ID DECR_HUMAN Reviewed; 335 AA. AC Q16698; B7Z6B8; Q2M304; Q93085; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 27-MAR-2024, entry version 201. DE RecName: Full=2,4-dienoyl-CoA reductase [(3E)-enoyl-CoA-producing], mitochondrial; DE EC=1.3.1.124 {ECO:0000269|PubMed:15531764}; DE AltName: Full=2,4-dienoyl-CoA reductase [NADPH]; DE Short=4-enoyl-CoA reductase [NADPH]; DE AltName: Full=Short chain dehydrogenase/reductase family 18C member 1; DE Flags: Precursor; GN Name=DECR1; Synonyms=DECR, SDR18C1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND SUBCELLULAR RP LOCATION. RC TISSUE=Liver; RX PubMed=7818482; DOI=10.1042/bj3040787; RA Koivuranta K.T., Hakkola E.H., Hiltunen J.K.; RT "Isolation and characterization of cDNA for human 120 kDa mitochondrial RT 2,4-dienoyl-coenzyme A reductase."; RL Biochem. J. 304:787-792(1994). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Liver; RA Ding J.H., Yang B.Z., Roe C.R.; RL Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=9403065; DOI=10.1006/geno.1997.5004; RA Helander H.M., Koivuranta K.T., Horelli-Kuitunen N., Palvimo J.J., RA Palotie A., Hiltunen J.K.; RT "Molecular cloning and characterization of the human mitochondrial 2,4- RT dienoyl-CoA reductase gene (DECR)."; RL Genomics 46:112-119(1997). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Pericardium; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16421571; DOI=10.1038/nature04406; RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., RA Platzer M., Shimizu N., Lander E.S.; RT "DNA sequence and analysis of human chromosome 8."; RL Nature 439:331-335(2006). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain; 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 [7] RP IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Lymphoblast; RX PubMed=14654843; DOI=10.1038/nature02166; RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.; RT "Proteomic characterization of the human centrosome by protein correlation RT profiling."; RL Nature 426:570-574(2003). RN [8] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-230, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [9] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [10] RP INVOLVEMENT IN DECRD. RX PubMed=24847004; DOI=10.1093/hmg/ddu218; RA Houten S.M., Denis S., Te Brinke H., Jongejan A., van Kampen A.H., RA Bradley E.J., Baas F., Hennekam R.C., Millington D.S., Young S.P., RA Frazier D.M., Gucsavas-Calikoglu M., Wanders R.J.; RT "Mitochondrial NADP(H) deficiency due to a mutation in NADK2 causes RT dienoyl-CoA reductase deficiency with hyperlysinemia."; RL Hum. Mol. Genet. 23:5009-5016(2014). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-69, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [13] RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 35-335 IN COMPLEX WITH NADP AND RP SUBSTRATE, CATALYTIC ACTIVITY, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, RP MUTAGENESIS OF ASN-148; TYR-199; SER-210 AND LYS-214, AND FUNCTION. RX PubMed=15531764; DOI=10.1074/jbc.m411069200; RA Alphey M.S., Yu W., Byres E., Li D., Hunter W.N.; RT "Structure and reactivity of human mitochondrial 2,4-dienoyl-CoA reductase: RT enzyme-ligand interactions in a distinctive short-chain reductase active RT site."; RL J. Biol. Chem. 280:3068-3077(2005). CC -!