SIR4_MOUSE
ID SIR4_MOUSE Reviewed; 333 AA.
AC Q8R216; D3Z1D9;
DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=NAD-dependent protein lipoamidase sirtuin-4, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03161, ECO:0000303|PubMed:25525879};
DE EC=2.3.1.- {ECO:0000255|HAMAP-Rule:MF_03161, ECO:0000305|PubMed:25525879};
DE AltName: Full=NAD-dependent ADP-ribosyltransferase sirtuin-4 {ECO:0000255|HAMAP-Rule:MF_03161};
DE EC=2.4.2.- {ECO:0000255|HAMAP-Rule:MF_03161};
DE AltName: Full=NAD-dependent protein biotinylase sirtuin-4 {ECO:0000255|HAMAP-Rule:MF_03161};
DE EC=2.3.1.- {ECO:0000255|HAMAP-Rule:MF_03161};
DE AltName: Full=NAD-dependent protein deacetylase sirtuin-4 {ECO:0000255|HAMAP-Rule:MF_03161};
DE EC=2.3.1.286 {ECO:0000255|HAMAP-Rule:MF_03161};
DE AltName: Full=Regulatory protein SIR2 homolog 4 {ECO:0000255|HAMAP-Rule:MF_03161};
DE AltName: Full=SIR2-like protein 4 {ECO:0000255|HAMAP-Rule:MF_03161};
DE Flags: Precursor;
GN Name=Sirt4; Synonyms=Sir2l4;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, INTERACTION WITH GLUD1, AND
RP TISSUE SPECIFICITY.
RX PubMed=16959573; DOI=10.1016/j.cell.2006.06.057;
RA Haigis M.C., Mostoslavsky R., Haigis K.M., Fahie K., Christodoulou D.C.,
RA Murphy A.J., Valenzuela D.M., Yancopoulos G.D., Karow M., Blander G.,
RA Wolberger C., Prolla T.A., Weindruch R., Alt F.W., Guarente L.;
RT "SIRT4 inhibits glutamate dehydrogenase and opposes the effects of calorie
RT restriction in pancreatic beta cells.";
RL Cell 126:941-954(2006).
RN [5]
RP FUNCTION.
RX PubMed=19220062; DOI=10.1021/bi802093g;
RA Du J., Jiang H., Lin H.;
RT "Investigating the ADP-ribosyltransferase activity of sirtuins with NAD
RT analogues and 32P-NAD.";
RL Biochemistry 48:2878-2890(2009).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, and Kidney;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP FUNCTION.
RX PubMed=20685656; DOI=10.1074/jbc.m110.124164;
RA Nasrin N., Wu X., Fortier E., Feng Y., Bare' O.C., Chen S., Ren X., Wu Z.,
RA Streeper R.S., Bordone L.;
RT "SIRT4 regulates fatty acid oxidation and mitochondrial gene expression in
RT liver and muscle cells.";
RL J. Biol. Chem. 285:31995-32002(2010).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION.
RX PubMed=23562301; DOI=10.1016/j.ccr.2013.02.024;
RA Jeong S.M., Xiao C., Finley L.W., Lahusen T., Souza A.L., Pierce K.,
RA Li Y.H., Wang X., Laurent G., German N.J., Xu X., Li C., Wang R.H., Lee J.,
RA Csibi A., Cerione R., Blenis J., Clish C.B., Kimmelman A., Deng C.X.,
RA Haigis M.C.;
RT "SIRT4 has tumor-suppressive activity and regulates the cellular metabolic
RT response to DNA damage by inhibiting mitochondrial glutamine metabolism.";
RL Cancer Cell 23:450-463(2013).
RN [9]
RP FUNCTION, AND INDUCTION.
RX PubMed=23663782; DOI=10.1016/j.cell.2013.04.023;
RA Csibi A., Fendt S.M., Li C., Poulogiannis G., Choo A.Y., Chapski D.J.,
RA Jeong S.M., Dempsey J.M., Parkhitko A., Morrison T., Henske E.P.,
RA Haigis M.C., Cantley L.C., Stephanopoulos G., Yu J., Blenis J.;
RT "The mTORC1 pathway stimulates glutamine metabolism and cell proliferation
RT by repressing SIRT4.";
RL Cell 153:840-854(2013).
RN [10]
RP FUNCTION, AND INTERACTION WITH PCCA; MCCC1 AND PC.
RX PubMed=23438705; DOI=10.1016/j.mito.2013.02.002;
RA Wirth M., Karaca S., Wenzel D., Ho L., Tishkoff D., Lombard D.B.,
RA Verdin E., Urlaub H., Jedrusik-Bode M., Fischle W.;
RT "Mitochondrial SIRT4-type proteins in Caenorhabditis elegans and mammals
RT interact with pyruvate carboxylase and other acetylated biotin-dependent
RT carboxylases.";
RL Mitochondrion 13:705-720(2013).
