ID   A0A397GUR8_9EURO        Unreviewed;       319 AA.
AC   A0A397GUR8;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   11-DEC-2019, entry version 5.
DE   RecName: Full=NAD-dependent protein deacylase {ECO:0000256|HAMAP-Rule:MF_03160};
DE            EC=2.3.1.- {ECO:0000256|HAMAP-Rule:MF_03160};
DE   AltName: Full=Regulatory protein SIR2 homolog 5 {ECO:0000256|HAMAP-Rule:MF_03160};
GN   ORFNames=CDV55_103214 {ECO:0000313|EMBL:RHZ53408.1};
OS   Aspergillus turcosus.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1245748 {ECO:0000313|EMBL:RHZ53408.1, ECO:0000313|Proteomes:UP000215394};
RN   [1] {ECO:0000313|EMBL:RHZ53408.1, ECO:0000313|Proteomes:UP000215394}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HMR AF 23 {ECO:0000313|EMBL:RHZ53408.1};
RA   Parent-Michaud M., Dufresne P.J., Fournier E., Martineau C., Moreira S.,
RA   Perkins V., De Repentigny L., Dufresne S.F.;
RT   "Draft genome sequences of two Aspergillus turcosus clinical strains
RT   isolated from bronchoalveolar lavage fluid: one azole-susceptible and the
RT   other azole-resistant.";
RL   Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: NAD-dependent lysine demalonylase, desuccinylase and
CC       deglutarylase that specifically removes malonyl, succinyl and glutaryl
CC       groups on target proteins. Has weak NAD-dependent protein deacetylase
CC       activity; however this activity may not be physiologically relevant in
CC       vivo. {ECO:0000256|HAMAP-Rule:MF_03160}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N(6)-glutaryl-L-lysyl-[protein] + NAD(+) = 2''-O-
CC         glutaryl-ADP-D-ribose + L-lysyl-[protein] + nicotinamide;
CC         Xref=Rhea:RHEA:47664, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:11875,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:17154, ChEBI:CHEBI:29969,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:87828, ChEBI:CHEBI:87829;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_03160};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N(6)-malonyl-L-lysyl-[protein] + NAD(+) = 2''-O-malonyl-
CC         ADP-D-ribose + L-lysyl-[protein] + nicotinamide;
CC         Xref=Rhea:RHEA:47672, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:11878,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:17154, ChEBI:CHEBI:29969,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:87831, ChEBI:CHEBI:87833;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_03160};
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_03160};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_03160};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_03160};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03160}.
CC   -!- DOMAIN: In contrast to class I sirtuins, class III sirtuins have only
CC       weak deacetylase activity. Difference in substrate specificity is
CC       probably due to a larger hydrophobic pocket with 2 residues (Tyr-73 and
CC       Arg-76) that bind to malonylated and succinylated substrates and define
CC       the specificity. {ECO:0000256|HAMAP-Rule:MF_03160}.
CC   -!- SIMILARITY: Belongs to the sirtuin family. Class III subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_03160}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_03160}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RHZ53408.1}.
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DR   EMBL; NKHV02000187; RHZ53408.1; -; Genomic_DNA.
DR   Proteomes; UP000215394; Unassembled WGS sequence.
DR   GO; GO:0005739; C:mitochondrion; 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:UniProtKB-UniRule.
DR   GO; GO:0036055; F:protein-succinyllysine desuccinylase 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; cd01412; SIRT5_Af1_CobB; 1.
DR   Gene3D; 3.30.1600.10; -; 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   Pfam; PF02146; SIR2; 1.
DR   SUPFAM; SSF52467; SSF52467; 1.
DR   PROSITE; PS50305; SIRTUIN; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_03160};
KW   Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03160};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_03160};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_03160};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_03160}.
FT   DOMAIN          12..319
FT                   /note="Deacetylase sirtuin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50305"
FT   NP_BIND         29..48
FT                   /note="NAD"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03160"
FT   NP_BIND         107..110
FT                   /note="NAD"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03160"
FT   NP_BIND         256..258
FT                   /note="NAD"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03160"
FT   NP_BIND         282..284
FT                   /note="NAD"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03160"
FT   ACT_SITE        127
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03160"
FT   METAL           135
FT                   /note="Zinc"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03160"
FT   METAL           213
FT                   /note="Zinc"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03160"
FT   BINDING         73
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03160"
FT   BINDING         76
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03160"
FT   BINDING         304
FT                   /note="NAD; via amide nitrogen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03160"
SQ   SEQUENCE   319 AA;  34776 MW;  49DC44E60E2F748E CRC64;
     MASSAIPAAD LRSFTEYLKG CKRILALLGA GISASSGLPT FRGAGGLWRS HDATDLATPE
     AFEANPDLVW QFYSYRRHMA LKAKPNRAHY ALAELARRNK DFITLTQNVD GLSQRANHPS
     EQLHLLHGSL FTVKCTSFYC NYLREDDFTD PIVPALAIPK GVPDLSPSAE DKTGEEASKA
     LSNALRMEEE KELDISDENV PLPALSLDVL PHCPECKEGL LRPGVVWFGE SLPLHTLEMV
     DNWLHSGPVD LILVIGTSAR VYPAAGYVDK ARARGARVAV VNMDRNDVGN SGLKKGDWFF
     QGDAGVIVPE ILKGVIGDI
//