ID C5M470_CANTT Unreviewed; 351 AA.
AC C5M470;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=NAD-dependent protein deacetylase {ECO:0000256|PIRNR:PIRNR037938};
DE EC=2.3.1.286 {ECO:0000256|PIRNR:PIRNR037938};
GN ORFNames=CTRG_00859 {ECO:0000313|EMBL:EER36120.1};
OS Candida tropicalis (strain ATCC MYA-3404 / T1) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=294747 {ECO:0000313|EMBL:EER36120.1, ECO:0000313|Proteomes:UP000002037};
RN [1] {ECO:0000313|EMBL:EER36120.1, ECO:0000313|Proteomes:UP000002037}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-3404 / T1 {ECO:0000313|Proteomes:UP000002037};
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
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|PIRNR:PIRNR037938};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR037938-3};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037938-3};
CC -!- SIMILARITY: Belongs to the sirtuin family. Class I subfamily.
CC {ECO:0000256|ARBA:ARBA00006924, ECO:0000256|PIRNR:PIRNR037938}.
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DR EMBL; GG692395; EER36120.1; -; Genomic_DNA.
DR RefSeq; XP_002546078.1; XM_002546032.1.
DR AlphaFoldDB; C5M470; -.
DR STRING; 294747.C5M470; -.
DR EnsemblFungi; CTRG_00859-t43_1; CTRG_00859-t43_1-p1; CTRG_00859.
DR GeneID; 8302158; -.
DR KEGG; ctp:CTRG_00859; -.
DR VEuPathDB; FungiDB:CTRG_00859; -.
DR eggNOG; KOG2682; Eukaryota.
DR HOGENOM; CLU_023643_7_2_1; -.
DR OrthoDB; 10545at2759; -.
DR Proteomes; UP000002037; Unassembled WGS sequence.
DR GO; GO:0099115; C:chromosome, subtelomeric region; IEA:EnsemblFungi.
DR GO; GO:0005737; C:cytoplasm; IEA:EnsemblFungi.
DR GO; GO:0031934; C:mating-type region heterochromatin; IEA:EnsemblFungi.
DR GO; GO:0005721; C:pericentric heterochromatin; IEA:EnsemblFungi.
DR GO; GO:0033553; C:rDNA heterochromatin; IEA:EnsemblFungi.
DR GO; GO:0070403; F:NAD+ binding; IEA:UniProtKB-UniRule.
DR GO; GO:0017136; F:NAD-dependent histone deacetylase activity; IEA:InterPro.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0031508; P:pericentric heterochromatin formation; IEA:EnsemblFungi.
DR GO; GO:0000183; P:rDNA heterochromatin formation; IEA:EnsemblFungi.
DR Gene3D; 3.30.1600.10; SIR2/SIRT2 'Small Domain; 1.
DR Gene3D; 3.40.50.1220; TPP-binding domain; 1.
DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR InterPro; IPR003000; Sirtuin.
DR InterPro; IPR026591; Sirtuin_cat_small_dom_sf.
DR InterPro; IPR017328; Sirtuin_class_I.
DR InterPro; IPR026590; Ssirtuin_cat_dom.
DR PANTHER; PTHR11085:SF10; NAD-DEPENDENT PROTEIN DEACETYLASE SIRTUIN-2; 1.
DR PANTHER; PTHR11085; NAD-DEPENDENT PROTEIN DEACYLASE SIRTUIN-5, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF02146; SIR2; 1.
DR PIRSF; PIRSF037938; SIR2_euk; 1.
DR SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1.
DR PROSITE; PS50305; SIRTUIN; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|PIRNR:PIRNR037938,
KW ECO:0000256|PIRSR:PIRSR037938-3};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|PIRNR:PIRNR037938};
KW Reference proteome {ECO:0000313|Proteomes:UP000002037};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR037938};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRNR:PIRNR037938}.
FT DOMAIN 1..265
FT /note="Deacetylase sirtuin-type"
FT /evidence="ECO:0000259|PROSITE:PS50305"
FT REGION 299..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 129
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR037938-1,
FT ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 27..31
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR037938-2"
FT BINDING 37..39
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR037938-2"
FT BINDING 109..112
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR037938-2"
FT BINDING 137
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037938-3,
FT ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 140
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037938-3,
FT ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 164
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037938-3,
FT ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 167
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037938-3,
FT ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 205..206
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR037938-2"
FT BINDING 229..231
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR037938-2"
FT BINDING 251
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR037938-2"
SQ SEQUENCE 351 AA; 40242 MW; D6E1DFA5AC6DB98B CRC64;
MSDIETTLQP IVDAIKKGKK VTFFNGAGIS TAAGIPDFRS PDTGLYANLA KLNLPFAEAV
FDIEYFKENP KPFYTLAEEL YPGNFAPTKF HYFIKLLQDE HSLRRVYTQN IDTLERLAGV
DDKYIVEAHG SFAKNHCVEC HKEMDTETLK KQMKDKSKDG IPTCDECHGY VKPDIVFFGE
GLPTKFFEKW EHDSRRVEIA IVAGTSLTVQ PFAFLPAEVS KKSIRLLVNN EKVGDFEHHP
RKTDVLALYD CDLVAEKLCA LLGWEEKLNE LYETERVKYG KPEIKENVLH EIEDKLKEEA
HLVEEGRSST KDNEEEEEDT GKKEEERDTK ETKKEEKEEA ELEKLIDKLS L
//