- FUNCTION: Auxiliary enzyme of beta-oxidation. It participates in the CC metabolism of unsaturated fatty enoyl-CoA esters having double bonds in CC both even- and odd-numbered positions in mitochondria. Catalyzes the CC NADP-dependent reduction of 2,4-dienoyl-CoA to yield trans-3-enoyl-CoA. CC {ECO:0000269|PubMed:15531764}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a (2E,4E)-dienoyl-CoA + H(+) + NADPH = a 4,5-saturated-(3E)- CC enoyl-CoA + NADP(+); Xref=Rhea:RHEA:45912, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:85101, CC ChEBI:CHEBI:85493; EC=1.3.1.124; CC Evidence={ECO:0000269|PubMed:15531764}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a (2E,4Z)-dienoyl-CoA + H(+) + NADPH = a 4,5-saturated-(3E)- CC enoyl-CoA + NADP(+); Xref=Rhea:RHEA:61892, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:85099, CC ChEBI:CHEBI:85493; EC=1.3.1.124; CC Evidence={ECO:0000269|PubMed:15531764}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(2E,4E)-hexadienoyl-CoA + H(+) + NADPH = (3E)-hexenoyl-CoA + CC NADP(+); Xref=Rhea:RHEA:44912, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, CC ChEBI:CHEBI:58349, ChEBI:CHEBI:84788, ChEBI:CHEBI:84790; CC Evidence={ECO:0000269|PubMed:15531764}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=7.7 uM for NADPH {ECO:0000269|PubMed:15531764}; CC KM=14.3 uM for trans-2,trans-4-hexadienoyl-CoA CC {ECO:0000269|PubMed:15531764}; CC Vmax=30.3 umol/min/mg enzyme {ECO:0000269|PubMed:15531764}; CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:15531764}. CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:7818482}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q16698-1; Sequence=Displayed; CC Name=2; CC IsoId=Q16698-2; Sequence=VSP_056388; CC -!- TISSUE SPECIFICITY: Heart = liver = pancreas > kidney >> skeletal CC muscle = lung. {ECO:0000269|PubMed:7818482}. CC -!- DISEASE: 2,4-dienoyl-CoA reductase deficiency (DECRD) [MIM:616034]: A CC rare, autosomal recessive, inborn error of polyunsaturated fatty acids CC and lysine metabolism, resulting in mitochondrial dysfunction. Affected CC individuals have a severe encephalopathy with neurologic and metabolic CC abnormalities beginning in early infancy. Laboratory studies show CC increased C10:2 carnitine levels and hyperlysinemia. CC {ECO:0000269|PubMed:24847004}. Note=The protein represented in this CC entry is involved in disease pathogenesis. A selective decrease in CC mitochondrial NADP(H) levels due to NADK2 mutations causes a deficiency CC of NADPH-dependent mitochondrial enzymes, such as DECR1 and AASS. CC {ECO:0000269|PubMed:24847004}. CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) CC family. 2,4-dienoyl-CoA reductase subfamily. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; L26050; AAA67551.1; -; mRNA. DR EMBL; U49352; AAB09423.1; -; mRNA. DR EMBL; U78302; AAB88724.1; -; Genomic_DNA. DR EMBL; U94980; AAB88724.1; JOINED; Genomic_DNA. DR EMBL; U94981; AAB88724.1; JOINED; Genomic_DNA. DR EMBL; U94982; AAB88724.1; JOINED; Genomic_DNA. DR EMBL; U94983; AAB88724.1; JOINED; Genomic_DNA. DR EMBL; U94984; AAB88724.1; JOINED; Genomic_DNA. DR EMBL; U94985; AAB88724.1; JOINED; Genomic_DNA. DR EMBL; U94986; AAB88724.1; JOINED; Genomic_DNA. DR EMBL; U94987; AAB88724.1; JOINED; Genomic_DNA. DR EMBL; AK300069; BAH13204.1; -; mRNA. DR EMBL; AC004612; AAC14671.1; -; Genomic_DNA. DR EMBL; AF049895; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC105080; AAI05081.1; -; mRNA. DR EMBL; BC105082; AAI05083.1; -; mRNA. DR CCDS; CCDS6250.1; -. [Q16698-1] DR CCDS; CCDS87618.1; -. [Q16698-2] DR PIR; S53352; S53352. DR RefSeq; NP_001317504.1; NM_001330575.1. [Q16698-2] DR RefSeq; NP_001350.1; NM_001359.1. [Q16698-1] DR RefSeq; XP_016868636.1; XM_017013147.1. DR RefSeq; XP_016868637.1; XM_017013148.1. DR PDB; 1W6U; X-ray; 1.75 A; A/B/C/D=35-335. DR PDB; 1W73; X-ray; 2.10 A; A/B/C/D=35-335. DR PDB; 1W8D; X-ray; 2.20 A; A/B/C/D=35-335. DR PDBsum; 1W6U; -. DR PDBsum; 1W73; -. DR PDBsum; 1W8D; -. DR AlphaFoldDB; Q16698; -. DR SMR; Q16698; -. DR BioGRID; 108030; 84. DR IntAct; Q16698; 45. DR MINT; Q16698; -. DR STRING; 9606.ENSP00000220764; -. DR DrugBank; DB08605; 6-METHYL-2(PROPANE-1-SULFONYL)-2H-THIENO[3,2-D][1,2,3]DIAZABORININ-1-OL. DR DrugBank; DB03461; Nicotinamide adenine dinucleotide phosphate. DR SwissLipids; SLP:000001049; -. DR CarbonylDB; Q16698; -. DR iPTMnet; Q16698; -. DR MetOSite; Q16698; -. DR PhosphoSitePlus; Q16698; -. DR SwissPalm; Q16698; -. DR BioMuta; DECR1; -. DR DMDM; 3913456; -. DR EPD; Q16698; -. DR jPOST; Q16698; -. DR MassIVE; Q16698; -. DR MaxQB; Q16698; -. DR PaxDb; 9606-ENSP00000220764; -. DR PeptideAtlas; Q16698; -. DR ProteomicsDB; 61037; -. [Q16698-1] DR ProteomicsDB; 6768; -. DR Pumba; Q16698; -. DR TopDownProteomics; Q16698-1; -. [Q16698-1] DR TopDownProteomics; Q16698-2; -. [Q16698-2] DR Antibodypedia; 12737; 310 antibodies from 28 providers. DR DNASU; 1666; -. DR Ensembl; ENST00000220764.7; ENSP00000220764.2; ENSG00000104325.7. [Q16698-1] DR Ensembl; ENST00000522161.5; ENSP00000429779.1; ENSG00000104325.7. [Q16698-2] DR GeneID; 1666; -. DR KEGG; hsa:1666; -. DR MANE-Select; ENST00000220764.7; ENSP00000220764.2; NM_001359.2; NP_001350.1. DR UCSC; uc003yek.2; human. [Q16698-1] DR AGR; HGNC:2753; -. DR CTD; 1666; -. DR DisGeNET; 1666; -. DR GeneCards; DECR1; -. DR HGNC; HGNC:2753; DECR1. DR HPA; ENSG00000104325; Tissue enhanced (heart muscle, liver). DR MIM; 222745; gene. DR MIM; 616034; phenotype. DR neXtProt; NX_Q16698; -. DR OpenTargets; ENSG00000104325; -. DR PharmGKB; PA141; -. DR VEuPathDB; HostDB:ENSG00000104325; -. DR eggNOG; KOG0725; Eukaryota. DR GeneTree; ENSGT00940000153801; -. DR HOGENOM; CLU_010194_1_2_1; -. DR InParanoid; Q16698; -. DR OMA; EFHSCDV; -. DR OrthoDB; 71414at2759; -. DR PhylomeDB; Q16698; -. DR TreeFam; TF315256; -. DR BRENDA; 1.3.1.124; 2681. DR PathwayCommons; Q16698; -. DR Reactome; R-HSA-77288; mitochondrial fatty acid beta-oxidation of unsaturated fatty acids. DR SABIO-RK; Q16698; -. DR SignaLink; Q16698; -. DR BioGRID-ORCS; 1666; 11 hits in 1159 CRISPR screens. DR ChiTaRS; DECR1; human. DR EvolutionaryTrace; Q16698; -. DR GenomeRNAi; 1666; -. DR Pharos; Q16698; Tbio. DR PRO; PR:Q16698; -. DR Proteomes; UP000005640; Chromosome 8. DR