ID ACADV_HUMAN Reviewed; 655 AA. AC P49748; B4DEB6; F5H2A9; O76056; Q8WUL0; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 02-SEP-2026, entry version 235. DE RecName: Full=Very long-chain acyl-CoA dehydrogenase, mitochondrial {ECO:0000303|PubMed:7668252}; DE Short=VLCAD {ECO:0000303|PubMed:7668252}; DE EC=1.3.8.9 {ECO:0000269|PubMed:21237683}; DE AltName: Full=Long-chain acyl-CoA dehydrogenase, mitochondrial; DE EC=1.3.8.8 {ECO:0000269|PubMed:17374501, ECO:0000269|PubMed:21237683, ECO:0000269|PubMed:7668252, ECO:0000269|PubMed:9461620, ECO:0000269|PubMed:9599005, ECO:0000269|PubMed:9839948}; DE Flags: Precursor; GN Name=ACADVL {ECO:0000312|HGNC:HGNC:92}; GN Synonyms=VLCAD {ECO:0000303|PubMed:7668252}; 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), PARTIAL PROTEIN SEQUENCE, FUNCTION, RP CATALYTIC ACTIVITY, PATHWAY, INVOLVEMENT IN ACADVLD, AND TRANSIT PEPTIDE. RX PubMed=7668252; RA Aoyama T., Souri M., Ueno I., Kamijo T., Yamaguchi S., Rhead W.J., RA Tanaka K., Hashimoto T.; RT "Cloning of human very-long-chain acyl-coenzyme A dehydrogenase and RT molecular characterization of its deficiency in two patients."; RL Am. J. Hum. Genet. 57:273-283(1995). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND VARIANTS RP ACADVLD MET-260; ASP-281; ALA-283; ALA-317; CYS-366; GLU-381 DEL; ASP-441 RP AND ILE-602. RC TISSUE=Placenta; RX PubMed=8845838; DOI=10.1093/hmg/5.4.461; RA Andresen B.S., Bross P., Vianey-Saban C., Divry P., Zabot M.-T., Roe C.R., RA Nada M.A., Byskov A., Kruse T.A., Neve S., Kristiansen K., Knudsen I., RA Corydon M.J., Gregersen N.; RT "Cloning and characterization of human very-long-chain acyl-CoA RT dehydrogenase cDNA, chromosomal assignment of the gene and identification RT in four patients of nine different mutations within the VLCAD gene."; RL Hum. Mol. Genet. 5:461-472(1996). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1). RC TISSUE=Peripheral blood; RX PubMed=8554625; DOI=10.1006/bbrc.1995.2867; RA Orii K.O., Aoyama T., Souri M., Orii K.E., Kondo N., Orii T., Hashimoto T.; RT "Genomic DNA organization of human mitochondrial very-long-chain acyl-CoA RT dehydrogenase and mutation analysis."; RL Biochem. Biophys. Res. Commun. 217:987-992(1995). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RC TISSUE=Cerebellum; 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=16625196; DOI=10.1038/nature04689; RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.; RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the RT human lineage."; RL Nature 440:1045-1049(2006). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Liver, Lung, and Pancreas; 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 CHARACTERIZATION. RX PubMed=7769092; DOI=10.1172/jci117947; RA Aoyama T., Souri M., Ushikubo S., Kamijo T., Yamaguchi S., Kelley R.I., RA Rhead W.J., Uetake K., Tanaka K., Hashimoto T.; RT "Purification of human very-long-chain acyl-coenzyme A dehydrogenase and RT characterization of its deficiency in seven patients."; RL J. Clin. Invest. 95:2465-2473(1995). RN [8] RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, RP SUBUNIT, SUBCELLULAR LOCATION, MUTAGENESIS OF PHE-458 AND GLU-462, ACTIVE RP SITE, AND CHARACTERIZATION OF VARIANT ACADVLD LEU-458. RX PubMed=9461620; DOI=10.1074/jbc.273.7.4227; RA Souri M., Aoyama T., Cox G.F., Hashimoto T.; RT "Catalytic and FAD-binding residues of mitochondrial very long chain acyl- RT coenzyme A dehydrogenase."; RL J. Biol. Chem. 273:4227-4231(1998). RN [9] RP VARIANTS ACADVLD ASP-43; ASN-158; ARG-159; MET-174; SER-185; LYS-218; RP ARG-243; THR-247; MET-260; LYS-278 DEL; ASP-281; ALA-283; ASP-290; GLU-294; RP ASN-299; ALA-317; VAL-352; CYS-366; HIS-366; GLU-381 DEL; HIS-405; ASP-441; RP HIS-450; GLN-453; ASN-454; HIS-456; TRP-459; GLU-463; GLN-469; TRP-469; RP PRO-502; ILE-602 AND TRP-613. RX PubMed=9973285; DOI=10.1086/302261; RA Andresen B.S., Olpin S., Poorthuis B.J.H.M., Scholte H.R., Vianey-Saban C., RA Wanders R., Ijlst L., Morris A., Pourfarzam M., Bartlett K., RA Baumgartner E.R., de Klerk J.B.C., Schroeder L.D., Corydon T.J., Lund H., RA Winter V., Bross P., Bolund L., Gregersen N.; RT "Clear correlation of genotype with disease phenotype in very-long-chain RT acyl-CoA dehydrogenase deficiency."; RL Am. J. Hum. Genet. 64:479-494(1999). RN [10] RP CATALYTIC ACTIVITY (ISOFORM 2), SUBCELLULAR LOCATION (ISOFORM 2), TOPOLOGY RP (ISOFORM 2), CHARACTERIZATION OF VARIANTS ACADVLD PRO-490 AND PRO-502, AND RP HOMODIMERIZATION. RX PubMed=17374501; DOI=10.1016/j.ymgme.2007.01.013; RA Goetzman E.S., Wang Y., He M., Mohsen A.W., Ninness B.K., Vockley J.; RT "Expression and characterization of mutations in human very long-chain RT acyl-CoA dehydrogenase using a prokaryotic system."; RL Mol. Genet. Metab. 91:138-147(2007). RN [11] RP FUNCTION, CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY. RX PubMed=17564966; DOI=10.1086/519219; RA He M., Rutledge S.L., Kelly D.R., Palmer C.A., Murdoch G., Majumder N., RA Nicholls R.D., Pei Z., Watkins P.A., Vockley J.; RT "A new genetic disorder in mitochondrial fatty acid beta-oxidation: ACAD9 RT deficiency."; RL Am. J. Hum. Genet. 81:87-103(2007). RN [12] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-239 AND LYS-331, AND RP IDENTIFICATION BY MASS 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 [13] 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 [14] RP 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 [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-517 AND SER-522, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [16] 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 [17] RP CLEAVAGE OF TRANSIT PEPTIDE [LARGE SCALE ANALYSIS] AFTER TYR-40, AND 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 [18] RP REVIEW ON THE PHYSIOLOGICAL ROLE OF THE MITOCHONDRIAL FATTY ACID RP BETA-OXIDATION, FUNCTION, AND CAUTION. RX PubMed=26474213; DOI=10.1146/annurev-physiol-021115-105045; RA Houten S.M., Violante S., Ventura F.V., Wanders R.J.; RT "The Biochemistry and Physiology of Mitochondrial Fatty Acid beta-Oxidation RT and Its Genetic Disorders."; RL Annu. Rev. Physiol. 78:23-44(2016). RN [19] {ECO:0007744|PDB:2UXW} RP X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 69-655 IN COMPLEX WITH FAD AND RP SUBSTRATE ANALOG. RA Pike A.C.W., Hozjan V., Smee C., Berridge G., Burgess N., Salah E., RA Bunkoczi G., Uppenberg J., Ugochukwu E., von Delft F., Arrowsmith C.H., RA Edwards A., Weigelt J., Sundstrom M., Oppermann U.; RT "Crystal Structure of Human Very Long Chain Acyl- Coa Dehydrogenase RT (Acadvl)."; RL Submitted (MAR-2007) to the PDB data bank. RN [20] {ECO:0007744|PDB:3B96} RP X-RAY CRYSTALLOGRAPHY (1.91 ANGSTROMS) OF 69-655 IN COMPLEX WITH RP TETRADECANOYL-COA AND FAD, FUNCTION, SUBUNIT, COFACTOR, AND ACTIVE SITE. RX PubMed=18227065; DOI=10.1074/jbc.m709135200; RA McAndrew R.P., Wang Y., Mohsen A.W., He M., Vockley J., Kim J.J.; RT "Structural basis for substrate fatty acyl chain specificity: crystal RT structure of human very-long-chain acyl-CoA dehydrogenase."; RL J. Biol. Chem. 283:9435-9443(2008). RN [21] RP VARIANTS ACADVLD GLU-130 DEL; LYS-299 DEL; GLN-382 AND TRP-613. RX PubMed=8554073; RA Souri M., Aoyama T., Orii K., Yamaguchi S., Hashimoto T.; RT "Mutation analysis of very-long-chain acyl-coenzyme A dehydrogenase (VLCAD) RT deficiency: identification and characterization of mutant VLCAD cDNAs from RT four patients."; RL Am. J. Hum. Genet. 