ID ACADS_HUMAN Reviewed; 412 AA. AC P16219; P78331; DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1990, sequence version 1. DT 27-MAR-2024, entry version 229. DE RecName: Full=Short-chain specific acyl-CoA dehydrogenase, mitochondrial; DE Short=SCAD; DE EC=1.3.8.1 {ECO:0000269|PubMed:21237683}; DE AltName: Full=Butyryl-CoA dehydrogenase; DE Flags: Precursor; GN Name=ACADS; 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]. RX PubMed=2565344; DOI=10.1172/jci114058; RA Naito E., Ozasa H., Ikeda Y., Tanaka K.; RT "Molecular cloning and nucleotide sequence of complementary DNAs encoding RT human short chain acyl-coenzyme A dehydrogenase and the study of the RT molecular basis of human short chain acyl-coenzyme A dehydrogenase RT deficiency."; RL J. Clin. Invest. 83:1605-1613(1989). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=9383286; DOI=10.1007/s003359900612; RA Corydon M.J., Andresen B.S., Bross P., Kjeldsen M., Andreasen P.H., RA Eiberg H., Koelvraa S., Gregersen N.; RT "Structural organization of the human short-chain acyl-CoA dehydrogenase RT gene."; RL Mamm. Genome 8:922-926(1997). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Yamagata K., Oda N., Furuta H., Vaxillaire M., Southam L., Boriraj V., RA Chen X., Oda Y., Takeda J., Yamada S., Nishigori H., Lebeau M.M., RA Lathrop M., Cox R.D., Bell G.I.; RT "Transcription map of the 5cM region surrounding the hepatocyte nuclear RT factor-1a/MODY3 gene on chromosome 12."; RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Retinal pigment epithelium; 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 [5] RP PROTEIN SEQUENCE OF 25-34. RC TISSUE=Liver; RX PubMed=1286669; DOI=10.1002/elps.11501301201; RA Hochstrasser D.F., Frutiger S., Paquet N., Bairoch A., Ravier F., RA Pasquali C., Sanchez J.-C., Tissot J.-D., Bjellqvist B., Vargas R., RA Appel R.D., Hughes G.J.; RT "Human liver protein map: a reference database established by RT microsequencing and gel comparison."; RL Electrophoresis 13:992-1001(1992). RN [6] 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 [7] RP FUNCTION, CATALYTIC ACTIVITY, AND SUBSTRATE SPECIFICITY. RX PubMed=21237683; DOI=10.1016/j.ymgme.2010.12.005; RA He M., Pei Z., Mohsen A.W., Watkins P., Murdoch G., Van Veldhoven P.P., RA Ensenauer R., Vockley J.; RT "Identification and characterization of new long chain acyl-CoA RT dehydrogenases."; RL Mol. Genet. Metab. 102:418-429(2011). RN [8] RP IDENTIFICATION BY 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 [9] 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 [10] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 30-412 IN COMPLEX WITH FAD AND RP SUBSTRATE ANALOG, AND COFACTOR. RG Structural genomics consortium (SGC); RT "Crystal structure of human RAB14."; RL Submitted (FEB-2009) to the PDB data bank. RN [11] RP VARIANTS ACADSD TRP-46 AND CYS-107. RX PubMed=1692038; DOI=10.1172/jci114607; RA Naito E., Indo Y., Tanaka K.; RT "Identification of two variant short chain acyl-coenzyme A dehydrogenase RT alleles, each containing a different point mutation in a patient with short RT chain acyl-coenzyme A dehydrogenase deficiency."; RL J. Clin. Invest. 