RNAct; Q16698; Protein. DR Bgee; ENSG00000104325; Expressed in left ventricle myocardium and 200 other cell types or tissues. DR ExpressionAtlas; Q16698; baseline and differential. DR GO; GO:1902494; C:catalytic complex; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome. DR GO; GO:0005739; C:mitochondrion; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; HDA:UniProtKB. DR GO; GO:0008670; F:2,4-dienoyl-CoA reductase (NADPH) activity; IDA:UniProtKB. DR GO; GO:0042802; F:identical protein binding; IPI:UniProtKB. DR GO; GO:0070402; F:NADPH binding; IDA:UniProtKB. DR GO; GO:0006635; P:fatty acid beta-oxidation; IDA:UniProtKB. DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; ISS:YuBioLab. DR CDD; cd05369; TER_DECR_SDR_a; 1. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR InterPro; IPR002347; SDR_fam. DR PANTHER; PTHR43658:SF14; 2,4-DIENOYL-COA REDUCTASE [(3E)-ENOYL-COA-PRODUCING], MITOCHONDRIAL; 1. DR PANTHER; PTHR43658; SHORT-CHAIN DEHYDROGENASE/REDUCTASE; 1. DR Pfam; PF13561; adh_short_C2; 1. DR PRINTS; PR00081; GDHRDH. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1. DR UCD-2DPAGE; Q16698; -. DR Genevisible; Q16698; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Fatty acid metabolism; KW Lipid metabolism; Mitochondrion; NADP; Oxidoreductase; Phosphoprotein; KW Reference proteome; Transit peptide. FT TRANSIT 1..34 FT /note="Mitochondrion" FT /evidence="ECO:0000305|PubMed:7818482" FT CHAIN 35..335 FT /note="2,4-dienoyl-CoA reductase [(3E)-enoyl-CoA- FT producing], mitochondrial" FT /id="PRO_0000031965" FT ACT_SITE 199 FT /note="Proton acceptor" FT /evidence="ECO:0000255" FT BINDING 66..71 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000269|PubMed:15531764" FT BINDING 91 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000269|PubMed:15531764" FT BINDING 91 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 117 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000269|PubMed:15531764" FT BINDING 119 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:15531764" FT BINDING 149 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:15531764" FT BINDING 157 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:15531764" FT BINDING 214 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000269|PubMed:15531764" FT BINDING 240..243 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000269|PubMed:15531764" FT BINDING 251 FT /ligand="substrate" FT /evidence="ECO:0000250" FT MOD_RES 42 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q9CQ62" FT MOD_RES 42 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q9CQ62" FT MOD_RES 49 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q9CQ62" FT MOD_RES 49 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q9CQ62" FT MOD_RES 69 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 73 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:Q9CQ62" FT MOD_RES 97 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q9CQ62" FT MOD_RES 97 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q9CQ62" FT MOD_RES 230 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 244 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q9CQ62" FT MOD_RES 