58:97-106(1996). RN [22] RP VARIANT ACADVLD HIS-450. RX PubMed=9546340; DOI=10.1002/ana.410430422; RA Smelt A.H., Poorthuis B.J.H.M., Onkenhout W., Scholte H.R., Andresen B.S., RA van Duinen S.G., Gregersen N., Wintzen A.R.; RT "Very long chain acyl-coenzyme A dehydrogenase deficiency with adult RT onset."; RL Ann. Neurol. 43:540-544(1998). RN [23] RP VARIANT ACADVLD PRO-490, CHARACTERIZATION OF VARIANT ACADVLD PRO-490, RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, SUBSTRATE SPECIFICITY, AND RP MUTAGENESIS OF ALA-490. RX PubMed=9839948; DOI=10.1046/j.1432-1327.1998.2570592.x; RA Souri M., Aoyama T., Yamaguchi S., Hashimoto T.; RT "Relationship between structure and substrate-chain-length specificity of RT mitochondrial very-long-chain acyl-coenzyme A dehydrogenase."; RL Eur. J. Biochem. 257:592-598(1998). RN [24] RP VARIANT ACADVLD TRP-583, CHARACTERIZATION OF VARIANT ACADVLD TRP-583, RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, SUBUNIT, SUBCELLULAR LOCATION, AND RP TOPOLOGY. RX PubMed=9599005; DOI=10.1016/s0014-5793(98)00343-3; RA Souri M., Aoyama T., Hoganson G., Hashimoto T.; RT "Very-long-chain acyl-CoA dehydrogenase subunit assembles to the dimer form RT on mitochondrial inner membrane."; RL FEBS Lett. 426:187-190(1998). RN [25] RP VARIANTS ACADVLD GLU-130 DEL; PRO-213; GLU-247; MET-260; LYS-278 DEL; RP ALA-283; ASP-441; LEU-458; PRO-490; LYS-534; TRP-613 AND GLN-615. RX PubMed=10077518; DOI=10.1161/01.cir.99.10.1337; RA Mathur A., Sims H.F., Gopalakrishnan D., Gibson B., Rinaldo P., Vockley J., RA Hug G., Strauss A.W.; RT "Molecular heterogeneity in very-long-chain acyl-CoA dehydrogenase RT deficiency causing pediatric cardiomyopathy and sudden death."; RL Circulation 99:1337-1343(1999). CC -!- FUNCTION: Catalyzes the first of the four reactions of the CC mitochondrial fatty acid beta-oxidation (FAO) pathway, which consists CC in the proR-proR stereospecific alpha, beta-dehydrogenation of fatty CC acyl-CoA thioesters using the electron transfer flavoprotein (ETF) as CC their physiologic electron acceptor, resulting in the formation of CC trans-2-enoyl-CoA ((2E)-enoyl-CoA) (PubMed:17564966, PubMed:18227065, CC PubMed:26474213, PubMed:7668252, PubMed:9461620, PubMed:9599005, CC PubMed:9839948). The mitochondrial FAO pathway is the major energy- CC producing process in tissues and is performed through cycles of four CC consecutive reactions (PubMed:26474213, PubMed:7668252). Each FAO cycle CC shortens the fatty acyl-CoA by two carbons, yielding one acetyl-CoA CC (for the citric acid cycle), one FADH(2), and one NADH (which donate CC electrons to the respiratory chain for ATP production) CC (PubMed:26474213, PubMed:7668252). Among the different mitochondrial CC acyl-CoA dehydrogenases, very long-chain specific acyl-CoA CC dehydrogenase acts specifically on fatty acyl-CoAs with saturated 12 to CC 24 carbons long primary chains (PubMed:17564966, PubMed:21237683, CC PubMed:9839948), but can also catalyze monounsaturated fatty acids such CC as oleate ((9Z)-octadecenoate), (9Z)-hexadecenoate, and others CC (PubMed:17564966). Can use (4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate as CC substrate in vitro (which is not primarily used for energy but mainly CC beta-oxidized in the peroxisomes) (PubMed:17564966, PubMed:26474213). CC In addition, based on its established catalytic mechanism, and combined CC genetic interaction or mutant phenotype evidence, it is predicted to CC act also on substrates that have not been tested experimentally but are CC metabolized by mitochondrial FAO, including long-chain unsaturated CC fatty acids such as linoleate (9Z,12Z-octadecadienoate), linolenate CC (9Z,12Z,15Z-octadecatrienoate), and others (PubMed:26474213). Among the CC different mitochondrial acyl-CoA dehydrogenases, its FAO activity CC overlaps with that of ACAD9 and ACADL, but plays a primary role in CC tissues where it is the main long-chain ACAD expressed, such as the CC heart and skeletal muscle (PubMed:17564966). CC {ECO:0000269|PubMed:17564966, ECO:0000269|PubMed:18227065, CC ECO:0000269|PubMed:21237683, ECO:0000269|PubMed:7668252, CC ECO:0000269|PubMed:9461620, ECO:0000269|PubMed:9599005, CC ECO:0000269|PubMed:9839948, ECO:0000303|PubMed:26474213}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a long-chain 2,3-saturated fatty acyl-CoA + oxidized CC [electron-transfer flavoprotein] + H(+) = a long-chain (2E)-enoyl-CoA CC + reduced [electron-transfer flavoprotein]; Xref=Rhea:RHEA:17721, CC Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:83721, CC ChEBI:CHEBI:83727; EC=1.3.8.8; Evidence={ECO:0000269|PubMed:17564966, CC ECO:0000269|PubMed:21237683, ECO:0000269|PubMed:7668252, CC ECO:0000269|PubMed:9461620, ECO:0000269|PubMed:9599005, CC ECO:0000269|PubMed:9839948}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17722; CC Evidence={ECO:0000305|PubMed:17374501}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a very-long-chain 2,3-saturated fatty acyl-CoA + oxidized CC [electron-transfer flavoprotein] + H(+) = a very-long-chain (2E)- CC enoyl-CoA + reduced [electron-transfer flavoprotein]; CC Xref=Rhea:RHEA:19181, Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, CC ChEBI:CHEBI:83724, ChEBI:CHEBI:83728; EC=1.3.8.9; CC Evidence={ECO:0000269|PubMed:21237683}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19182; CC Evidence={ECO:0000305|PubMed:21237683}; CC -!- CATALYTIC ACTIVITY: CC Reaction=tetracosanoyl-CoA + oxidized [electron-transfer flavoprotein] CC + H(+) = (2E)-tetracosenoyl-CoA + reduced [electron-transfer CC flavoprotein]; Xref=Rhea:RHEA:47232, Rhea:RHEA-COMP:10685, Rhea:RHEA- CC COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, CC ChEBI:CHEBI:65052, ChEBI:CHEBI:74693; CC Evidence={ECO:0000269|PubMed:21237683}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47233; CC Evidence={ECO:0000305|PubMed:21237683}; CC -!- CATALYTIC ACTIVITY: CC Reaction=docosanoyl-CoA + oxidized [electron-transfer flavoprotein] + CC H(+) = (2E)-docosenoyl-CoA + reduced [electron-transfer CC flavoprotein]; Xref=Rhea:RHEA:47228, Rhea:RHEA-COMP:10685, Rhea:RHEA- CC COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, CC ChEBI:CHEBI:65059, ChEBI:CHEBI:74692; CC Evidence={ECO:0000269|PubMed:21237683}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47229; CC Evidence={ECO:0000305|PubMed:21237683}; CC -!- CATALYTIC ACTIVITY: CC Reaction=eicosanoyl-CoA + oxidized [electron-transfer flavoprotein] + CC H(+) = (2E)-eicosenoyl-CoA + reduced [electron-transfer CC flavoprotein]; Xref=Rhea:RHEA:47236, Rhea:RHEA-COMP:10685, Rhea:RHEA- CC COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57380, ChEBI:CHEBI:57692, CC ChEBI:CHEBI:58307, ChEBI:CHEBI:74691; CC Evidence={ECO:0000269|PubMed:21237683}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47237; CC Evidence={ECO:0000305|PubMed:21237683}; CC -!- CATALYTIC ACTIVITY: CC Reaction=octadecanoyl-CoA + oxidized [electron-transfer flavoprotein] + CC H(+) = (2E)-octadecenoyl-CoA + reduced [electron-transfer CC flavoprotein]; Xref=Rhea:RHEA:47240, Rhea:RHEA-COMP:10685, Rhea:RHEA- CC COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57394, ChEBI:CHEBI:57692, CC ChEBI:CHEBI:58307, ChEBI:CHEBI:71412; CC Evidence={ECO:0000269|PubMed:17564966, ECO:0000269|PubMed:21237683, CC ECO:0000269|PubMed:9839948}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47241; CC Evidence={ECO:0000269|PubMed:9839948}; CC -!