |
OMAi | ERDCHGL |
Family and domain databases
Gene3Di | 3.30.1600.10, 1 hit |
HAMAPi | MF_01968, Sirtuin_ClassU, 1 hit |
IDEALi | IID90011 |
InterProi | View protein in InterPro IPR029035, DHS-like_NAD/FAD-binding_dom IPR003000, Sirtuin IPR026591, Sirtuin_cat_small_dom_sf IPR028628, Sirtuin_class_U IPR026590, Ssirtuin_cat_dom |
Pfami | View protein in Pfam PF02146, SIR2, 1 hit |
SUPFAMi | SSF52467, SSF52467, 1 hit |
PROSITEi | View protein in PROSITE PS50305, SIRTUIN, 1 hit |
i Sequence
Sequence statusi: Complete.
Q9WYW0-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MKMKEFLDLL NESRLTVTLT GAGISTPSGI PDFRGPNGIY KKYSQNVFDI
60 70 80 90 100
DFFYSHPEEF YRFAKEGIFP MLQAKPNLAH VLLAKLEEKG LIEAVITQNI
110 120 130 140 150
DRLHQRAGSK KVIELHGNVE EYYCVRCEKK YTVEDVIKKL ESSDVPLCDD
160 170 180 190 200
CNSLIRPNIV FFGENLPQDA LREAIGLSSR ASLMIVLGSS LVVYPAAELP
210 220 230 240
LITVRSGGKL VIVNLGETPF DDIATLKYNM DVVEFARRVM EEGGIS
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AE000512 Genomic DNA Translation: AAD35575.1 |
PIRi | A72370 |
RefSeqi | NP_228300.1, NC_000853.1 |
Genome annotation databases
EnsemblBacteriai | AAD35575; AAD35575; TM_0490 |
KEGGi | tma:TM0490 |
PATRICi | fig|243274.5.peg.497 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AE000512 Genomic DNA Translation: AAD35575.1 |
PIRi | A72370 |
RefSeqi | NP_228300.1, NC_000853.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1YC5 | X-ray | 1.40 | A | 1-246 | [»] | |
2H2D | X-ray | 1.70 | A | 1-246 | [»] | |
2H2F | X-ray | 2.20 | A | 1-246 | [»] | |
2H2G | X-ray | 1.63 | A | 1-246 | [»] | |
2H2H | X-ray | 2.20 | A | 1-246 | [»] | |
2H2I | X-ray | 1.80 | A | 1-246 | [»] | |
2H4F | X-ray | 2.00 | A | 1-246 | [»] | |
2H4H | X-ray | 1.99 | A | 1-246 | [»] | |
2H4J | X-ray | 2.10 | A | 1-246 | [»] | |
2H59 | X-ray | 1.90 | A/B | 1-246 | [»] | |
3D4B | X-ray | 1.90 | A | 1-246 | [»] | |
3D81 | X-ray | 2.50 | A | 1-246 | [»] | |
3JR3 | X-ray | 1.50 | A | 1-246 | [»] | |
3PDH | X-ray | 1.80 | A | 1-246 | [»] | |
4BUZ | X-ray | 1.90 | A | 1-246 | [»] | |
4BV2 | X-ray | 3.30 | A/B | 1-246 | [»] | |
SMRi | Q9WYW0 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
DIPi | DIP-29141N |
IntActi | Q9WYW0, 1 interactor |
STRINGi | 243274.THEMA_02220 |
Chemistry databases
ChEMBLi | CHEMBL3217404 |
Proteomic databases
PRIDEi | Q9WYW0 |
Protocols and materials databases
DNASUi | 897531 |
Genome annotation databases
EnsemblBacteriai | AAD35575; AAD35575; TM_0490 |
KEGGi | tma:TM0490 |
PATRICi | fig|243274.5.peg.497 |
Phylogenomic databases
eggNOGi | COG0846, Bacteria |
InParanoidi | Q9WYW0 |
OMAi | ERDCHGL |
Enzyme and pathway databases
BRENDAi | 2.3.1.286, 6331 |
Miscellaneous databases
EvolutionaryTracei | Q9WYW0 |
PROi | PR:Q9WYW0 |
Family and domain databases
Gene3Di | 3.30.1600.10, 1 hit |
HAMAPi | MF_01968, Sirtuin_ClassU, 1 hit |
IDEALi | IID90011 |
InterProi | View protein in InterPro IPR029035, DHS-like_NAD/FAD-binding_dom IPR003000, Sirtuin IPR026591, Sirtuin_cat_small_dom_sf IPR028628, Sirtuin_class_U IPR026590, Ssirtuin_cat_dom |
Pfami | View protein in Pfam PF02146, SIR2, 1 hit |
SUPFAMi | SSF52467, SSF52467, 1 hit |
PROSITEi | View protein in PROSITE PS50305, SIRTUIN, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | NPD_THEMA | |
Accessioni | Q9WYW0Primary (citable) accession number: Q9WYW0 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | October 31, 2003 |
Last sequence update: | November 1, 1999 | |
Last modified: | February 23, 2022 | |
This is version 132 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families