244 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q9CQ62" FT MOD_RES 260 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q9CQ62" FT MOD_RES 260 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q9CQ62" FT MOD_RES 319 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q9CQ62" FT MOD_RES 319 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q9CQ62" FT VAR_SEQ 1..23 FT /note="MKLPARVFFTLGSRLPCGLAPRR -> MSGLGKKHLLLMGE (in FT isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_056388" FT VARIANT 333 FT /note="K -> N (in dbSNP:rs15094)" FT /id="VAR_012034" FT MUTAGEN 148 FT /note="N->A: Reduces enzyme activity by 97%." FT /evidence="ECO:0000269|PubMed:15531764" FT MUTAGEN 199 FT /note="Y->A: Reduces enzyme activity by 99%. Strongly FT reduced affinity for substrate and for NADP." FT /evidence="ECO:0000269|PubMed:15531764" FT MUTAGEN 210 FT /note="S->A: Reduces enzyme activity by over 99%." FT /evidence="ECO:0000269|PubMed:15531764" FT MUTAGEN 214 FT /note="K->A: Reduces enzyme activity by over 99%." FT /evidence="ECO:0000269|PubMed:15531764" FT CONFLICT 287 FT /note="D -> G (in Ref. 2; AAB09423)" FT /evidence="ECO:0000305" FT CONFLICT 292 FT /note="I -> V (in Ref. 2; AAB09423)" FT /evidence="ECO:0000305" FT CONFLICT 303 FT /note="E -> G (in Ref. 2; AAB09423)" FT /evidence="ECO:0000305" FT CONFLICT 311 FT /note="F -> G (in Ref. 2; AAB09423)" FT /evidence="ECO:0000305" FT HELIX 36..43 FT /evidence="ECO:0007829|PDB:1W6U" FT TURN 54..59 FT /evidence="ECO:0007829|PDB:1W6U" FT STRAND 61..65 FT /evidence="ECO:0007829|PDB:1W6U" FT TURN 66..68 FT /evidence="ECO:0007829|PDB:1W6U" FT HELIX 70..81 FT /evidence="ECO:0007829|PDB:1W6U" FT STRAND 85..91 FT /evidence="ECO:0007829|PDB:1W6U" FT HELIX 93..107 FT /evidence="ECO:0007829|PDB:1W6U" FT STRAND 111..115 FT /evidence="ECO:0007829|PDB:1W6U" FT HELIX 121..134 FT /evidence="ECO:0007829|PDB:1W6U" FT STRAND 139..143 FT /evidence="ECO:0007829|PDB:1W6U" FT HELIX 153..155 FT /evidence="ECO:0007829|PDB:1W6U" FT HELIX 158..185 FT /evidence="ECO:0007829|PDB:1W6U" FT STRAND 190..195 FT /evidence="ECO:0007829|PDB:1W6U" FT HELIX 199..202 FT /evidence="ECO:0007829|PDB:1W6U" FT HELIX 208..228 FT /evidence="ECO:0007829|PDB:1W6U" FT HELIX 229..231 FT /evidence="ECO:0007829|PDB:1W6U" FT STRAND 233..240 FT /evidence="ECO:0007829|PDB:1W6U" FT STRAND 254..256 FT /evidence="ECO:0007829|PDB:1W73" FT HELIX 257..263 FT /evidence="ECO:0007829|PDB:1W6U" FT HELIX 274..284 FT /evidence="ECO:0007829|PDB:1W6U" FT HELIX 287..289 FT /evidence="ECO:0007829|PDB:1W6U" FT STRAND 296..300 FT /evidence="ECO:0007829|PDB:1W6U" FT HELIX 303..308 FT /evidence="ECO:0007829|PDB:1W6U" FT HELIX 312..316 FT /evidence="ECO:0007829|PDB:1W6U" FT HELIX 319..325 FT /evidence="ECO:0007829|PDB:1W6U" SQ SEQUENCE 335 AA; 36068 MW; F04E72AACB718430 CRC64; MKLPARVFFT LGSRLPCGLA PRRFFSYGTK ILYQNTEALQ SKFFSPLQKA MLPPNSFQGK VAFITGGGTG LGKGMTTLLS SLGAQCVIAS RKMDVLKATA EQISSQTGNK VHAIQCDVRD PDMVQNTVSE LIKVAGHPNI VINNAAGNFI SPTERLSPNA WKTITDIVLN GTAFVTLEIG KQLIKAQKGA AFLSITTIYA ETGSGFVVPS ASAKAGVEAM SKSLAAEWGK YGMRFNVIQP GPIKTKGAFS RLDPTGTFEK EMIGRIPCGR LGTVEELANL AAFLCSDYAS WINGAVIKFD GGEEVLISGE FNDLRKVTKE QWDTIEELIR KTKGS //