- CATALYTIC ACTIVITY: CC Reaction=oxidized [electron-transfer flavoprotein] + hexadecanoyl-CoA + CC H(+) = (2E)-hexadecenoyl-CoA + reduced [electron-transfer CC flavoprotein]; Xref=Rhea:RHEA:43448, Rhea:RHEA-COMP:10685, Rhea:RHEA- CC COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57379, ChEBI:CHEBI:57692, CC ChEBI:CHEBI:58307, ChEBI:CHEBI:61526; CC Evidence={ECO:0000269|PubMed:21237683, ECO:0000269|PubMed:7668252, CC ECO:0000269|PubMed:9461620, ECO:0000269|PubMed:9599005, CC ECO:0000269|PubMed:9839948}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43449; CC Evidence={ECO:0000269|PubMed:7668252}; CC -!- CATALYTIC ACTIVITY: CC Reaction=tetradecanoyl-CoA + oxidized [electron-transfer flavoprotein] CC + H(+) = (2E)-tetradecenoyl-CoA + reduced [electron-transfer CC flavoprotein]; Xref=Rhea:RHEA:47316, Rhea:RHEA-COMP:10685, Rhea:RHEA- CC COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57385, ChEBI:CHEBI:57692, CC ChEBI:CHEBI:58307, ChEBI:CHEBI:61405; CC Evidence={ECO:0000269|PubMed:21237683, ECO:0000269|PubMed:9839948}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47317; CC Evidence={ECO:0000269|PubMed:9839948}; CC -!- CATALYTIC ACTIVITY: CC Reaction=dodecanoyl-CoA + oxidized [electron-transfer flavoprotein] + CC H(+) = (2E)-dodecenoyl-CoA + reduced [electron-transfer CC flavoprotein]; Xref=Rhea:RHEA:47296, Rhea:RHEA-COMP:10685, Rhea:RHEA- CC COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57330, ChEBI:CHEBI:57375, CC ChEBI:CHEBI:57692, ChEBI:CHEBI:58307; CC Evidence={ECO:0000269|PubMed:21237683, ECO:0000269|PubMed:9839948}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47297; CC Evidence={ECO:0000269|PubMed:9839948}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(13Z)-docosenoyl-CoA + oxidized [electron-transfer CC flavoprotein] + H(+) = (2E,13Z)-docosadienoyl-CoA + reduced CC [electron-transfer flavoprotein]; Xref=Rhea:RHEA:83051, Rhea:RHEA- CC COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:74068, CC ChEBI:CHEBI:76391; Evidence={ECO:0000305|PubMed:17564966}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:83052; CC Evidence={ECO:0000305|PubMed:17564966}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(11Z)-eicosenoyl-CoA + oxidized [electron-transfer CC flavoprotein] + H(+) = (2E,11Z)-eicosadienoyl-CoA + reduced CC [electron-transfer flavoprotein]; Xref=Rhea:RHEA:83055, Rhea:RHEA- CC COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:74069, CC ChEBI:CHEBI:76388; Evidence={ECO:0000305|PubMed:17564966}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:83056; CC Evidence={ECO:0000305|PubMed:17564966}; CC -!- CATALYTIC ACTIVITY: CC Reaction=oxidized [electron-transfer flavoprotein] + (9Z)-octadecenoyl- CC CoA + H(+) = (2E,9Z)-octadecadienoyl-CoA + reduced [electron-transfer CC flavoprotein]; Xref=Rhea:RHEA:47300, Rhea:RHEA-COMP:10685, Rhea:RHEA- CC COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57387, ChEBI:CHEBI:57692, CC ChEBI:CHEBI:58307, ChEBI:CHEBI:77553; CC Evidence={ECO:0000269|PubMed:17564966}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47301; CC Evidence={ECO:0000305|PubMed:17564966}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(7Z)-hexadecenoyl-CoA + oxidized [electron-transfer CC flavoprotein] + H(+) = (2E,7Z)-hexadecadienoyl-CoA + reduced CC [electron-transfer flavoprotein]; Xref=Rhea:RHEA:47432, Rhea:RHEA- CC COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:87698, CC ChEBI:CHEBI:87717; Evidence={ECO:0000305|PubMed:17564966}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47433; CC Evidence={ECO:0000305|PubMed:17564966}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(5Z)-tetradecenoyl-CoA + oxidized [electron-transfer CC flavoprotein] + H(+) = (2E,5Z)-tetradecadienoyl-CoA + reduced CC [electron-transfer flavoprotein]; Xref=Rhea:RHEA:47448, Rhea:RHEA- CC COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:84650, CC ChEBI:CHEBI:87701; Evidence={ECO:0000305|PubMed:17564966}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47449; CC Evidence={ECO:0000305|PubMed:17564966}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(11Z)-octadecenoyl-CoA + oxidized [electron-transfer CC flavoprotein] + H(+) = (2E,11Z)-octadecadienoyl-CoA + reduced CC [electron-transfer flavoprotein]; Xref=Rhea:RHEA:83023, Rhea:RHEA- CC COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:75121, CC ChEBI:CHEBI:76558; Evidence={ECO:0000305|PubMed:17564966}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:83024; CC Evidence={ECO:0000305|PubMed:17564966}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(9Z)-hexadecenoyl-CoA + oxidized [electron-transfer CC flavoprotein] + H(+) = (2E,9Z)-hexadecadienoyl-CoA + reduced CC [electron-transfer flavoprotein]; Xref=Rhea:RHEA:47304, Rhea:RHEA- CC COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:61540, CC ChEBI:CHEBI:77549; Evidence={ECO:0000269|PubMed:17564966}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47305; CC Evidence={ECO:0000305|PubMed:17564966}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(7Z)-tetradecenoyl-CoA + oxidized [electron-transfer CC flavoprotein] + H(+) = (2E,7Z)-tetradecadienoyl-CoA + reduced CC [electron-transfer flavoprotein]; Xref=Rhea:RHEA:82939, Rhea:RHEA- CC COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:232643, CC ChEBI:CHEBI:232680; Evidence={ECO:0000305|PubMed:17564966}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:82940; CC Evidence={ECO:0000305|PubMed:17564966}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(5Z)-dodecenoyl-CoA + oxidized [electron-transfer CC flavoprotein] + H(+) = (2E,5Z)-dodecadienoyl-CoA + reduced [electron- CC transfer flavoprotein]; Xref=Rhea:RHEA:82951, Rhea:RHEA-COMP:10685, CC Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692, CC ChEBI:CHEBI:58307, ChEBI:CHEBI:230464, ChEBI:CHEBI:232684; CC Evidence={ECO:0000305|PubMed:17564966}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:82952; CC Evidence={ECO:0000305|PubMed:17564966}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(6Z)-hexadecenoyl-CoA + oxidized [electron-transfer CC flavoprotein] + H(+) = (2E,6Z)-hexadecadienoyl-CoA + reduced CC [electron-transfer flavoprotein]; Xref=Rhea:RHEA:83155, Rhea:RHEA- CC COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:74339, CC ChEBI:CHEBI:232761; Evidence={ECO:0000305|PubMed:17564966}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:83156; CC Evidence={ECO:0000305|PubMed:17564966}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(4Z)-tetradecenoyl-CoA + oxidized [electron-transfer CC flavoprotein] + H(+) = (2E,4Z)-tetradecadienoyl-CoA + reduced CC [electron-transfer flavoprotein]; Xref=Rhea:RHEA:83159, Rhea:RHEA- CC COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:232764, CC ChEBI:CHEBI:232765; Evidence={ECO:0000305|PubMed:17564966}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:83160; CC Evidence={ECO:0000305|PubMed:17564966}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(6Z)-octadecenoyl-CoA + oxidized [electron-transfer CC flavoprotein] + H(+) = (2E,6Z)-octadecadienoyl-CoA + reduced CC [electron-transfer flavoprotein]; Xref=Rhea:RHEA:83207, Rhea:RHEA- CC COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:75123, CC ChEBI:CHEBI:232772; Evidence={ECO:0000305|PubMed:17564966}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:83208; CC