RN [11]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION BY FASTING.
RX PubMed=24043310; DOI=10.1128/mcb.00087-13;
RA Laurent G., de Boer V.C., Finley L.W., Sweeney M., Lu H., Schug T.T.,
RA Cen Y., Jeong S.M., Li X., Sauve A.A., Haigis M.C.;
RT "SIRT4 represses peroxisome proliferator-activated receptor alpha activity
RT to suppress hepatic fat oxidation.";
RL Mol. Cell. Biol. 33:4552-4561(2013).
RN [12]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=23746352; DOI=10.1016/j.molcel.2013.05.012;
RA Laurent G., German N.J., Saha A.K., de Boer V.C., Davies M., Koves T.R.,
RA Dephoure N., Fischer F., Boanca G., Vaitheesvaran B., Lovitch S.B.,
RA Sharpe A.H., Kurland I.J., Steegborn C., Gygi S.P., Muoio D.M.,
RA Ruderman N.B., Haigis M.C.;
RT "SIRT4 coordinates the balance between lipid synthesis and catabolism by
RT repressing malonyl CoA decarboxylase.";
RL Mol. Cell 50:686-698(2013).
RN [13]
RP FUNCTION.
RX PubMed=25525879; DOI=10.1016/j.cell.2014.11.046;
RA Mathias R.A., Greco T.M., Oberstein A., Budayeva H.G., Chakrabarti R.,
RA Rowland E.A., Kang Y., Shenk T., Cristea I.M.;
RT "Sirtuin 4 is a lipoamidase regulating pyruvate dehydrogenase complex
RT activity.";
RL Cell 159:1615-1625(2014).
CC -!- FUNCTION: Acts as NAD-dependent protein lipoamidase, biotinylase,
CC deacetylase and ADP-ribosyl transferase (PubMed:19220062). Catalyzes
CC more efficiently removal of lipoyl- and biotinyl- than acetyl-lysine
CC modifications. Inhibits the pyruvate dehydrogenase complex (PDH)
CC activity via the enzymatic hydrolysis of the lipoamide cofactor from
CC the E2 component, DLAT, in a phosphorylation-independent manner
CC (PubMed:25525879). Catalyzes the transfer of ADP-ribosyl groups onto
CC target proteins, including mitochondrial GLUD1, inhibiting GLUD1 enzyme
CC activity. Acts as a negative regulator of mitochondrial glutamine
CC metabolism by mediating mono ADP-ribosylation of GLUD1: expressed in
CC response to DNA damage and negatively regulates anaplerosis by
CC inhibiting GLUD1, leading to block metabolism of glutamine into
CC tricarboxylic acid cycle and promoting cell cycle arrest
CC (PubMed:16959573). In response to mTORC1 signal, SIRT4 expression is
CC repressed, promoting anaplerosis and cell proliferation
CC (PubMed:23663782). Acts as a tumor suppressor (PubMed:23562301,
CC PubMed:23663782). Also acts as a NAD-dependent protein deacetylase:
CC mediates deacetylation of 'Lys-471' of MLYCD, inhibiting its activity,
CC thereby acting as a regulator of lipid homeostasis (PubMed:23746352).
CC Does not seem to deacetylate PC (PubMed:23438705). Controls fatty acid
CC oxidation by inhibiting PPARA transcriptional activation. Impairs
CC SIRT1-PPARA interaction probably through the regulation of NAD(+)
CC levels (PubMed:24043310, PubMed:20685656). Down-regulates insulin
CC secretion (By similarity). {ECO:0000255|HAMAP-Rule:MF_03161,
CC ECO:0000269|PubMed:19220062, ECO:0000269|PubMed:20685656,
CC ECO:0000269|PubMed:23438705, ECO:0000269|PubMed:23562301,
CC ECO:0000269|PubMed:23663782, ECO:0000269|PubMed:23746352,
CC ECO:0000269|PubMed:24043310, ECO:0000269|PubMed:25525879}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-N(6)-lipoyl-L-lysyl-[protein] + H2O + NAD(+) = 2''-O-
CC lipoyl-ADP-D-ribose + L-lysyl-[protein] + nicotinamide;
CC Xref=Rhea:RHEA:63640, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:10474,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:17154, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:83099, ChEBI:CHEBI:189572;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03161,
CC ECO:0000305|PubMed:25525879};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63641;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03161,
CC ECO:0000305|PubMed:25525879};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(6)-biotinyl-L-lysyl-[protein] + NAD(+) = 2''-O-
CC biotinyl-ADP-D-ribose + L-lysyl-[protein] + nicotinamide;
CC Xref=Rhea:RHEA:70479, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:10505,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:17154, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:83144, ChEBI:CHEBI:189573;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03161};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70480;
CC Evidence={ECO:0000255|HAMAP-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:0000255|HAMAP-Rule:MF_03161};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43637;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03161};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-cysteinyl-[protein] + NAD(+) = H(+) + nicotinamide + S-(ADP-
CC D-ribosyl)-L-cysteinyl-[protein]; Xref=Rhea:RHEA:56612, Rhea:RHEA-
CC COMP:10131, Rhea:RHEA-COMP:14624, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17154, ChEBI:CHEBI:29950, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:140607; Evidence={ECO:0000255|HAMAP-Rule:MF_03161};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03161};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_03161};
CC -!- SUBUNIT: Interacts with IDE and SLC25A5 (By similarity). Interacts with
CC GLUD1 (PubMed:16959573). Interacts with DLAT and PDHX (By similarity).