85:1575-1582(1990). RN [12] RP VARIANTS ACADSD CYS-92; ARG-177 AND CYS-383, AND VARIANTS TRP-171 AND RP SER-209. RX PubMed=9499414; DOI=10.1093/hmg/7.4.619; RA Gregersen N., Winter V.S., Corydon M.J., Corydon T.J., Rinaldo P., RA Ribes A., Martinez G., Bennett M.J., Vianey-Saban C., Bhala A., Hale D.E., RA Lehnert W., Kmoch S., Roig M., Riudor E., Eiberg H., Andresen B.S., RA Bross P., Bolund L.A., Koelvraa S.; RT "Identification of four new mutations in the short-chain acyl-CoA RT dehydrogenase (SCAD) gene in two patients: one of the variant alleles, RT 511C-->T, is present at an unexpectedly high frequency in the general RT population, as was the case for 625G-->A, together conferring RT susceptibility to ethylmalonic aciduria."; RL Hum. Mol. Genet. 7:619-627(1998). RN [13] RP VARIANTS ACADSD SER-90; GLU-104 DEL; VAL-192; TRP-325; LEU-353 AND TRP-380, RP VARIANTS TRP-171 AND SER-209, CHARACTERIZATION OF VARIANTS ACADSD SER-90; RP GLU-104 DEL; VAL-192; TRP-325; LEU-353 AND TRP-380, CHARACTERIZATION OF RP VARIANTS TRP-171 AND SER-209, FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY. RX PubMed=11134486; DOI=10.1203/00006450-200101000-00008; RA Corydon M.J., Vockley J., Rinaldo P., Rhead W.J., Kjeldsen M., Winter V.S., RA Riggs C., Babovic-Vuksanovic D., Smeitink J., De Jong J., Levy H., RA Sewell A.C., Roe C., Matern D., Dasouki M., Gregersen N.; RT "Role of common gene variations in the molecular pathogenesis of short- RT chain acyl-CoA dehydrogenase deficiency."; RL Pediatr. Res. 49:18-23(2001). CC -!- FUNCTION: Short-chain specific acyl-CoA dehydrogenase is one of the CC acyl-CoA dehydrogenases that catalyze the first step of mitochondrial CC fatty acid beta-oxidation, an aerobic process breaking down fatty acids CC into acetyl-CoA and allowing the production of energy from fats (By CC similarity). The first step of fatty acid beta-oxidation consists in CC the removal of one hydrogen from C-2 and C-3 of the straight-chain CC fatty acyl-CoA thioester, resulting in the formation of trans-2-enoyl- CC CoA (By similarity). Among the different mitochondrial acyl-CoA CC dehydrogenases, short-chain specific acyl-CoA dehydrogenase acts CC specifically on acyl-CoAs with saturated 4 to 6 carbons long primary CC chains (PubMed:21237683, PubMed:11134486). CC {ECO:0000250|UniProtKB:P15651, ECO:0000269|PubMed:11134486, CC ECO:0000269|PubMed:21237683}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a short-chain 2,3-saturated fatty acyl-CoA + H(+) + oxidized CC [electron-transfer flavoprotein] = a short-chain (2E)-enoyl-CoA + CC reduced [electron-transfer flavoprotein]; Xref=Rhea:RHEA:47196, CC Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:87487, CC ChEBI:CHEBI:87488; EC=1.3.8.1; CC Evidence={ECO:0000269|PubMed:21237683}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47197; CC Evidence={ECO:0000305|PubMed:11134486}; CC -!- CATALYTIC ACTIVITY: CC Reaction=butanoyl-CoA + H(+) + oxidized [electron-transfer CC flavoprotein] = (2E)-butenoyl-CoA + reduced [electron-transfer CC flavoprotein]; Xref=Rhea:RHEA:24004, Rhea:RHEA-COMP:10685, Rhea:RHEA- CC COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57332, ChEBI:CHEBI:57371, CC ChEBI:CHEBI:57692, ChEBI:CHEBI:58307; EC=1.3.8.1; CC Evidence={ECO:0000269|PubMed:21237683}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24005; CC Evidence={ECO:0000305|PubMed:11134486}; CC -!