Evidence={ECO:0000305|PubMed:17564966}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(4Z)-hexadecenoyl-CoA + oxidized [electron-transfer CC flavoprotein] + H(+) = (2E,4Z)-hexadecadienoyl-CoA + reduced CC [electron-transfer flavoprotein]; Xref=Rhea:RHEA:83223, Rhea:RHEA- CC COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:232775, CC ChEBI:CHEBI:232776; Evidence={ECO:0000305|PubMed:17564966}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:83224; CC Evidence={ECO:0000305|PubMed:17564966}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(11Z)-docosenoyl-CoA(4-) + oxidized [electron-transfer CC flavoprotein] + H(+) = (2E,11Z)-docosadienoyl-CoA + reduced CC [electron-transfer flavoprotein]; Xref=Rhea:RHEA:83291, Rhea:RHEA- CC COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:232625, CC ChEBI:CHEBI:232888; Evidence={ECO:0000305|PubMed:17564966}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:83292; CC Evidence={ECO:0000305|PubMed:17564966}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(9Z)-eicosenoyl-CoA + oxidized [electron-transfer CC flavoprotein] + H(+) = (2E,9Z)-eicosadienoyl-CoA + reduced [electron- CC transfer flavoprotein]; Xref=Rhea:RHEA:83335, Rhea:RHEA-COMP:10685, CC Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692, CC ChEBI:CHEBI:58307, ChEBI:CHEBI:232891, ChEBI:CHEBI:232892; CC Evidence={ECO:0000305|PubMed:17564966}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:83336; CC Evidence={ECO:0000305|PubMed:17564966}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(7Z)-octadecenoyl-CoA + oxidized [electron-transfer CC flavoprotein] + H(+) = (2E,7Z)-octadecadienoyl-CoA + reduced CC [electron-transfer flavoprotein]; Xref=Rhea:RHEA:83371, Rhea:RHEA- CC COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:152050, CC ChEBI:CHEBI:232899; Evidence={ECO:0000305|PubMed:17564966}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:83372; CC Evidence={ECO:0000305|PubMed:17564966}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(5Z)-hexadecenoyl-CoA + oxidized [electron-transfer CC flavoprotein] + H(+) = (2E,5Z)-hexadecadienoyl-CoA + reduced CC [electron-transfer flavoprotein]; Xref=Rhea:RHEA:83387, Rhea:RHEA- CC COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:232908, CC ChEBI:CHEBI:232910; Evidence={ECO:0000305|PubMed:17564966}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:83388; CC Evidence={ECO:0000305|PubMed:17564966}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(9Z,12Z)-octadecadienoyl-CoA + oxidized [electron-transfer CC flavoprotein] + H(+) = (2E,9Z,12Z)-octadecatrienoyl-CoA + reduced CC [electron-transfer flavoprotein]; Xref=Rhea:RHEA:48188, Rhea:RHEA- CC COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:57383, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, CC ChEBI:CHEBI:77558; Evidence={ECO:0000305|PubMed:17564966}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48189; CC Evidence={ECO:0000305|PubMed:17564966}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(7Z,10Z)-hexadecadienoyl-CoA + oxidized [electron-transfer CC flavoprotein] + H(+) = (2E,7Z,10Z)-hexadecatrienoyl-CoA + reduced CC [electron-transfer flavoprotein]; Xref=Rhea:RHEA:84463, Rhea:RHEA- CC COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:233785, CC ChEBI:CHEBI:233825; Evidence={ECO:0000305|PubMed:17564966}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:84464; CC Evidence={ECO:0000305|PubMed:17564966}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(5Z,8Z)-tetradecadienoyl-CoA + oxidized [electron-transfer CC flavoprotein] + H(+) = (2E,5Z,8Z)-tetradecatrienoyl-CoA + reduced CC [electron-transfer flavoprotein]; Xref=Rhea:RHEA:84467, Rhea:RHEA- CC COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:233789, CC ChEBI:CHEBI:233827; Evidence={ECO:0000305|PubMed:17564966}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:84468; CC Evidence={ECO:0000305|PubMed:17564966}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(6Z)-dodecenoyl-CoA + oxidized [electron-transfer CC flavoprotein] + H(+) = (2E,6Z)-dodecadienoyl-CoA + reduced [electron- CC transfer flavoprotein]; Xref=Rhea:RHEA:84471, Rhea:RHEA-COMP:10685, CC Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692, CC ChEBI:CHEBI:58307, ChEBI:CHEBI:233834, ChEBI:CHEBI:233835; CC Evidence={ECO:0000305|PubMed:17564966}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:84472; CC Evidence={ECO:0000305|PubMed:17564966}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(4Z)-decenoyl-CoA(4-) + oxidized [electron-transfer CC flavoprotein] + H(+) = (2E,4Z)-decadienoyl-CoA + reduced [electron- CC transfer flavoprotein]; Xref=Rhea:RHEA:84475, Rhea:RHEA-COMP:10685, CC Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692, CC ChEBI:CHEBI:58307, ChEBI:CHEBI:137593, ChEBI:CHEBI:233838; CC Evidence={ECO:0000305|PubMed:17564966}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:84476; CC Evidence={ECO:0000305|PubMed:17564966}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(9Z,12Z,15Z)-octadecatrienoyl-CoA + oxidized [electron- CC transfer flavoprotein] + H(+) = (2E,9Z,12Z,15Z)-octadecatetraenoyl- CC CoA + reduced [electron-transfer flavoprotein]; Xref=Rhea:RHEA:84595, CC Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:74034, CC ChEBI:CHEBI:233840; Evidence={ECO:0000305|PubMed:17564966}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:84596; CC Evidence={ECO:0000305|PubMed:17564966}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(7Z,10Z,13Z)-hexadecatrienoyl-CoA + oxidized [electron- CC transfer flavoprotein] + H(+) = (2E,7Z,10Z,13Z)-hexadecatetraenoyl- CC CoA + reduced [electron-transfer flavoprotein]; Xref=Rhea:RHEA:84599, CC Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:177091, CC ChEBI:CHEBI:233792; Evidence={ECO:0000305|PubMed:17564966}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:84600; CC Evidence={ECO:0000305|PubMed:17564966}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(5Z,8Z,11Z)-tetradecatrienoyl-CoA + oxidized [electron- CC transfer flavoprotein] + H(+) = (2E,5Z,8Z,11Z)-tetradecatetraenoyl- CC CoA + reduced [electron-transfer flavoprotein]; Xref=Rhea:RHEA:84603, CC Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:233795, CC ChEBI:CHEBI:233796; Evidence={ECO:0000305|PubMed:17564966}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:84604; CC Evidence={ECO:0000305|PubMed:17564966}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(6Z,9Z)-dodecadienoyl-CoA + oxidized [electron-transfer CC flavoprotein] + H(+) = (2E,6Z,9Z)-dodecatrienoyl-CoA + reduced CC [electron-transfer flavoprotein]; Xref=Rhea:RHEA:84607, Rhea:RHEA- CC COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:233810, CC ChEBI:CHEBI:233847; Evidence={ECO:0000305|PubMed:17564966}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:84608; CC Evidence={ECO:0000305|PubMed:17564966}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(4Z,7Z)-decadienoyl-CoA + oxidized [electron-transfer CC flavoprotein] + H(+) = (2E,4Z,7Z)-decatrienoyl-CoA + reduced CC [electron-transfer flavoprotein]; Xref=Rhea:RHEA:84611, Rhea:RHEA- CC COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:233850, CC ChEBI:CHEBI:233851; Evidence={ECO:0000305|PubMed:17564966}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:84612; CC Evidence={ECO:0000305|PubMed:17564966}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(6Z,9Z,12Z)-octadecatrienoyl-CoA + oxidized [electron-transfer CC flavoprotein] + H(+) = (2E,6Z,9Z,12Z)-octadecatetraenoyl-CoA + CC reduced [electron-transfer flavoprotein]; Xref=Rhea:RHEA:84619, CC Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:57363, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, CC ChEBI:CHEBI:233778; Evidence={ECO:0000305|PubMed:17564966}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:84620; CC Evidence={ECO:0000305|PubMed:17564966}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(4Z,7Z,10Z)-hexadecatrienoyl-CoA + oxidized [electron-transfer CC flavoprotein] + H(+) = (2E,4Z,7Z,10Z)-hexadecatetraenoyl-CoA + CC reduced [electron-transfer flavoprotein]; Xref=Rhea:RHEA:84623, CC Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:233781, CC ChEBI:CHEBI:233783; Evidence={ECO:0000305|PubMed:17564966}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:84624; CC Evidence={ECO:0000305|PubMed:17564966}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(6Z,9Z,12Z,15Z)-octadecatetraenoyl-CoA + oxidized [electron- CC transfer flavoprotein] + H(+) = (2E,6Z,9Z,12Z,15Z)- CC octadecapentaenoyl-CoA + reduced [electron-transfer flavoprotein]; CC Xref=Rhea:RHEA:85107, Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, CC ChEBI:CHEBI:71489, ChEBI:CHEBI:233740; CC Evidence={ECO:0000305|PubMed:17564966}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:85108; CC Evidence={ECO:0000305|PubMed:17564966}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(4Z,7Z,10Z,13Z)-hexadecatetraenoyl-CoA + oxidized [electron- CC transfer flavoprotein] + H(+) = (2E,4Z,7Z,10Z,13Z)- CC hexadecapentaenoyl-CoA + reduced [electron-transfer flavoprotein]; CC Xref=Rhea:RHEA:85123, Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, CC ChEBI:CHEBI:233765, ChEBI:CHEBI:233790; CC Evidence={ECO:0000305|PubMed:17564966}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:85124; CC Evidence={ECO:0000305|PubMed:17564966}; CC -!- CATALYTIC ACTIVITY: [Isoform 2]: CC Reaction=a long-chain 2,3-saturated fatty acyl-CoA + oxidized CC [electron-transfer flavoprotein] + H(+) = a long-chain (2E)-enoyl-CoA CC + reduced [electron-transfer flavoprotein]; Xref=Rhea:RHEA:17721, CC Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:83721, CC ChEBI:CHEBI:83727; EC=1.3.8.8; CC Evidence={ECO:0000269|PubMed:17374501}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17722; CC Evidence={ECO:0000305|PubMed:17374501}; CC -!- CATALYTIC ACTIVITY: [Isoform 2]: CC Reaction=eicosanoyl-CoA + oxidized [electron-transfer flavoprotein] + CC H(+) = (2E)-eicosenoyl-CoA + reduced [electron-transfer CC flavoprotein]; Xref=Rhea:RHEA:47236, Rhea:RHEA-COMP:10685, Rhea:RHEA- CC COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57380, ChEBI:CHEBI:57692, CC ChEBI:CHEBI:58307, ChEBI:CHEBI:74691; CC Evidence={ECO:0000269|PubMed:17374501}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47237; CC Evidence={ECO:0000305|PubMed:17374501}; CC -!- CATALYTIC ACTIVITY: [Isoform 2]: CC Reaction=octadecanoyl-CoA + oxidized [electron-transfer flavoprotein] + CC H(+) = (2E)-octadecenoyl-CoA + reduced [electron-transfer CC flavoprotein]; Xref=Rhea:RHEA:47240, Rhea:RHEA-COMP:10685, Rhea:RHEA- CC COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57394, ChEBI:CHEBI:57692, CC ChEBI:CHEBI:58307, ChEBI:CHEBI:71412; CC Evidence={ECO:0000269|PubMed:17374501}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47241; CC Evidence={ECO:0000305|PubMed:17374501}; CC -!- CATALYTIC ACTIVITY: [Isoform 2]: CC Reaction=oxidized [electron-transfer flavoprotein] + hexadecanoyl-CoA + CC H(+) = (2E)-hexadecenoyl-CoA + reduced [electron-transfer CC flavoprotein]; Xref=Rhea:RHEA:43448, Rhea:RHEA-COMP:10685, Rhea:RHEA- CC COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57379, ChEBI:CHEBI:57692, CC ChEBI:CHEBI:58307, ChEBI:CHEBI:61526; CC Evidence={ECO:0000269|PubMed:17374501}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43449; CC Evidence={ECO:0000305|PubMed:17374501}; CC -!- CATALYTIC ACTIVITY: [Isoform 2]: CC Reaction=tetradecanoyl-CoA + oxidized [electron-transfer flavoprotein] CC + H(+) = (2E)-tetradecenoyl-CoA + reduced [electron-transfer CC flavoprotein]; Xref=Rhea:RHEA:47316, Rhea:RHEA-COMP:10685, Rhea:RHEA- CC COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57385, ChEBI:CHEBI:57692, CC ChEBI:CHEBI:58307, ChEBI:CHEBI:61405; CC Evidence={ECO:0000269|PubMed:17374501}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47317; CC Evidence={ECO:0000305|PubMed:17374501}; CC -!- CATALYTIC ACTIVITY: [Isoform 2]: CC Reaction=oxidized [electron-transfer flavoprotein] + (9Z)-octadecenoyl- CC CoA + H(+) = (2E,9Z)-octadecadienoyl-CoA + reduced [electron-transfer CC flavoprotein]; Xref=Rhea:RHEA:47300, Rhea:RHEA-COMP:10685, Rhea:RHEA- CC COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57387, ChEBI:CHEBI:57692, CC ChEBI:CHEBI:58307, ChEBI:CHEBI:77553; CC Evidence={ECO:0000269|PubMed:17374501}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47301; CC Evidence={ECO:0000305|PubMed:17374501}; CC -!- CATALYTIC ACTIVITY: [Isoform 2]: CC Reaction=(9Z)-hexadecenoyl-CoA + oxidized [electron-transfer CC flavoprotein] + H(+) = (2E,9Z)-hexadecadienoyl-CoA + reduced CC [electron-transfer flavoprotein]; Xref=Rhea:RHEA:47304, Rhea:RHEA- CC COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:61540, CC ChEBI:CHEBI:77549; Evidence={ECO:0000269|PubMed:17374501}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47305; CC Evidence={ECO:0000305|PubMed:17374501}; CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000269|PubMed:18227065, ECO:0000269|PubMed:9461620}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=4.4 uM for hexadecanoyl-CoA {ECO:0000269|PubMed:9461620}; CC -!- PATHWAY: Lipid metabolism; mitochondrial fatty acid beta-oxidation. CC {ECO:0000269|PubMed:7668252, ECO:0000269|PubMed:9599005, CC ECO:0000269|PubMed:9839948}. CC -!- SUBUNIT: Homodimer (PubMed:17374501, PubMed:18227065, PubMed:9461620, CC PubMed:9599005). Homodimerizes after import into the mitochondrion CC (PubMed:9599005). {ECO:0000269|PubMed:17374501, CC ECO:0000269|PubMed:18227065, ECO:0000269|PubMed:9461620, CC ECO:0000269|PubMed:9599005}. CC -!- INTERACTION: CC P49748; Q53T94: TAF1B; NbExp=3; IntAct=EBI-727618, EBI-1560239; CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane CC {ECO:0000269|PubMed:9461620, ECO:0000269|PubMed:9599005}; Peripheral CC membrane protein {ECO:0000269|PubMed:9599005}. CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Mitochondrion inner membrane CC {ECO:0000269|PubMed:17374501}; Peripheral membrane protein CC {ECO:0000269|PubMed:17374501}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=P49748-1; Sequence=Displayed; CC Name=2; Synonyms=DeltaEx3 VLCAD {ECO:0000303|PubMed:17374501}; CC IsoId=P49748-2; Sequence=VSP_007734; CC Name=3; CC IsoId=P49748-3; Sequence=VSP_046031; CC -!- TISSUE SPECIFICITY: Predominantly expressed in heart and skeletal CC muscle (at both mRNA and protein levels) (PubMed:17564966, CC PubMed:8845838). Also detected in kidney and liver (at protein level) CC (PubMed:8845838). {ECO:0000269|PubMed:17564966, CC ECO:0000269|PubMed:8845838}. CC -!- PTM: S-nitrosylation at Cys-237 in liver improves catalytic efficiency. CC {ECO:0000250|UniProtKB:P50544}. CC -!