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Protein

NAD-dependent protein deacetylase

Gene

cobB

Organism
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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 Publications

Catalytic activityi

NAD+ + an acetylprotein = nicotinamide + O-acetyl-ADP-ribose + a protein.UniRule annotation1 Publication

Cofactori

Zn2+UniRule annotation3 PublicationsNote: Binds 1 zinc ion per subunit.UniRule annotation3 Publications

Enzyme regulationi

Non-competitively inhibited by nicotinamide but not by nicotinic acid.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei116Proton acceptorCurated1
Metal bindingi124Zinc1
Metal bindingi127Zinc1
Metal bindingi148Zinc1
Metal bindingi151Zinc1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi21 – 40NADAdd BLAST20
Nucleotide bindingi98 – 101NAD4
Nucleotide bindingi188 – 190NAD3
Nucleotide bindingi214 – 216NAD3
Nucleotide bindingi231 – 232NAD2

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Metal-binding, NAD, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
NAD-dependent protein deacetylaseUniRule annotation (EC:3.5.1.-UniRule annotation)
Alternative name(s):
Regulatory protein SIR2 homologUniRule annotation
Short name:
Sir2Tm
Gene namesi
Name:cobBUniRule annotation
Synonyms:sir2
Ordered Locus Names:TM_0490
OrganismiThermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Taxonomic identifieri243274 [NCBI]
Taxonomic lineageiBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga
Proteomesi
  • UP000008183 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi33F → A: Reduces kcat for NAD(+), greatly increases sensitivity to nicotinamide inhibition. 1 Publication1
Mutagenesisi101D → N: Alters cosubstrate specificity, decreases Km for NAD(+), enzyme unable to discriminate between NAD(+) and nicotinic acid adenine dinucleotide (NAAD). 1 Publication1
Mutagenesisi116H → A: 2-fold decrease in turnover and peptide affinity. 1 Publication1
Mutagenesisi116H → Y: 10-fold decrease in turnover and peptide affinity. 1 Publication1
Mutagenesisi165N → D: Increased affinity for substrate peptides with a lysine or arginine at position -1. 1 Publication1

Chemistry databases

ChEMBLiCHEMBL3217404.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001103621 – 246NAD-dependent protein deacetylaseAdd BLAST246

Interactioni

Protein-protein interaction databases

DIPiDIP-29141N.
STRINGi243274.TM0490.

Structurei

Secondary structure

1246
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi4 – 12Combined sources9
Beta strandi14 – 20Combined sources7
Helixi22 – 24Combined sources3
Helixi26 – 28Combined sources3
Beta strandi33 – 35Combined sources3
Helixi38 – 42Combined sources5
Turni45 – 48Combined sources4
Helixi50 – 55Combined sources6
Helixi57 – 67Combined sources11
Helixi69 – 73Combined sources5
Helixi78 – 88Combined sources11
Beta strandi93 – 97Combined sources5
Helixi103 – 106Combined sources4
Beta strandi112 – 114Combined sources3
Beta strandi117 – 124Combined sources8
Turni125 – 127Combined sources3
Beta strandi130 – 132Combined sources3
Helixi133 – 139Combined sources7
Turni140 – 142Combined sources3
Beta strandi143 – 145Combined sources3
Turni149 – 151Combined sources3
Beta strandi154 – 159Combined sources6
Helixi168 – 180Combined sources13
Beta strandi182 – 188Combined sources7
Helixi196 – 198Combined sources3
Helixi199 – 206Combined sources8
Beta strandi209 – 213Combined sources5
Helixi221 – 223Combined sources3
Beta strandi225 – 228Combined sources4
Helixi232 – 243Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1YC5X-ray1.40A1-246[»]
2H2DX-ray1.70A1-246[»]
2H2FX-ray2.20A1-246[»]
2H2GX-ray1.63A1-246[»]
2H2HX-ray2.20A1-246[»]
2H2IX-ray1.80A1-246[»]
2H4FX-ray2.00A1-246[»]
2H4HX-ray1.99A1-246[»]
2H4JX-ray2.10A1-246[»]
2H59X-ray1.90A/B1-246[»]
3D4BX-ray1.90A1-246[»]
3D81X-ray2.50A1-246[»]
3JR3X-ray1.50A1-246[»]
3PDHX-ray1.80A1-246[»]
4BUZX-ray1.90A1-246[»]
4BV2X-ray3.30A/B1-246[»]
ProteinModelPortaliQ9WYW0.
SMRiQ9WYW0.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9WYW0.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini4 – 246Deacetylase sirtuin-typeUniRule annotationAdd BLAST243

Sequence similaritiesi

Belongs to the sirtuin family. Class U subfamily.UniRule annotation
Contains 1 deacetylase sirtuin-type domain.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105NDF. Bacteria.
COG0846. LUCA.
InParanoidiQ9WYW0.
KOiK12410.
OMAiVTEFHGN.

