ID A0A2P1NLT3_9BURK Unreviewed; 259 AA.
AC A0A2P1NLT3;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=NAD-dependent protein deacylase {ECO:0000256|HAMAP-Rule:MF_01121};
DE EC=2.3.1.286 {ECO:0000256|HAMAP-Rule:MF_01121};
DE AltName: Full=Regulatory protein SIR2 homolog {ECO:0000256|HAMAP-Rule:MF_01121};
GN Name=cobB {ECO:0000256|HAMAP-Rule:MF_01121};
GN ORFNames=C7H73_10355 {ECO:0000313|EMBL:AVP58024.1};
OS Pulveribacter suum.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Pulveribacter.
OX NCBI_TaxID=2116657 {ECO:0000313|EMBL:AVP58024.1, ECO:0000313|Proteomes:UP000241829};
RN [1] {ECO:0000313|Proteomes:UP000241829}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC2-7 {ECO:0000313|Proteomes:UP000241829};
RA Kim S.-J., Heo J., Ahn J.-H., Kwon S.-W.;
RT "Genome sequencing of Melaminivora sp. strain SC2-7.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: NAD-dependent lysine deacetylase and desuccinylase that
CC specifically removes acetyl and succinyl groups on target proteins.
CC Modulates the activities of several proteins which are inactive in
CC their acylated form. {ECO:0000256|HAMAP-Rule:MF_01121}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(6)-acetyl-L-lysyl-[protein] + NAD(+) = 2''-O-acetyl-
CC ADP-D-ribose + L-lysyl-[protein] + nicotinamide;
CC Xref=Rhea:RHEA:43636, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:10731,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:17154, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:61930, ChEBI:CHEBI:83767;
CC EC=2.3.1.286; Evidence={ECO:0000256|HAMAP-Rule:MF_01121};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(6)-succinyl-L-lysyl-[protein] + NAD(+) = 2''-O-
CC succinyl-ADP-D-ribose + L-lysyl-[protein] + nicotinamide;
CC Xref=Rhea:RHEA:47668, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:11877,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:17154, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:87830, ChEBI:CHEBI:87832;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01121};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01121}.
CC -!- DOMAIN: 2 residues (Tyr-70 and Arg-73) present in a large hydrophobic
CC pocket are probably involved in substrate specificity. They are
CC important for desuccinylation activity, but dispensable for
CC deacetylation activity. {ECO:0000256|HAMAP-Rule:MF_01121}.
CC -!- SIMILARITY: Belongs to the sirtuin family. Class III subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_01121}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01121,
CC ECO:0000256|PROSITE-ProRule:PRU00236}.
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DR EMBL; CP027792; AVP58024.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P1NLT3; -.
DR KEGG; melm:C7H73_10355; -.
DR OrthoDB; 9800582at2; -.
DR Proteomes; UP000241829; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0070403; F:NAD+ binding; IEA:UniProtKB-UniRule.
DR GO; GO:0034979; F:NAD-dependent protein deacetylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0036054; F:protein-malonyllysine demalonylase activity; IEA:InterPro.
DR GO; GO:0036055; F:protein-succinyllysine desuccinylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.30.1600.10; SIR2/SIRT2 'Small Domain; 1.
DR Gene3D; 3.40.50.1220; TPP-binding domain; 1.
DR HAMAP; MF_01121; Sirtuin_ClassIII; 1.
DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR InterPro; IPR003000; Sirtuin.
DR InterPro; IPR026591; Sirtuin_cat_small_dom_sf.
DR InterPro; IPR027546; Sirtuin_class_III.
DR InterPro; IPR026590; Ssirtuin_cat_dom.
DR PANTHER; PTHR11085:SF12; NAD-DEPENDENT PROTEIN DEACYLASE SIRTUIN-5, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11085; NAD-DEPENDENT PROTEIN DEACYLASE SIRTUIN-5, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF02146; SIR2; 1.
DR SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1.
DR PROSITE; PS50305; SIRTUIN; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01121};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_01121};
KW Reference proteome {ECO:0000313|Proteomes:UP000241829};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..258
FT /note="Deacetylase sirtuin-type"
FT /evidence="ECO:0000259|PROSITE:PS50305"
FT ACT_SITE 123
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01121"
FT BINDING 70
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01121"
FT BINDING 73
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01121"
FT BINDING 105..108
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01121"
FT BINDING 218..220
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01121"
FT BINDING 236
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01121"
SQ SEQUENCE 259 AA; 26990 MW; 23483050F7087E17 CRC64;
MNSPQEQQAV QAWIAQATRI AVLTGAGMSA ESGVPTFRDA TSGHWAQFNP QDMASERGFR
AAPARVWDWY AHRRAGVAAV QPNAGHRALA AFARRHPGRL TLITQNVDGL HQRAGSAGVL
CLHGDLMLDR WLDAPRACCQ LHAAAPGSPP RCAACGNLVR PGVVWFGESL PAEVLDAAQQ
AAQAAELMLV VGTAGAVYPA AGLAHLARQA GARVVVLNPA ASELDSAAHA VLRGTAAQLL
PQLLAPEGQG AATHLKETA
//