CC Interacts with MCCC1 (via the biotin carboxylation domain)
CC (PubMed:23438705). Interacts with PCCA and PC (PubMed:23438705).
CC {ECO:0000250|UniProtKB:Q9Y6E7, ECO:0000269|PubMed:16959573,
CC ECO:0000269|PubMed:23438705}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000255|HAMAP-
CC Rule:MF_03161, ECO:0000269|PubMed:16959573,
CC ECO:0000269|PubMed:23746352}.
CC -!- TISSUE SPECIFICITY: Detected in kidney, heart, brain, liver and
CC pancreatic islets (at protein level). {ECO:0000269|PubMed:16959573}.
CC -!- INDUCTION: Expression is directly activated by ATF4/CREB2. In response
CC to mTORC1 signal, expression is down-regulated due to degradation of
CC ATF4/CREB2 (PubMed:23663782). Induced following DNA damage
CC (PubMed:23562301). The expression is strongly inhibited by fasting
CC (PubMed:24043310). {ECO:0000269|PubMed:23562301,
CC ECO:0000269|PubMed:23663782, ECO:0000269|PubMed:24043310}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype. Decreased mitochondrial
CC protein ADP-ribosylation. Increased plasma insulin levels. Mice develop
CC lung tumors more frequently. Defects in lipid metabolism, leading to
CC increased protection against diet-induced obesity. Animals show higher
CC levels of NAD(+) in liver (PubMed:24043310). In the hepatic periportal
CC zone, decreased number of mitochondria with an increase in their length
CC (PubMed:24043310). {ECO:0000269|PubMed:16959573,
CC ECO:0000269|PubMed:23562301, ECO:0000269|PubMed:23746352,
CC ECO:0000269|PubMed:24043310}.
CC -!- MISCELLANEOUS: According to some authors, ADP-ribosyltransferase
CC activity of sirtuins may be an inefficient side reaction of the
CC deacetylase activity and may not be physiologically relevant.
CC {ECO:0000305|PubMed:19220062}.
CC -!- SIMILARITY: Belongs to the sirtuin family. Class II subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03161}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH22653.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC117735; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC159539; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466529; EDL19856.1; -; Genomic_DNA.
DR EMBL; CH466529; EDL19857.1; -; Genomic_DNA.
DR EMBL; BC022653; AAH22653.1; ALT_INIT; mRNA.
DR CCDS; CCDS51628.1; -.
DR RefSeq; NP_001161163.1; NM_001167691.1.
DR RefSeq; NP_598521.1; NM_133760.1.
DR RefSeq; XP_017176616.1; XM_017321127.1.
DR AlphaFoldDB; Q8R216; -.
DR SMR; Q8R216; -.
DR BioGRID; 217445; 3.
DR STRING; 10090.ENSMUSP00000107697; -.
DR PhosphoSitePlus; Q8R216; -.
DR EPD; Q8R216; -.
DR MaxQB; Q8R216; -.
DR PaxDb; Q8R216; -.
DR PeptideAtlas; Q8R216; -.
DR PRIDE; Q8R216; -.
DR ProteomicsDB; 261179; -.
DR Antibodypedia; 31464; 391 antibodies from 39 providers.
DR Ensembl; ENSMUST00000112066; ENSMUSP00000107697; ENSMUSG00000029524.
DR Ensembl; ENSMUST00000112067; ENSMUSP00000107698; ENSMUSG00000029524.
DR GeneID; 75387; -.
DR KEGG; mmu:75387; -.
DR UCSC; uc008zdy.1; mouse.
DR CTD; 23409; -.
DR MGI; MGI:1922637; Sirt4.
DR VEuPathDB; HostDB:ENSMUSG00000029524; -.
DR eggNOG; KOG2683; Eukaryota.
DR GeneTree; ENSGT00940000158891; -.
DR HOGENOM; CLU_023643_3_2_1; -.
DR InParanoid; Q8R216; -.