- CATALYTIC ACTIVITY: CC Reaction=H(+) + oxidized [electron-transfer flavoprotein] + pentanoyl- CC CoA = (2E)-pentenoyl-CoA + reduced [electron-transfer flavoprotein]; CC Xref=Rhea:RHEA:43456, Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57389, ChEBI:CHEBI:57692, CC ChEBI:CHEBI:58307, ChEBI:CHEBI:86160; CC Evidence={ECO:0000250|UniProtKB:Q3ZBF6}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43457; CC Evidence={ECO:0000305|PubMed:11134486}; CC -!- CATALYTIC ACTIVITY: CC Reaction=H(+) + hexanoyl-CoA + oxidized [electron-transfer CC flavoprotein] = (2E)-hexenoyl-CoA + reduced [electron-transfer CC flavoprotein]; Xref=Rhea:RHEA:43464, Rhea:RHEA-COMP:10685, Rhea:RHEA- CC COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, CC ChEBI:CHEBI:62077, ChEBI:CHEBI:62620; CC Evidence={ECO:0000269|PubMed:21237683}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43465; CC Evidence={ECO:0000305|PubMed:11134486}; CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|Ref.10}; CC Note=Binds 1 FAD per subunit. {ECO:0000269|Ref.10}; CC -!- PATHWAY: Lipid metabolism; mitochondrial fatty acid beta-oxidation. CC {ECO:0000305|PubMed:11134486}. CC -!- SUBUNIT: Homotetramer. {ECO:0000269|Ref.10}. CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix CC {ECO:0000250|UniProtKB:Q3ZBF6}. CC -!- DISEASE: Acyl-CoA dehydrogenase short-chain deficiency (ACADSD) CC [MIM:201470]: An inborn error of mitochondrial fatty acid beta- CC oxidation resulting in acute acidosis and muscle weakness in infants, CC and a form of lipid-storage myopathy in adults. CC {ECO:0000269|PubMed:11134486, ECO:0000269|PubMed:1692038, CC ECO:0000269|PubMed:9499414}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family. CC {ECO:0000305}. CC -!- WEB RESOURCE: Name=Wikipedia; Note=Butyryl-CoA dehydrogenase entry; CC URL="https://en.wikipedia.org/wiki/Butyryl_CoA_dehydrogenase"; 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; M26393; AAA60307.1; -; mRNA. DR EMBL; Z80345; CAB02492.1; -; Genomic_DNA. DR EMBL; Z80347; CAB02492.1; JOINED; Genomic_DNA. DR EMBL; U83992; AAD00552.1; -; Genomic_DNA. DR EMBL; U83991; AAD00552.1; JOINED; Genomic_DNA. DR EMBL; BC025963; AAH25963.1; -; mRNA. DR CCDS; CCDS9207.1; -. DR PIR; A30605; A30605. DR RefSeq; NP_000008.1; NM_000017.3. DR RefSeq; NP_001289483.1; NM_001302554.1. DR PDB; 2VIG; X-ray; 1.90 A; A/B/C/D/E/F/G/H=30-412. DR PDB; 7Y0A; X-ray; 2.32 A; A/B/C/D=25-412. DR PDB; 7Y0B; X-ray; 2.08 A; A/B/C/D=25-412. DR PDBsum; 2VIG; -. DR PDBsum; 7Y0A; -. DR PDBsum; 7Y0B; -. DR AlphaFoldDB; P16219; -. DR SMR; P16219; -. DR BioGRID; 106553; 24. DR IntAct; P16219; 13. DR MINT; P16219; -. DR STRING; 9606.ENSP00000242592; -. DR DrugBank; DB03059; Acetoacetyl-CoA. DR DrugBank; DB03147; Flavin adenine dinucleotide. DR DrugBank; DB00157; NADH. DR SwissLipids; SLP:000001403; -. DR iPTMnet; P16219; -. DR MetOSite; P16219; -. DR PhosphoSitePlus; P16219; -. DR SwissPalm; P16219; -. DR BioMuta; ACADS; -. DR DMDM; 113019; -. DR DOSAC-COBS-2DPAGE; P16219; -. DR EPD; P16219; -. DR jPOST; P16219; -. DR MassIVE; P16219; -. DR MaxQB; P16219; -. DR PaxDb; 9606-ENSP00000242592; -. DR PeptideAtlas; P16219; -. DR ProteomicsDB; 53323; -. DR Pumba; P16219; -. DR Antibodypedia; 1579; 305 antibodies from 31 providers. DR DNASU; 35; -. DR Ensembl; ENST00000242592.9; ENSP00000242592.4; ENSG00000122971.9. DR