- DISEASE: Acyl-CoA dehydrogenase very long-chain deficiency (ACADVLD) CC [MIM:201475]: An inborn error of mitochondrial fatty acid beta- CC oxidation which leads to impaired long-chain fatty acid beta-oxidation. CC It is clinically heterogeneous, with three major phenotypes: a severe CC childhood form characterized by early onset, high mortality and high CC incidence of cardiomyopathy; a milder childhood form with later onset, CC characterized by hypoketotic hypoglycemia, low mortality and rare CC cardiomyopathy; an adult form, with isolated skeletal muscle CC involvement, rhabdomyolysis and myoglobinuria, usually triggered by CC exercise or fasting. {ECO:0000269|PubMed:10077518, CC ECO:0000269|PubMed:17374501, ECO:0000269|PubMed:7668252, CC ECO:0000269|PubMed:8554073, ECO:0000269|PubMed:8845838, CC ECO:0000269|PubMed:9461620, ECO:0000269|PubMed:9546340, CC ECO:0000269|PubMed:9599005, ECO:0000269|PubMed:9839948, CC ECO:0000269|PubMed:9973285}. 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 -!- CAUTION: Some reactions in this entry are inferred from combined CC genetic interaction or mutant phenotype evidence and direct CC experimental evidence in parent reaction. {ECO:0000303|PubMed:26474213, CC ECO:0000305|PubMed:17564966}. 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; D43682; BAA07781.1; -; mRNA. DR EMBL; L46590; AAA79002.1; -; Genomic_DNA. DR EMBL; X86556; CAA60253.1; -; mRNA. DR EMBL; D78298; BAA29057.1; -; Genomic_DNA. DR EMBL; AK293549; BAG57027.1; -; mRNA. DR EMBL; AC120057; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC000399; AAH00399.1; -; mRNA. DR EMBL; BC012912; AAH12912.1; -; mRNA. DR EMBL; BC020218; AAH20218.1; -; mRNA. DR CCDS; CCDS11090.1; -. [P49748-1] DR CCDS; CCDS42249.1; -. [P49748-2] DR CCDS; CCDS58509.1; -. [P49748-3] DR PIR; S54183; S54183. DR RefSeq; NP_000009.1; NM_000018.4. [P49748-1] DR RefSeq; NP_001029031.1; NM_001033859.3. [P49748-2] DR RefSeq; NP_001257376.1; NM_001270447.2. [P49748-3] DR PDB; 2UXW; X-ray; 1.45 A; A=69-655. DR PDB; 3B96; X-ray; 1.91 A; A=69-655. DR PDB; 7S7G; X-ray; 1.34 A; A=69-655. DR AlphaFoldDB; P49748; -. DR SASBDB; P49748; -. DR SMR; P49748; -. DR BioGRID; 106555; 159. DR FunCoup; P49748; 1596. DR IntAct; P49748; 76. DR MINT; P49748; -. DR NDEx; IQUERY-CP-ACADVL; 5 NDEx IQuery Curated Pathways. DR STRING; 9606.ENSP00000438689; -. DR BindingDB; P49748; -. DR ChEMBL; CHEMBL4105892; -. DR SwissLipids; SLP:000001330; -. [P49748-2] DR SwissLipids; SLP:000001332; -. DR CarbonylDB; P49748; -. DR GlyGen; P49748; 3 sites, 1 O-linked glycan (3 sites). DR iPTMnet; P49748; -. DR PhosphoSitePlus; P49748; -. DR SwissPalm; P49748; -. DR BioMuta; ACADVL; -. DR DMDM; 1703068; -. DR CPTAC; CPTAC-454; -. DR CPTAC; CPTAC-455; -. DR jPOST; P49748; -. DR MassIVE; P49748; -. DR PaxDb; 9606-ENSP00000438689; -. DR PeptideAtlas; P49748; -. DR ProteomicsDB; 25916; -. DR ProteomicsDB; 56061; -. [P49748-1] DR ProteomicsDB; 56062; -. [P49748-2] DR Pumba; P49748; -. DR Antibodypedia; 11798; 299 antibodies from 35 providers. DR DNASU; 37; -. DR Ensembl; ENST00000350303.9; ENSP00000344152.5; ENSG00000072778.21. [P49748-2] DR Ensembl; ENST00000356839.10; ENSP00000349297.5; ENSG00000072778.21. [P49748-1] DR Ensembl; ENST00000543245.6; ENSP00000438689.2; ENSG00000072778.21. [P49748-3] DR GeneID; 37; -. DR KEGG; hsa:37; -. DR MANE-Select; ENST00000356839.10; ENSP00000349297.5; NM_000018.4; NP_000009.1. DR UCSC; uc002gev.5; human. [P49748-1] DR AGR; HGNC:92; -. DR ClinPGx; PA24428; -. DR CTD; 37; -. DR DisGeNET; 37; -. DR GeneCards; ACADVL; -. DR GeneReviews; ACADVL; -. DR HGNC; HGNC:92; ACADVL. DR HPA; ENSG00000072778; Low tissue specificity. DR MalaCards; ACADVL; -. DR MIM; 201475; phenotype. DR MIM; 609575; gene. DR OpenTargets; ENSG00000072778; -. DR Orphanet; 26793; Very long chain acyl-CoA dehydrogenase deficiency. DR VEuPathDB; HostDB:ENSG00000072778; -. DR eggNOG; KOG0137; Eukaryota. DR GeneTree; ENSGT00940000158535; -. DR HOGENOM; CLU_018204_11_2_1; -. DR InParanoid; P49748; -. DR OMA; NAFMGLR; -. DR OrthoDB; 2588832at2759; -. DR PAN-GO; P49748; 2 GO annotations based on evolutionary models. DR PhylomeDB; P49748; -. DR BioCyc; MetaCyc:ENSG00000072778-MONOMER; -. DR BRENDA; 1.3.8.8; 2681. DR BRENDA; 1.3.8.9; 2681. DR PathwayCommons; P49748; -. DR Reactome; R-HSA-381038; XBP1(S) activates chaperone genes. DR Reactome; R-HSA-77305; Beta oxidation of palmitoyl-CoA to myristoyl-CoA. DR SignaLink; P49748; -. DR SIGNOR; P49748; -. DR UniPathway; UPA00660; -. DR Agora; ENSG00000072778; -. DR BioGRID-ORCS; 37; 9 hits in 1156 CRISPR screens. DR ChiTaRS; ACADVL; human. DR EvolutionaryTrace; P49748; -. DR GenomeRNAi; 37; -. DR Pharos; P49748; Tbio. DR PRO; PR:P49748; -. DR Proteomes; UP000005640; Chromosome 17. DR RNAct; P49748; protein. DR Bgee; ENSG00000072778; Expressed in right adrenal gland cortex and 203 other cell types or tissues. DR ExpressionAtlas; P49748; baseline and differential. DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome. DR GO; GO:0031966; C:mitochondrial membrane; IDA:BHF-UCL. DR GO; GO:0042645; C:mitochondrial nucleoid; IDA:BHF-UCL. DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB. DR GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IMP:UniProtKB. DR GO; GO:0000062; F:fatty-acyl-CoA binding; IBA:GO_Central. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IDA:UniProtKB. DR GO; GO:0042802; F:identical protein binding; IDA:UniProtKB. DR GO; GO:0004466; F:long-chain fatty acyl-CoA dehydrogenase activity; IDA:BHF-UCL. DR GO; GO:0070991; F:medium-chain fatty acyl-CoA dehydrogenase activity; IEA:RHEA. DR GO; GO:0017099; F:very-long-chain fatty acyl-CoA dehydrogenase activity; IDA:UniProtKB. DR GO; GO:0015980; P:energy derivation by oxidation of organic compounds; TAS:ProtInc. DR GO; GO:0030855; P:epithelial cell differentiation; IEP:UniProtKB. DR GO; GO:0033539; P:fatty acid beta-oxidation using acyl-CoA dehydrogenase; IDA:BHF-UCL. DR GO; GO:0045717; P:negative regulation of fatty acid biosynthetic process; ISS:BHF-UCL. DR GO; GO:0046322; P:negative regulation of fatty acid oxidation; ISS:BHF-UCL. DR GO; GO:0090181; P:regulation of cholesterol metabolic process; ISS:BHF-UCL. DR GO; GO:0001659; P:temperature homeostasis; ISS:BHF-UCL. DR CDD; cd01161; VLCAD; 1. DR DisProt; DP04188; -. DR FunFam; 1.20.140.10:FF:000008; acyl-CoA dehydrogenase family member 9, mitochondrial; 1. DR FunFam; 1.20.140.10:FF:000017; very long-chain specific acyl-CoA dehydrogenase, mitochondrial; 1. DR FunFam; 2.40.110.10:FF:000006; very long-chain specific acyl-CoA dehydrogenase, mitochondrial; 1. DR FunFam; 1.10.540.10:FF:000001; Very long-chain-specific acyl-CoA dehydrogenase, mitochondrial; 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; 2. DR InterPro; IPR049448; ACAD9/ACADV-like_C. DR InterPro; IPR006089; Acyl-CoA_DH_CS. 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; IPR006091; AcylCoA_DH/ox_M. 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:SF11; VERY LONG-CHAIN SPECIFIC ACYL-COA DEHYDROGENASE, MITOCHONDRIAL; 1. DR Pfam; PF21343; ACAD9-ACADV_C; 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 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 PDBsum; 2UXW; -. DR PDBsum; 3B96; -. DR PDBsum; 7S7G; -. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Cardiomyopathy; KW Direct protein sequencing; Disease variant; FAD; Fatty acid metabolism; KW Flavoprotein; Lipid metabolism; Membrane; Mitochondrion; KW Mitochondrion inner membrane; Oxidoreductase; Phosphoprotein; KW Proteomics identification; Reference proteome; S-nitrosylation; KW Transit peptide. FT TRANSIT 1..40 FT /note="Mitochondrion" FT /evidence="ECO:0000269|PubMed:7668252, FT ECO:0007744|PubMed:25944712" FT CHAIN 41..655 FT /note="Very long-chain acyl-CoA dehydrogenase, FT mitochondrial" FT /id="PRO_0000000515" FT REGION 23..42 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 41..482 FT /note="Catalytic" FT /evidence="ECO:0000305|PubMed:18227065" FT REGION 483..516 FT /note="Membrane-anchoring" FT /evidence="ECO:0000305|PubMed:18227065" FT ACT_SITE 462 FT /note="Proton acceptor" FT /evidence="ECO:0000269|PubMed:18227065, FT ECO:0000269|PubMed:9461620, ECO:0007744|PDB:2UXW, FT ECO:0007744|PDB:3B96" FT BINDING 214..223 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000269|PubMed:18227065, FT ECO:0007744|PDB:2UXW, ECO:0007744|PDB:3B96" FT BINDING 249..251 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000269|PubMed:18227065, FT ECO:0007744|PDB:2UXW, ECO:0007744|PDB:3B96" FT BINDING 461..463 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:18227065, FT ECO:0007744|PDB:2UXW, ECO:0007744|PDB:3B96" FT BINDING 464..466 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000269|PubMed:18227065, FT ECO:0007744|PDB:2UXW, ECO:0007744|PDB:3B96" FT BINDING 562 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000269|PubMed:18227065, FT ECO:0007744|PDB:2UXW, ECO:0007744|PDB:3B96" FT MOD_RES 51 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P50544" FT MOD_RES 71 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P50544" FT MOD_RES 71 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P50544" FT MOD_RES 195 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:P50544" FT MOD_RES 237 FT /note="S-nitrosocysteine" FT /evidence="ECO:0000250|UniProtKB:P50544" FT MOD_RES 239 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 239 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P50544" FT MOD_RES 276 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P50544" FT MOD_RES 276 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P50544" FT MOD_RES 278 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P50544" FT MOD_RES 278 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P50544" FT MOD_RES 298 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P50544" FT MOD_RES 331 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 331 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P50544" FT MOD_RES 372 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:P50544" FT MOD_RES 482 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P50544" FT MOD_RES 482 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P50544" FT MOD_RES 517 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 522 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 550 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P50544" FT MOD_RES 556 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P50544" FT MOD_RES 556 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P50544" FT MOD_RES 639 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:P50544" FT VAR_SEQ 1..20 FT /note="MQAARMAASLGRQLLRLGGG -> MLGGLAAAAGTRIMGKEIEAEAQRPLRQ FT TWRPGQPPAMTAKTM (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_046031" FT VAR_SEQ 47..68 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_007734" FT VARIANT 17 FT /note="L -> F (in dbSNP:rs2230179)" FT /id="VAR_029286" FT VARIANT 43 FT /note="G -> D (in ACADVLD; benign; dbSNP:rs2230178)" FT /evidence="ECO:0000269|PubMed:9973285" FT /id="VAR_000330" FT VARIANT 65 FT /note="P -> L (in dbSNP:rs28934585)" FT /id="VAR_048176" FT VARIANT 130 FT /note="Missing (in ACADVLD; dbSNP:rs387906251)" FT /evidence="ECO:0000269|PubMed:10077518, FT ECO:0000269|PubMed:8554073" FT /id="VAR_000331" FT VARIANT 158 FT /note="T -> N (in ACADVLD)" FT /evidence="ECO:0000269|PubMed:9973285" FT /id="VAR_000332" FT VARIANT 159 FT /note="Q -> R (in ACADVLD; uncertain significance; FT dbSNP:rs746688190)" FT /evidence="ECO:0000269|PubMed:9973285" FT /id="VAR_000333" FT VARIANT 174 FT /note="V -> M (in ACADVLD; dbSNP:rs369560930)" FT /evidence="ECO:0000269|PubMed:9973285" FT /id="VAR_000334" FT VARIANT 185 FT /note="G -> S (in ACADVLD; likely pathogenic; FT dbSNP:rs545215807)" FT /evidence="ECO:0000269|PubMed:9973285" FT /id="VAR_000335" FT VARIANT 213 FT /note="A -> P (in ACADVLD; likely pathogenic; FT dbSNP:rs140629318)" FT /evidence="ECO:0000269|PubMed:10077518" FT /id="VAR_010101" FT VARIANT 218 FT /note="E -> K (in ACADVLD; likely pathogenic; FT dbSNP:rs1432183079)" FT /evidence="ECO:0000269|PubMed:9973285" FT /id="VAR_000336" FT VARIANT 243 FT /note="L -> R (in ACADVLD)" FT /evidence="ECO:0000269|PubMed:9973285" FT /id="VAR_000337" FT VARIANT 247 FT /note="K -> E (in ACADVLD; dbSNP:rs387906253)" FT /evidence="ECO:0000269|PubMed:10077518" FT /id="VAR_010102" FT VARIANT 247 FT /note="K -> T (in ACADVLD)" FT /evidence="ECO:0000269|PubMed:9973285" FT /id="VAR_000338" FT VARIANT 260 FT /note="T -> M (in ACADVLD; likely pathogenic; FT dbSNP:rs113994168)" FT /evidence="ECO:0000269|PubMed:10077518, FT ECO:0000269|PubMed:8845838, ECO:0000269|PubMed:9973285" FT /id="VAR_000339" FT VARIANT 278 FT /note="Missing (in ACADVLD)" FT /evidence="ECO:0000269|PubMed:10077518, FT ECO:0000269|PubMed:9973285" FT /id="VAR_000340" FT VARIANT 281 FT /note="A -> D (in ACADVLD)" FT /evidence="ECO:0000269|PubMed:8845838, FT ECO:0000269|PubMed:9973285" FT /id="VAR_000341" FT VARIANT 283 FT /note="V -> A (in ACADVLD; pathogenic; dbSNP:rs113994167)" FT /evidence="ECO:0000269|PubMed:10077518, FT ECO:0000269|PubMed:8845838, ECO:0000269|PubMed:9973285" FT /id="VAR_000342" FT VARIANT 290 FT /note="G -> D (in ACADVLD; dbSNP:rs866464446)" FT /evidence="ECO:0000269|PubMed:9973285" FT /id="VAR_000343" FT VARIANT 294 FT /note="G -> E (in ACADVLD; uncertain significance; FT dbSNP:rs200573371)" FT /evidence="ECO:0000269|PubMed:9973285" FT /id="VAR_000344" FT VARIANT 299 FT /note="K -> N (in ACADVLD; dbSNP:rs774716484)" FT /evidence="ECO:0000269|PubMed:9973285" FT /id="VAR_000345" FT VARIANT 299 FT /note="Missing (in ACADVLD)" FT /evidence="ECO:0000269|PubMed:8554073" FT /id="VAR_000346" FT VARIANT 317 FT /note="V -> A (in ACADVLD; dbSNP:rs398123095)" FT /evidence="ECO:0000269|PubMed:8845838, FT ECO:0000269|PubMed:9973285" FT /id="VAR_000347" FT VARIANT 352 FT /note="M -> V (in ACADVLD; dbSNP:rs2071296420)" FT /evidence="ECO:0000269|PubMed:9973285" FT /id="VAR_000348" FT VARIANT 359 FT /note="A -> S (in dbSNP:rs1051701)" FT /id="VAR_011990" FT VARIANT 366 FT /note="R -> C (in ACADVLD; dbSNP:rs771874163)" FT /evidence="ECO:0000269|PubMed:8845838, FT ECO:0000269|PubMed:9973285" FT /id="VAR_000349" FT VARIANT 366 FT /note="R -> H (in ACADVLD; likely pathogenic; FT dbSNP:rs112406105)" FT /evidence="ECO:0000269|PubMed:9973285" FT /id="VAR_000350" FT VARIANT 381 FT /note="Missing (in ACADVLD; dbSNP:rs1057517281)" FT /evidence="ECO:0000269|PubMed:8845838, FT ECO:0000269|PubMed:9973285" FT /id="VAR_000351" FT VARIANT 382 FT /note="K -> Q (in ACADVLD; likely pathogenic; FT dbSNP:rs118204015)" FT /evidence="ECO:0000269|PubMed:8554073" FT /id="VAR_000352" FT VARIANT 405 FT /note="D -> H (in ACADVLD)" FT /evidence="ECO:0000269|PubMed:9973285" FT /id="VAR_000353" FT VARIANT 441 FT /note="G -> D (in ACADVLD; likely pathogenic; FT dbSNP:rs2309689)" FT /evidence="ECO:0000269|PubMed:10077518, FT ECO:0000269|PubMed:8845838, ECO:0000269|PubMed:9973285" FT /id="VAR_000354" FT VARIANT 450 FT /note="R -> H (in