DR OMA; RRHYWAR; -.
DR OrthoDB; 1407693at2759; -.
DR PhylomeDB; Q8R216; -.
DR TreeFam; TF106182; -.
DR Reactome; R-MMU-2151201; Transcriptional activation of mitochondrial biogenesis.
DR BioGRID-ORCS; 75387; 1 hit in 76 CRISPR screens.
DR ChiTaRS; Sirt4; mouse.
DR PRO; PR:Q8R216; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q8R216; protein.
DR Bgee; ENSMUSG00000029524; Expressed in retinal neural layer and 140 other tissues.
DR Genevisible; Q8R216; MM.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:CACAO.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR GO; GO:0019213; F:deacetylase activity; IBA:GO_Central.
DR GO; GO:0061690; F:lipoamidase activity; IMP:UniProtKB.
DR GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IMP:UniProtKB.
DR GO; GO:0070403; F:NAD+ binding; IEA:UniProtKB-UniRule.
DR GO; GO:0106420; F:NAD-dependent protein biotinidase activity; ISS:UniProtKB.
DR GO; GO:0034979; F:NAD-dependent protein deacetylase activity; IDA:UniProtKB.
DR GO; GO:0106419; F:NAD-dependent protein lipoamidase activity; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:UniProtKB.
DR GO; GO:0071456; P:cellular response to hypoxia; IEA:Ensembl.
DR GO; GO:0006541; P:glutamine metabolic process; IMP:UniProtKB.
DR GO; GO:0010667; P:negative regulation of cardiac muscle cell apoptotic process; ISO:MGI.
DR GO; GO:0046322; P:negative regulation of fatty acid oxidation; IDA:UniProtKB.
DR GO; GO:0046676; P:negative regulation of insulin secretion; IMP:MGI.
DR GO; GO:1903217; P:negative regulation of protein processing involved in protein targeting to mitochondrion; ISO:MGI.
DR GO; GO:0034983; P:peptidyl-lysine deacetylation; IDA:UniProtKB.
DR GO; GO:0046889; P:positive regulation of lipid biosynthetic process; IDA:UniProtKB.
DR GO; GO:0006471; P:protein ADP-ribosylation; IMP:UniProtKB.
DR GO; GO:0006476; P:protein deacetylation; IBA:GO_Central.
DR GO; GO:0000820; P:regulation of glutamine family amino acid metabolic process; IMP:CACAO.
DR GO; GO:1904182; P:regulation of pyruvate dehydrogenase activity; IMP:UniProtKB.
DR GO; GO:0072350; P:tricarboxylic acid metabolic process; IMP:UniProtKB.
DR Gene3D; 3.30.1600.10; -; 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 Pfam; PF02146; SIR2; 1.
DR SUPFAM; SSF52467; SSF52467; 1.
DR PROSITE; PS50305; SIRTUIN; 1.
PE 1: Evidence at protein level;
KW DNA damage; Glycosyltransferase; Metal-binding; Mitochondrion; NAD;
KW Nucleotidyltransferase; Reference proteome; Transferase; Transit peptide;
KW Tumor suppressor; Zinc.
FT TRANSIT 1..25
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03161"
FT CHAIN 26..333
FT /note="NAD-dependent protein lipoamidase sirtuin-4,
FT mitochondrial"
FT /id="PRO_0000110265"
FT DOMAIN 42..317
FT /note="Deacetylase sirtuin-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03161"
FT ACT_SITE 158
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03161"
FT BINDING 59..79
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03161"
FT BINDING 140..143
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03161"
FT BINDING 166
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03161"
FT BINDING 169
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03161"
FT BINDING 217
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03161"
FT BINDING 220
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03161"
FT BINDING 257..259
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03161"
FT BINDING 283..285
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03161"
FT BINDING 301
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03161"
FT CONFLICT 67
FT /note="G -> S (in Ref. 2; AAH22653)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 333 AA; 37525 MW; AD9FBB1CC217D05E CRC64;
MSGLTFRPTK GRWITHLSRP RSCGPSGLFV PPSPPLDPEK IKELQRFISL SKKLLVMTGA
GISTESGIPD YRSEKVGLYA RTDRRPIQHI DFVRSAPVRQ RYWARNFVGW PQFSSHQPNP
AHWALSNWER LGKLHWLVTQ NVDALHSKAG SQRLTELHGC MHRVLCLNCG EQTARRVLQE
RFQALNPSWS AEAQGVAPDG DVFLTEEQVR SFQVPCCDRC GGPLKPDVVF FGDTVNPDKV
DFVHRRVKEA DSLLVVGSSL QVYSGYRFIL TAREQKLPIA ILNIGPTRSD DLACLKLDSR
CGELLPLIDP RRQHSDVQRL EMNFPLSSAA QDP