GeneID; 35; -. DR KEGG; hsa:35; -. DR MANE-Select; ENST00000242592.9; ENSP00000242592.4; NM_000017.4; NP_000008.1. DR UCSC; uc001tza.5; human. DR AGR; HGNC:90; -. DR CTD; 35; -. DR DisGeNET; 35; -. DR GeneCards; ACADS; -. DR GeneReviews; ACADS; -. DR HGNC; HGNC:90; ACADS. DR HPA; ENSG00000122971; Tissue enhanced (liver, skeletal muscle). DR MalaCards; ACADS; -. DR MIM; 201470; phenotype. DR MIM; 606885; gene. DR neXtProt; NX_P16219; -. DR OpenTargets; ENSG00000122971; -. DR Orphanet; 26792; Short chain acyl-CoA dehydrogenase deficiency. DR PharmGKB; PA24426; -. DR VEuPathDB; HostDB:ENSG00000122971; -. DR eggNOG; KOG0139; Eukaryota. DR GeneTree; ENSGT00940000158866; -. DR HOGENOM; CLU_018204_0_2_1; -. DR InParanoid; P16219; -. DR OMA; LYREAPM; -. DR OrthoDB; 275353at2759; -. DR PhylomeDB; P16219; -. DR TreeFam; TF105019; -. DR BioCyc; MetaCyc:HS04619-MONOMER; -. DR PathwayCommons; P16219; -. DR Reactome; R-HSA-77350; Beta oxidation of hexanoyl-CoA to butanoyl-CoA. DR Reactome; R-HSA-77352; Beta oxidation of butanoyl-CoA to acetyl-CoA. DR SABIO-RK; P16219; -. DR SignaLink; P16219; -. DR UniPathway; UPA00660; -. DR BioGRID-ORCS; 35; 11 hits in 1158 CRISPR screens. DR ChiTaRS; ACADS; human. DR EvolutionaryTrace; P16219; -. DR GenomeRNAi; 35; -. DR Pharos; P16219; Tbio. DR PRO; PR:P16219; -. DR Proteomes; UP000005640; Chromosome 12. DR RNAct; P16219; Protein. DR Bgee; ENSG00000122971; Expressed in right lobe of liver and 158 other cell types or tissues. DR ExpressionAtlas; P16219; baseline and differential. DR GO; GO:0005813; C:centrosome; IDA:HPA. DR GO; GO:0005759; C:mitochondrial matrix; ISS:UniProtKB. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; HDA:UniProtKB. DR GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IDA:BHF-UCL. DR GO; GO:0004085; F:butyryl-CoA dehydrogenase activity; ISS:UniProtKB. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0046359; P:butyrate catabolic process; IBA:GO_Central. DR GO; GO:0006635; P:fatty acid beta-oxidation; TAS:ProtInc. DR GO; GO:0033539; P:fatty acid beta-oxidation using acyl-CoA dehydrogenase; IDA:BHF-UCL. DR CDD; cd01158; SCAD_SBCAD; 1. DR Gene3D; 1.10.540.10; Acyl-CoA dehydrogenase/oxidase, N-terminal domain; 1. DR Gene3D; 2.40.110.10; Butyryl-CoA Dehydrogenase, subunit A, domain 2; 1. DR Gene3D; 1.20.140.10; Butyryl-CoA Dehydrogenase, subunit A, domain 3; 1. DR InterPro; IPR006089; Acyl-CoA_DH_CS. DR InterPro; IPR006091; Acyl-CoA_Oxase/DH_mid-dom. DR InterPro; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf. DR InterPro; IPR036250; AcylCo_DH-like_C. DR InterPro; IPR009075; AcylCo_DH/oxidase_C. DR InterPro; IPR013786; AcylCoA_DH/ox_N. DR InterPro; IPR037069; AcylCoA_DH/ox_N_sf. DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom_sf. DR PANTHER; PTHR43884; ACYL-COA DEHYDROGENASE; 1. DR PANTHER; PTHR43884:SF42; SHORT-CHAIN SPECIFIC ACYL-COA DEHYDROGENASE, MITOCHONDRIAL; 1. DR Pfam; PF00441; Acyl-CoA_dh_1; 1. DR Pfam; PF02770; Acyl-CoA_dh_M; 1. DR Pfam; PF02771; Acyl-CoA_dh_N; 1. DR PIRSF; PIRSF016578; HsaA; 1. DR SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1. DR SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1. DR PROSITE; PS00072; ACYL_COA_DH_1; 1. DR PROSITE; PS00073; ACYL_COA_DH_2; 1. DR SWISS-2DPAGE; P16219; -. DR UCD-2DPAGE; P16219; -. DR