ID A0A3B6MNA5_WHEAT Unreviewed; 396 AA.
AC A0A3B6MNA5;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=NAD-dependent protein deacylase {ECO:0000256|HAMAP-Rule:MF_03161};
DE EC=2.3.1.- {ECO:0000256|HAMAP-Rule:MF_03161};
DE AltName: Full=Regulatory protein SIR2 homolog {ECO:0000256|HAMAP-Rule:MF_03161};
GN ORFNames=CFC21_076701 {ECO:0000313|EMBL:KAF7071371.1};
OS Triticum aestivum (Wheat).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=4565 {ECO:0000313|EnsemblPlants:TraesCS5D02G124700.1};
RN [1] {ECO:0000313|EMBL:KAF7071371.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF7071371.1};
RX PubMed=29069494;
RA Zimin A.V., Puiu D., Hall R., Kingan S., Clavijo B.J., Salzberg S.L.;
RT "The first near-complete assembly of the hexaploid bread wheat genome,
RT Triticum aestivum.";
RL Gigascience 6:1-7(2017).
RN [2] {ECO:0000313|EnsemblPlants:TraesCS5D02G124700.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Chinese Spring
RC {ECO:0000313|EnsemblPlants:TraesCS5D02G124700.1};
RX PubMed=30115783; DOI=10.1126/science.aar7191;
RG International wheat genome sequencing consortium (IWGSC);
RT "Shifting the limits in wheat research and breeding using a fully annotated
RT reference genome.";
RL Science 361:EAAR7191-EAAR7191(2018).
RN [3] {ECO:0000313|EnsemblPlants:TraesCS5D02G124700.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (OCT-2018) to UniProtKB.
RN [4] {ECO:0000313|EMBL:KAF7071371.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF7071371.1};
RA Zimin A.V., Puiu D., Shumante A., Alonge M., Salzberg S.L.;
RT "The second near-complete assembly of the hexaploid bread wheat (Triticum
RT aestivum) genome.";
RL Submitted (MAR-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: NAD-dependent protein deacylase. Catalyzes the NAD-dependent
CC hydrolysis of acyl groups from lysine residues. {ECO:0000256|HAMAP-
CC Rule:MF_03161}.
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_03161};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_03161};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_03161};
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000256|HAMAP-
CC Rule:MF_03161}.
CC -!- SIMILARITY: Belongs to the sirtuin family. Class II subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_03161}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_03161}.
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DR EMBL; CM022225; KAF7071371.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3B6MNA5; -.
DR SMR; A0A3B6MNA5; -.
DR STRING; 4565.A0A3B6MNA5; -.
DR EnsemblPlants; TraesCS5D02G124700.1; TraesCS5D02G124700.1; TraesCS5D02G124700.
DR Gramene; TraesCAD_scaffold_041501_01G000100.1; TraesCAD_scaffold_041501_01G000100.1; TraesCAD_scaffold_041501_01G000100.
DR Gramene; TraesCLE_scaffold_016819_01G000100.1; TraesCLE_scaffold_016819_01G000100.1; TraesCLE_scaffold_016819_01G000100.
DR Gramene; TraesCS5D02G124700.1; TraesCS5D02G124700.1; TraesCS5D02G124700.
DR Gramene; TraesCS5D03G0316100.1; TraesCS5D03G0316100.1.CDS; TraesCS5D03G0316100.
DR Gramene; TraesKAR5D01G0138010.1; cds.TraesKAR5D01G0138010.1; TraesKAR5D01G0138010.
DR Gramene; TraesPAR_scaffold_038402_01G000100.1; TraesPAR_scaffold_038402_01G000100.1; TraesPAR_scaffold_038402_01G000100.
DR Gramene; TraesROB_scaffold_001323_01G000100.1; TraesROB_scaffold_001323_01G000100.1; TraesROB_scaffold_001323_01G000100.
DR Gramene; TraesWEE_scaffold_011797_01G000100.1; TraesWEE_scaffold_011797_01G000100.1; TraesWEE_scaffold_011797_01G000100.
DR Proteomes; UP000019116; Chromosome 5D.
DR Proteomes; UP000815260; Chromosome 5D.
DR GO; GO:0005759; C:mitochondrial matrix; IBA:GO_Central.
DR GO; GO:0004407; F:histone deacetylase activity; IBA:GO_Central.
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:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR CDD; cd01409; SIRT4; 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_01967; Sirtuin_ClassII; 1.
DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR InterPro; IPR003000; Sirtuin.
DR InterPro; IPR026591; Sirtuin_cat_small_dom_sf.
DR InterPro; IPR026587; Sirtuin_class_II.
DR InterPro; IPR026590; Ssirtuin_cat_dom.
DR PANTHER; PTHR11085; NAD-DEPENDENT PROTEIN DEACYLASE SIRTUIN-5, MITOCHONDRIAL-RELATED; 1.
DR PANTHER; PTHR11085:SF2; NAD-DEPENDENT PROTEIN LIPOAMIDASE SIRTUIN-4, MITOCHONDRIAL; 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 Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_03161}; Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03161};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_03161};
KW Reference proteome {ECO:0000313|Proteomes:UP000019116};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_03161};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_03161}.
FT DOMAIN 97..396
FT /note="Deacetylase sirtuin-type"
FT /evidence="ECO:0000259|PROSITE:PS50305"
FT ACT_SITE 218
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03161,
FT ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 201..204
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03161"
FT BINDING 226
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03161,
FT ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 229
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03161,
FT ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 293
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03161,
FT ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 296
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03161,
FT ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 359..361
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03161"
FT BINDING 377
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03161"
SQ SEQUENCE 396 AA; 43784 MW; 429FA04E358DCC14 CRC64;
MAAVLAAHGS RVSASIIAGF GSALRGIPKG FCPRFYNIQA SIYNGLVHRR KIPLPLRCSF
RSIQARNNHS SSAVVPKDYC ETYIQFLRDK RIVPDSDPPS SKDVDLLYRF IDKSNKLMVL
TGAGMSTESG IPDYRSPNGA YSSGFKPLTH QEFVRSIRAR RRYWARSYAG WRRFRRAQPN
TAHYALASLE RIGRVHTMVT QNVDRLHHRA GSKPVELHGS VYEVICLDCG TSISRESFQE
QVKDLNPKWA LAIDSLEEGQ PGSSRSFGMQ QRPDGDIEID EKFWEQDFDI PSCSQCGGVL
KPDVVMFGDN VPRERADSAK EAARNCDALL VVGSAVMTMS AFRLARLAHE ANAPIAAINI
GGTRADSIIS LKINARCGEI LPRVLQMGSL AVPSIS
//