Family and domain databases

Gene3Di3.30.1600.10. 2 hits.
3.40.50.1220. 3 hits.
HAMAPiMF_01968. Sirtuin_ClassU. 1 hit.
InterProiIPR029035. DHS-like_NAD/FAD-binding_dom.
IPR003000. Sirtuin.
IPR026591. Sirtuin_cat_small_dom.
IPR028628. Sirtuin_class_U.
IPR026590. Ssirtuin_cat_dom.
[Graphical view]
PANTHERiPTHR11085. PTHR11085. 1 hit.
PfamiPF02146. SIR2. 1 hit.
[Graphical view]
SUPFAMiSSF52467. SSF52467. 1 hit.
PROSITEiPS50305. SIRTUIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9WYW0-1 [UniParc]FASTAAdd to basket

« Hide

        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
Length:246
Mass (Da):27,538
Last modified:November 1, 1999 - v1
Checksum:i6BD2EF1B751C190D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000512 Genomic DNA. Translation: AAD35575.1.
PIRiA72370.
RefSeqiNP_228300.1. NC_000853.1.
WP_010865133.1. NC_000853.1.

Genome annotation databases

EnsemblBacteriaiAAD35575; AAD35575; TM_0490.
GeneIDi897531.
KEGGitma:TM0490.
PATRICi23935885. VBITheMar51294_0497.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000512 Genomic DNA. Translation: AAD35575.1.
PIRiA72370.
RefSeqiNP_228300.1. NC_000853.1.
WP_010865133.1. NC_000853.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1YC5X-ray1.40A1-246[»]
2H2DX-ray1.70A1-246[»]
2H2FX-ray2.20A1-246[»]
2H2GX-ray1.63A1-246[»]
2H2HX-ray2.20A1-246[»]
2H2IX-ray1.80A1-246[»]
2H4FX-ray2.00A1-246[»]
2H4HX-ray1.99A1-246[»]
2H4JX-ray2.10A1-246[»]
2H59X-ray1.90A/B1-246[»]
3D4BX-ray1.90A1-246[»]
3D81X-ray2.50A1-246[»]
3JR3X-ray1.50A1-246[»]
3PDHX-ray1.80A1-246[»]
4BUZX-ray1.90A1-246[»]
4BV2X-ray3.30A/B1-246[»]
ProteinModelPortaliQ9WYW0.
SMRiQ9WYW0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-29141N.
STRINGi243274.TM0490.

Chemistry databases

ChEMBLiCHEMBL3217404.

Protocols and materials databases

DNASUi897531.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAD35575; AAD35575; TM_0490.
GeneIDi897531.
KEGGitma:TM0490.
PATRICi23935885. VBITheMar51294_0497.

Phylogenomic databases

eggNOGiENOG4105NDF. Bacteria.
COG0846. LUCA.
InParanoidiQ9WYW0.
KOiK12410.
OMAiVTEFHGN.

Miscellaneous databases

EvolutionaryTraceiQ9WYW0.
PROiQ9WYW0.

Family and domain databases

Gene3Di3.30.1600.10. 2 hits.
3.40.50.1220. 3 hits.
HAMAPiMF_01968. Sirtuin_ClassU. 1 hit.
InterProiIPR029035. DHS-like_NAD/FAD-binding_dom.
IPR003000. Sirtuin.
IPR026591. Sirtuin_cat_small_dom.
IPR028628. Sirtuin_class_U.
IPR026590. Ssirtuin_cat_dom.
[Graphical view]
PANTHERiPTHR11085. PTHR11085. 1 hit.
PfamiPF02146. SIR2. 1 hit.
[Graphical view]
SUPFAMiSSF52467. SSF52467. 1 hit.
PROSITEiPS50305. SIRTUIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiNPD_THEMA
AccessioniPrimary (citable) accession number: Q9WYW0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 2003
Last sequence update: November 1, 1999
Last modified: November 2, 2016
This is version 109 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.