ACADVLD; likely pathogenic; FT dbSNP:rs118204016)" FT /evidence="ECO:0000269|PubMed:9546340, FT ECO:0000269|PubMed:9973285" FT /id="VAR_000355" FT VARIANT 453 FT /note="R -> Q (in ACADVLD; likely pathogenic; FT dbSNP:rs138058572)" FT /evidence="ECO:0000269|PubMed:9973285" FT /id="VAR_000356" FT VARIANT 454 FT /note="D -> N (in ACADVLD; dbSNP:rs1419606204)" FT /evidence="ECO:0000269|PubMed:9973285" FT /id="VAR_000357" FT VARIANT 456 FT /note="R -> H (in ACADVLD; likely pathogenic; FT dbSNP:rs794727112)" FT /evidence="ECO:0000269|PubMed:9973285" FT /id="VAR_000358" FT VARIANT 458 FT /note="F -> L (in ACADVLD; likely pathogenic; loss of FT acyl-CoA dehydrogenase activity; Loss of FAD FT cofactor-binding; dbSNP:rs118204017)" FT /evidence="ECO:0000269|PubMed:10077518, FT ECO:0000269|PubMed:9461620" FT /id="VAR_010103" FT VARIANT 459 FT /note="R -> W (in ACADVLD; dbSNP:rs766742117)" FT /evidence="ECO:0000269|PubMed:9973285" FT /id="VAR_000359" FT VARIANT 463 FT /note="G -> E (in ACADVLD; dbSNP:rs200366828)" FT /evidence="ECO:0000269|PubMed:9973285" FT /id="VAR_000360" FT VARIANT 469 FT /note="R -> Q (in ACADVLD; likely pathogenic; FT dbSNP:rs398123083)" FT /evidence="ECO:0000269|PubMed:9973285" FT /id="VAR_000361" FT VARIANT 469 FT /note="R -> W (in ACADVLD; likely pathogenic; FT dbSNP:rs113994170)" FT /evidence="ECO:0000269|PubMed:9973285" FT /id="VAR_000362" FT VARIANT 490 FT /note="A -> P (in ACADVLD; likely pathogenic; decreased FT association with mitochondrial inner membrane; may affect FT substrate specificity, possibly reducing the affinity for FT long-chain acyl-CoA substrates; dbSNP:rs759775666)" FT /evidence="ECO:0000269|PubMed:10077518, FT ECO:0000269|PubMed:17374501, ECO:0000269|PubMed:9839948" FT /id="VAR_010104" FT VARIANT 502 FT /note="L -> P (in ACADVLD; decreased association with FT mitochondrial inner membrane; decreased specific activity FT towards several substrates in vitro)" FT /evidence="ECO:0000269|PubMed:17374501, FT ECO:0000269|PubMed:9973285" FT /id="VAR_000363" FT VARIANT 534 FT /note="E -> K (in ACADVLD; uncertain significance; FT dbSNP:rs2230180)" FT /evidence="ECO:0000269|PubMed:10077518" FT /id="VAR_010105" FT VARIANT 583 FT /note="S -> W (in ACADVLD; Loss of homodimerization; loss FT of localization to mitochondrial inner membrane; FT dbSNP:rs1085307648)" FT /evidence="ECO:0000269|PubMed:9599005" FT /id="VAR_083892" FT VARIANT 602 FT /note="L -> I (in ACADVLD)" FT /evidence="ECO:0000269|PubMed:8845838, FT ECO:0000269|PubMed:9973285" FT /id="VAR_000364" FT VARIANT 613 FT /note="R -> W (in ACADVLD; likely pathogenic; FT dbSNP:rs118204014)" FT /evidence="ECO:0000269|PubMed:10077518, FT ECO:0000269|PubMed:8554073, ECO:0000269|PubMed:9973285" FT /id="VAR_000365" FT VARIANT 615 FT /note="R -> Q (in ACADVLD; likely benign; FT dbSNP:rs148584617)" FT /evidence="ECO:0000269|PubMed:10077518" FT /id="VAR_010106" FT VARIANT 623 FT /note="S -> F (in dbSNP:rs13383)" FT /id="VAR_011991" FT MUTAGEN 458 FT /note="F->T: Decreased acyl-CoA dehydrogenase activity. FT Decreased affinity for acyl-CoA. No effect on FAD FT cofactor-binding." FT /evidence="ECO:0000269|PubMed:9461620" FT MUTAGEN 458 FT /note="F->V: Loss of acyl-CoA dehydrogenase activity. Loss FT of FAD cofactor-binding." FT /evidence="ECO:0000269|PubMed:9461620" FT MUTAGEN 458 FT /note="F->Y: Decreased acyl-CoA dehydrogenase activity. No FT effect on affinity for acyl-CoA. Decreased FAD FT cofactor-binding." FT /evidence="ECO:0000269|PubMed:9461620" FT MUTAGEN 462 FT /note="E->D: Decreased acyl-CoA dehydrogenase activity. No FT effect on affinity for acyl-CoA. No effect on FAD FT cofactor-binding." FT /evidence="ECO:0000269|PubMed:9461620" FT MUTAGEN 462 FT /note="E->Q: Loss of acyl-CoA dehydrogenase activity. No FT effect on FAD cofactor-binding." FT /evidence="ECO:0000269|PubMed:9461620" FT MUTAGEN 490 FT /note="A->G,V,S,D,H: Changed substrate specificity with FT decreased affinity for tetradecanoyl-CoA and FT hexadecanoyl-CoA." FT /evidence="ECO:0000269|PubMed:9839948" FT CONFLICT 193 FT /note="G -> C (in Ref. 3; BAA29057)" FT /evidence="ECO:0000305" FT CONFLICT 200 FT /note="K -> E (in Ref. 4; BAG57027)" FT /evidence="ECO:0000305" FT CONFLICT 541 FT /note="E -> K (in Ref. 4; BAG57027)" FT /evidence="ECO:0000305" FT HELIX 73..78 FT /evidence="ECO:0007829|PDB:7S7G" FT TURN 85..87 FT /evidence="ECO:0007829|PDB:7S7G" FT HELIX 96..115 FT /evidence="ECO:0007829|PDB:7S7G" FT HELIX 119..125 FT /evidence="ECO:0007829|PDB:7S7G" FT HELIX 130..138 FT /evidence="ECO:0007829|PDB:7S7G" FT TURN 139..142 FT /evidence="ECO:0007829|PDB:7S7G" FT HELIX 148..150 FT /evidence="ECO:0007829|PDB:7S7G" FT HELIX 157..170 FT /evidence="ECO:0007829|PDB:7S7G" FT HELIX 172..179 FT /evidence="ECO:0007829|PDB:7S7G" FT HELIX 180..185 FT /evidence="ECO:0007829|PDB:7S7G" FT HELIX 187..192 FT /evidence="ECO:0007829|PDB:7S7G" FT HELIX 195..207 FT /evidence="ECO:0007829|PDB:7S7G" FT STRAND 212..215 FT /evidence="ECO:0007829|PDB:7S7G" FT STRAND 221..223 FT /evidence="ECO:0007829|PDB:7S7G" FT HELIX 225..227 FT /evidence="ECO:0007829|PDB:7S7G" FT STRAND 231..234 FT /evidence="ECO:0007829|PDB:7S7G" FT STRAND 238..251 FT /evidence="ECO:0007829|PDB:7S7G" FT TURN 252..255 FT /evidence="ECO:0007829|PDB:7S7G" FT STRAND 257..268 FT /evidence="ECO:0007829|PDB:7S7G" FT TURN 270..272 FT /evidence="ECO:0007829|PDB:7S7G" FT STRAND 275..285 FT /evidence="ECO:0007829|PDB:7S7G" FT HELIX 286..288 FT /evidence="ECO:0007829|PDB:7S7G" FT STRAND 289..293 FT /evidence="ECO:0007829|PDB:7S7G" FT HELIX 295..298 FT /evidence="ECO:0007829|PDB:7S7G" FT STRAND 307..318 FT /evidence="ECO:0007829|PDB:7S7G" FT HELIX 319..321 FT /evidence="ECO:0007829|PDB:7S7G" FT STRAND 322..325 FT /evidence="ECO:0007829|PDB:7S7G" FT HELIX 329..365 FT /evidence="ECO:0007829|PDB:7S7G" FT HELIX 373..375 FT /evidence="ECO:0007829|PDB:7S7G" FT HELIX 377..405 FT /evidence="ECO:0007829|PDB:7S7G" FT HELIX 412..437 FT /evidence="ECO:0007829|PDB:7S7G" FT HELIX 439..442 FT /evidence="ECO:0007829|PDB:7S7G" FT HELIX 448..455 FT /evidence="ECO:0007829|PDB:7S7G" FT HELIX 456..459 FT /evidence="ECO:0007829|PDB:7S7G" FT STRAND 461..463 FT /evidence="ECO:0007829|PDB:7S7G" FT HELIX 465..486 FT /evidence="ECO:0007829|PDB:7S7G" FT TURN 494..496 FT /evidence="ECO:0007829|PDB:7S7G" FT TURN 522..524 FT /evidence="ECO:0007829|PDB:7S7G" FT HELIX 527..529 FT /evidence="ECO:0007829|PDB:7S7G" FT HELIX 530..554 FT /evidence="ECO:0007829|PDB:7S7G" FT HELIX 555..560 FT /evidence="ECO:0007829|PDB:7S7G" FT HELIX 562..591 FT /evidence="ECO:0007829|PDB:7S7G" FT HELIX 596..622 FT /evidence="ECO:0007829|PDB:7S7G" FT HELIX 627..644 FT /evidence="ECO:0007829|PDB:7S7G" SQ SEQUENCE 655 AA; 70390 MW; A5594D1EA7911D19 CRC64; MQAARMAASL GRQLLRLGGG SSRLTALLGQ PRPGPARRPY AGGAAQLALD KSDSHPSDAL TRKKPAKAES KSFAVGMFKG QLTTDQVFPY PSVLNEEQTQ FLKELVEPVS RFFEEVNDPA KNDALEMVEE TTWQGLKELG AFGLQVPSEL GGVGLCNTQY ARLVEIVGMH DLGVGITLGA HQSIGFKGIL LFGTKAQKEK YLPKLASGET VAAFCLTEPS SGSDAASIRT SAVPSPCGKY YTLNGSKLWI SNGGLADIFT VFAKTPVTDP ATGAVKEKIT AFVVERGFGG ITHGPPEKKM GIKASNTAEV FFDGVRVPSE NVLGEVGSGF KVAMHILNNG RFGMAAALAG TMRGIIAKAV DHATNRTQFG EKIHNFGLIQ EKLARMVMLQ YVTESMAYMV SANMDQGATD FQIEAAISKI FGSEAAWKVT DECIQIMGGM GFMKEPGVER VLRDLRIFRI FEGTNDILRL FVALQGCMDK GKELSGLGSA LKNPFGNAGL LLGEAGKQLR RRAGLGSGLS LSGLVHPELS RSGELAVRAL EQFATVVEAK LIKHKKGIVN EQFLLQRLAD GAIDLYAMVV VLSRASRSLS EGHPTAQHEK MLCDTWCIEA AARIREGMAA LQSDPWQQEL YRNFKSISKA LVERGGVVTS NPLGF //