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SIR5_PONAB
ID   SIR5_PONAB              Reviewed;         310 AA.
AC   Q5R6G3; Q5RCF2;
DT   24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=NAD-dependent protein deacylase sirtuin-5, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03160};
DE            EC=2.3.1.- {ECO:0000255|HAMAP-Rule:MF_03160};
DE   AltName: Full=Regulatory protein SIR2 homolog 5 {ECO:0000255|HAMAP-Rule:MF_03160};
DE   AltName: Full=SIR2-like protein 5 {ECO:0000255|HAMAP-Rule:MF_03160};
DE   Flags: Precursor;
GN   Name=SIRT5 {ECO:0000255|HAMAP-Rule:MF_03160};
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Heart;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) 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. Activates CPS1 and contributes to the
CC       regulation of blood ammonia levels during prolonged fasting: acts by
CC       mediating desuccinylation and deglutarylation of CPS1, thereby
CC       increasing CPS1 activity in response to elevated NAD levels during
CC       fasting. Activates SOD1 by mediating its desuccinylation, leading to
CC       reduced reactive oxygen species. Activates SHMT2 by mediating its
CC       desuccinylation. Modulates ketogenesis through the desuccinylation and
CC       activation of HMGCS2. Has weak NAD-dependent protein deacetylase
CC       activity; however this activity may not be physiologically relevant in
CC       vivo. Can deacetylate cytochrome c (CYCS) and a number of other
CC       proteins in vitro such as UOX. {ECO:0000255|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:0000255|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:0000255|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:0000255|HAMAP-Rule:MF_03160};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_03160};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_03160};
CC   -!- SUBUNIT: Monomer. Homodimer. Interacts with CPS1. Interacts with PCCA
CC       (By similarity). {ECO:0000250|UniProtKB:Q9NXA8, ECO:0000255|HAMAP-
CC       Rule:MF_03160}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03160}.
CC       Cytoplasm, cytosol {ECO:0000255|HAMAP-Rule:MF_03160}. Nucleus
CC       {ECO:0000255|HAMAP-Rule:MF_03160}. Note=Mainly mitochondrial. Also
CC       present extramitochondrially, with a fraction present in the cytosol
CC       and very small amounts also detected in the nucleus.
CC       {ECO:0000255|HAMAP-Rule:MF_03160}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q5R6G3-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q5R6G3-2; Sequence=VSP_021600;
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-102
CC       and Arg-105) that bind to malonylated and succinylated substrates and
CC       define the specificity. {ECO:0000255|HAMAP-Rule:MF_03160}.
CC   -!- SIMILARITY: Belongs to the sirtuin family. Class III subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_03160}.
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DR   EMBL; CR858318; CAH90555.1; -; mRNA.
DR   EMBL; CR860527; CAH92653.1; -; mRNA.
DR   RefSeq; NP_001126552.1; NM_001133080.1. [Q5R6G3-1]
DR   RefSeq; NP_001128779.1; NM_001135307.2. [Q5R6G3-2]
DR   RefSeq; XP_009239703.1; XM_009241428.1.
DR   AlphaFoldDB; Q5R6G3; -.
DR   SMR; Q5R6G3; -.
DR   STRING; 9601.ENSPPYP00000018164; -.
DR   Ensembl; ENSPPYT00000018888; ENSPPYP00000018164; ENSPPYG00000016242. [Q5R6G3-1]
DR   Ensembl; ENSPPYT00000061604; ENSPPYP00000041853; ENSPPYG00000016242. [Q5R6G3-2]
DR   GeneID; 100173543; -.
DR   GeneID; 100189679; -.
DR   KEGG; pon:100189679; -.
DR   CTD; 23408; -.
DR   eggNOG; KOG2684; Eukaryota.
DR   GeneTree; ENSGT00940000156080; -.
DR   HOGENOM; CLU_023643_3_1_1; -.
DR   InParanoid; Q5R6G3; -.
DR   OMA; SMQVYPA; -.
DR   OrthoDB; 1459156at2759; -.
DR   TreeFam; TF106183; -.
DR   Proteomes; UP000001595; Chromosome 6.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; ISS:UniProtKB.
DR   GO; GO:0005759; C:mitochondrial matrix; ISS:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0070403; F:NAD+ binding; ISS:UniProtKB.
DR   GO; GO:0034979; F:NAD-dependent protein deacetylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0061697; F:protein-glutaryllysine deglutarylase activity; IEA:Ensembl.
DR   GO; GO:0036054; F:protein-malonyllysine demalonylase activity; ISS:UniProtKB.
DR   GO; GO:0036055; F:protein-succinyllysine desuccinylase activity; ISS:UniProtKB.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR   GO; GO:2000378; P:negative regulation of reactive oxygen species metabolic process; IEA:Ensembl.
DR   GO; GO:0036047; P:peptidyl-lysine demalonylation; ISS:UniProtKB.
DR   GO; GO:0036049; P:peptidyl-lysine desuccinylation; ISS:UniProtKB.
DR   GO; GO:0006476; P:protein deacetylation; ISS:UniProtKB.
DR   GO; GO:0036046; P:protein demalonylation; ISS:UniProtKB.
DR   GO; GO:0036048; P:protein desuccinylation; ISS:UniProtKB.
DR   GO; GO:0010566; P:regulation of ketone biosynthetic process; ISS:UniProtKB.
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   2: Evidence at transcript level;
KW   Alternative splicing; Cytoplasm; Metal-binding; Mitochondrion; NAD;
KW   Nucleus; Reference proteome; Transferase; Transit peptide; Zinc.
FT   TRANSIT         1..36
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03160"
FT   CHAIN           37..310
FT                   /note="NAD-dependent protein deacylase sirtuin-5,
FT                   mitochondrial"
FT                   /id="PRO_0000110268"
FT   DOMAIN          41..309
FT                   /note="Deacetylase sirtuin-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03160"
FT   ACT_SITE        158
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03160"
FT   BINDING         58..77
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03160"
FT   BINDING         102
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03160"
FT   BINDING         105
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03160"
FT   BINDING         140..143
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03160"
FT   BINDING         166
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03160"
FT   BINDING         169
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03160"
FT   BINDING         207
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03160"
FT   BINDING         212
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03160"
FT   BINDING         249..251
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03160"
FT   BINDING         275..277
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03160"
FT   BINDING         293
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03160"
FT   VAR_SEQ         189..206
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.1"
FT                   /id="VSP_021600"
SQ   SEQUENCE   310 AA;  33932 MW;  CE42BC34AF45FCBE CRC64;
     MRPLQIVPSR LISQLYCGLK PPASTRNQIC LKMARPSSSM ADFRKLFAKA KHIVIMSGAG
     VSAESGVPTF RGAGGYWRKW QAQDLATPLA FAHNPSRVWE FYHYRREVMG SKEPNAGHRA
     IAECETRLGK QGRRVVVITQ NIDELHRKAG TKNLLEIHGS LFKTRCTSCG VVAENYKSPI
     CPALSGKGAP EPGTQDASIP IEKLPRCEEA GCGGLLRPHV VWFGENLDPA ILEEVDRELA
     HCDLCLVVGT SSVVYPAAMF APQVAARGVP VAEFNTETTP ATNRFRFHFQ GPCGTTLPEA
     LARHENETVS
 
 
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