ID G8XB34_FLACA Unreviewed; 227 AA.
AC G8XB34;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 63.
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 OrderedLocusNames=FCOL_05885 {ECO:0000313|EMBL:AEW86002.1};
OS Flavobacterium columnare (strain ATCC 49512 / CIP 103533 / TG 44/87).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1041826 {ECO:0000313|EMBL:AEW86002.1, ECO:0000313|Proteomes:UP000005638};
RN [1] {ECO:0000313|Proteomes:UP000005638}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49512 / CIP 103533 / TG 44/87
RC {ECO:0000313|Proteomes:UP000005638};
RA Tekedar H.C., Karsi A., Gillaspy A.F., Dyer D., Benton N.R., Zaitshik J.,
RA Vamenta S., Banes M.M., Gulsoy N., Aboko-Cole M., Waldbieser G.C.,
RA Lawrence M.L.;
RT "Complete genome sequence of Flavobacterium columnare ATCC 49512.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AEW86002.1, ECO:0000313|Proteomes:UP000005638}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49512 / CIP 103533 / TG 44/87
RC {ECO:0000313|Proteomes:UP000005638};
RX PubMed=22535941; DOI=10.1128/JB.00281-12;
RA Tekedar H.C., Karsi A., Gillaspy A.F., Dyer D.W., Benton N.R., Zaitshik J.,
RA Vamenta S., Banes M.M., Gulsoy N., Aboko-Cole M., Waldbieser G.C.,
RA Lawrence M.L.;
RT "Genome Sequence of the Fish Pathogen Flavobacterium columnare ATCC
RT 49512.";
RL J. Bacteriol. 194:2763-2764(2012).
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-54 and Arg-57) 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; CP003222; AEW86002.1; -; Genomic_DNA.
DR RefSeq; WP_014165280.1; NC_016510.2.
DR AlphaFoldDB; G8XB34; -.
DR STRING; 1041826.FCOL_05885; -.
DR KEGG; fco:FCOL_05885; -.
DR eggNOG; COG0846; Bacteria.
DR HOGENOM; CLU_023643_3_1_10; -.
DR Proteomes; UP000005638; 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 CDD; cd01412; SIRT5_Af1_CobB; 1.
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:UP000005638};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..227
FT /note="Deacetylase sirtuin-type"
FT /evidence="ECO:0000259|PROSITE:PS50305"
FT ACT_SITE 105
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01121"
FT BINDING 10..29
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01121"
FT BINDING 54
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01121"
FT BINDING 57
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01121"
FT BINDING 87..90
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01121"
FT BINDING 170..172
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01121"
FT BINDING 215
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01121"
SQ SEQUENCE 227 AA; 25338 MW; D95BB3871DFF4D49 CRC64;
MKKKLVILTG AGMSAESGIS TFRDSNGLWE NHDIKEVASP EGWRKNPALV LDFYNKRRAQ
LKEVTPNRGH EIIAELEQKF DVQIITQNVD NLHERAGSSK ILHLHGELTK VRSTENSDYI
INWSEDLHIG DMAPDGSQLR PHIVWFGEAV PGINQAIPML EKADILIIIG TSLQVYPAAG
LMHYTRTDTP IYYIDPKPAS VNNLPNPIEI IPLSASEGMK NLVERGI
//