Genevisible; P16219; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Direct protein sequencing; Disease variant; FAD; KW Fatty acid metabolism; Flavoprotein; Lipid metabolism; Mitochondrion; KW Oxidoreductase; Phosphoprotein; Reference proteome; Transit peptide. FT TRANSIT 1..24 FT /note="Mitochondrion" FT /evidence="ECO:0000269|PubMed:1286669" FT CHAIN 25..412 FT /note="Short-chain specific acyl-CoA dehydrogenase, FT mitochondrial" FT /id="PRO_0000000498" FT ACT_SITE 392 FT /note="Proton acceptor" FT /evidence="ECO:0000250|UniProtKB:P15651" FT BINDING 152..161 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000269|Ref.10" FT BINDING 161 FT /ligand="substrate" FT BINDING 185..187 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000269|Ref.10" FT BINDING 269..272 FT /ligand="substrate" FT BINDING 297 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000269|Ref.10" FT BINDING 308 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000269|Ref.10" FT BINDING 365..369 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000269|Ref.10" FT BINDING 393 FT /ligand="substrate" FT BINDING 394..396 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000269|Ref.10" FT MOD_RES 27 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q07417" FT MOD_RES 51 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q07417" FT MOD_RES 51 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q07417" FT MOD_RES 72 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q07417" FT MOD_RES 129 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q07417" FT MOD_RES 129 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q07417" FT MOD_RES 208 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q07417" FT MOD_RES 262 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q07417" FT MOD_RES 262 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q07417" FT MOD_RES 306 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q07417" FT MOD_RES 306 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q07417" FT VARIANT 46 FT /note="R -> W (in ACADSD; dbSNP:rs121908003)" FT /evidence="ECO:0000269|PubMed:1692038" FT /id="VAR_000310" FT VARIANT 90 FT /note="G -> S (in ACADSD; loss of acyl-CoA dehydrogenase FT activity; dbSNP:rs121908005)" FT /evidence="ECO:0000269|PubMed:11134486" FT /id="VAR_013565" FT VARIANT 92 FT /note="G -> C (in ACADSD; dbSNP:rs121908004)" FT /evidence="ECO:0000269|PubMed:9499414" FT /id="VAR_000311" FT VARIANT 104 FT /note="Missing (in ACADSD; loss of acyl-CoA dehydrogenase FT activity; dbSNP:rs387906308)" FT /evidence="ECO:0000269|PubMed:11134486" FT /id="VAR_013566" FT VARIANT 107 FT /note="R -> C (in ACADSD; dbSNP:rs61732144)" FT /evidence="ECO:0000269|PubMed:1692038" FT /id="VAR_000312" FT VARIANT 171 FT /note="R -> W (69% of wild-type acyl-CoA dehydrogenase FT activity; confers susceptibility to ethylmalonicaciduria; FT dbSNP:rs1800556)" FT /evidence="ECO:0000269|PubMed:11134486, FT ECO:0000269|PubMed:9499414" FT /id="VAR_013567" FT VARIANT 177 FT /note="W -> R (in ACADSD; dbSNP:rs57443665)" FT /evidence="ECO:0000269|PubMed:9499414" FT /id="VAR_000314" FT VARIANT 192 FT /note="A -> V (in ACADSD; loss of acyl-CoA dehydrogenase FT activity; dbSNP:rs28940874)" FT /evidence="ECO:0000269|PubMed:11134486" FT /id="VAR_013568" FT