ID   A0A397GUR8_9EURO        Unreviewed;       319 AA.
AC   A0A397GUR8;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   13-NOV-2019, entry version 4.
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.,
RA   Moreira S., 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
RT   the 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
CC       glutaryl groups on target proteins. Has weak NAD-dependent protein
CC       deacetylase activity; however this activity may not be
CC       physiologically relevant in vivo. {ECO:0000256|HAMAP-
CC       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-
CC         malonyl-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; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_03160};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_03160};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|HAMAP-
CC       Rule:MF_03160}.
CC   -!- DOMAIN: In contrast to class I sirtuins, class III sirtuins have
CC       only weak deacetylase activity. Difference in substrate
CC       specificity is probably due to a larger hydrophobic pocket with 2
CC       residues (Tyr-73 and Arg-76) that bind to malonylated and
CC       succinylated substrates and define the specificity.
CC       {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
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_03160}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {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: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   Complete proteome {ECO:0000313|Proteomes:UP000215394};
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       Deacetylase sirtuin-type.
FT                                {ECO:0000259|PROSITE:PS50305}.
FT   NP_BIND      29     48       NAD. {ECO:0000256|HAMAP-Rule:MF_03160}.
FT   NP_BIND     107    110       NAD. {ECO:0000256|HAMAP-Rule:MF_03160}.
FT   NP_BIND     256    258       NAD. {ECO:0000256|HAMAP-Rule:MF_03160}.
FT   NP_BIND     282    284       NAD. {ECO:0000256|HAMAP-Rule:MF_03160}.
FT   ACT_SITE    127    127       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_03160}.
FT   METAL       135    135       Zinc. {ECO:0000256|HAMAP-Rule:MF_03160}.
FT   METAL       213    213       Zinc. {ECO:0000256|HAMAP-Rule:MF_03160}.
FT   BINDING      73     73       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_03160}.
FT   BINDING      76     76       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_03160}.
FT   BINDING     304    304       NAD; via amide nitrogen.
FT                                {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
//