VARIANT 209 FT /note="G -> S (86% of wild-type acyl-CoA dehydrogenase FT activity; confers susceptibility to ethylmalonicaciduria; FT dbSNP:rs1799958)" FT /evidence="ECO:0000269|PubMed:11134486, FT ECO:0000269|PubMed:9499414" FT /id="VAR_000315" FT VARIANT 325 FT /note="R -> W (in ACADSD; loss of acyl-CoA dehydrogenase FT activity; dbSNP:rs121908006)" FT /evidence="ECO:0000269|PubMed:11134486" FT /id="VAR_013569" FT VARIANT 353 FT /note="S -> L (in ACADSD; loss of acyl-CoA dehydrogenase FT activity; dbSNP:rs28941773)" FT /evidence="ECO:0000269|PubMed:11134486" FT /id="VAR_013570" FT VARIANT 380 FT /note="R -> W (in ACADSD; loss of acyl-CoA dehydrogenase FT activity; dbSNP:rs28940875)" FT /evidence="ECO:0000269|PubMed:11134486" FT /id="VAR_013571" FT VARIANT 383 FT /note="R -> C (in ACADSD; dbSNP:rs28940872)" FT /evidence="ECO:0000269|PubMed:9499414" FT /id="VAR_000316" FT VARIANT 383 FT /note="R -> H (in dbSNP:rs35233375)" FT /id="VAR_033458" FT HELIX 36..52 FT /evidence="ECO:0007829|PDB:2VIG" FT TURN 53..56 FT /evidence="ECO:0007829|PDB:2VIG" FT HELIX 57..63 FT /evidence="ECO:0007829|PDB:2VIG" FT HELIX 68..77 FT /evidence="ECO:0007829|PDB:2VIG" FT TURN 78..80 FT /evidence="ECO:0007829|PDB:2VIG" FT HELIX 86..88 FT /evidence="ECO:0007829|PDB:2VIG" FT HELIX 95..108 FT /evidence="ECO:0007829|PDB:2VIG" FT HELIX 110..121 FT /evidence="ECO:0007829|PDB:2VIG" FT HELIX 124..130 FT /evidence="ECO:0007829|PDB:2VIG" FT HELIX 133..139 FT /evidence="ECO:0007829|PDB:2VIG" FT HELIX 141..143 FT /evidence="ECO:0007829|PDB:2VIG" FT STRAND 144..147 FT /evidence="ECO:0007829|PDB:2VIG" FT STRAND 150..153 FT /evidence="ECO:0007829|PDB:2VIG" FT STRAND 159..162 FT /evidence="ECO:0007829|PDB:2VIG" FT HELIX 163..165 FT /evidence="ECO:0007829|PDB:2VIG" FT STRAND 169..173 FT /evidence="ECO:0007829|PDB:2VIG" FT STRAND 176..187 FT /evidence="ECO:0007829|PDB:2VIG" FT TURN 188..191 FT /evidence="ECO:0007829|PDB:2VIG" FT STRAND 193..200 FT /evidence="ECO:0007829|PDB:2VIG" FT STRAND 203..205 FT /evidence="ECO:0007829|PDB:2VIG" FT STRAND 210..218 FT /evidence="ECO:0007829|PDB:2VIG" FT STRAND 222..224 FT /evidence="ECO:0007829|PDB:2VIG" FT STRAND 230..232 FT /evidence="ECO:0007829|PDB:2VIG" FT STRAND 238..249 FT /evidence="ECO:0007829|PDB:2VIG" FT HELIX 250..252 FT /evidence="ECO:0007829|PDB:2VIG" FT STRAND 253..256 FT /evidence="ECO:0007829|PDB:2VIG" FT HELIX 260..296 FT /evidence="ECO:0007829|PDB:2VIG" FT HELIX 304..306 FT /evidence="ECO:0007829|PDB:2VIG" FT HELIX 308..336 FT /evidence="ECO:0007829|PDB:2VIG" FT HELIX 342..367 FT /evidence="ECO:0007829|PDB:2VIG" FT HELIX 368..372 FT /evidence="ECO:0007829|PDB:2VIG" FT HELIX 378..388 FT /evidence="ECO:0007829|PDB:2VIG" FT TURN 389..392 FT /evidence="ECO:0007829|PDB:2VIG" FT HELIX 395..411 FT /evidence="ECO:0007829|PDB:2VIG" SQ SEQUENCE 412 AA; 44297 MW; 3E946ADFC3DA3C0E CRC64; MAAALLARAS GPARRALCPR AWRQLHTIYQ SVELPETHQM LLQTCRDFAE KELFPIAAQV DKEHLFPAAQ VKKMGGLGLL AMDVPEELGG AGLDYLAYAI AMEEISRGCA STGVIMSVNN SLYLGPILKF GSKEQKQAWV TPFTSGDKIG CFALSEPGNG SDAGAASTTA RAEGDSWVLN GTKAWITNAW EASAAVVFAS TDRALQNKGI SAFLVPMPTP GLTLGKKEDK LGIRGSSTAN LIFEDCRIPK DSILGEPGMG FKIAMQTLDM GRIGIASQAL GIAQTALDCA VNYAENRMAF GAPLTKLQVI QFKLADMALA LESARLLTWR AAMLKDNKKP FIKEAAMAKL AASEAATAIS HQAIQILGGM GYVTEMPAER HYRDARITEI YEGTSEIQRL VIAGHLLRSY RS //