ID A0A177AW90_9BILA Unreviewed; 611 AA. AC A0A177AW90; DT 07-SEP-2016, integrated into UniProtKB/TrEMBL. DT 07-SEP-2016, sequence version 1. DT 27-NOV-2024, entry version 23. DE RecName: Full=Very long-chain specific acyl-CoA dehydrogenase, mitochondrial {ECO:0000256|ARBA:ARBA00040902}; DE EC=1.3.8.9 {ECO:0000256|ARBA:ARBA00039034}; GN ORFNames=A3Q56_06017 {ECO:0000313|EMBL:OAF66255.1}; OS Intoshia linei. OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mesozoa; Orthonectida; OC Rhopaluridae; Intoshia. OX NCBI_TaxID=1819745 {ECO:0000313|EMBL:OAF66255.1, ECO:0000313|Proteomes:UP000078046}; RN [1] {ECO:0000313|EMBL:OAF66255.1, ECO:0000313|Proteomes:UP000078046} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Intl2013 {ECO:0000313|EMBL:OAF66255.1}; RC TISSUE=Whole animal {ECO:0000313|EMBL:OAF66255.1}; RA Mikhailov K.V., Slusarev G.S., Nikitin M.A., Logacheva M.D., Penin A., RA Aleoshin V., Panchin Y.V.; RT "The genome of Intoshia linei affirms orthonectids as highly simplified RT spiralians."; RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Very long-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. The CC first step of fatty acid beta-oxidation consists in the removal of one CC hydrogen from C-2 and C-3 of the straight-chain fatty acyl-CoA CC thioester, resulting in the formation of trans-2-enoyl-CoA. Among the CC different mitochondrial acyl-CoA dehydrogenases, very long-chain CC specific acyl-CoA dehydrogenase acts specifically on acyl-CoAs with CC saturated 12 to 24 carbons long primary chains. CC {ECO:0000256|ARBA:ARBA00045422}. 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:0000256|ARBA:ARBA00001337}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43449; CC Evidence={ECO:0000256|ARBA:ARBA00001337}; 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:0000256|ARBA:ARBA00000364}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47241; CC Evidence={ECO:0000256|ARBA:ARBA00000364}; 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:0000256|ARBA:ARBA00001765}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47233; CC Evidence={ECO:0000256|ARBA:ARBA00001765}; 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:0000256|ARBA:ARBA00001236}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47317; CC Evidence={ECO:0000256|ARBA:ARBA00001236}; 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:0000256|ARBA:ARBA00036538}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19182; CC Evidence={ECO:0000256|ARBA:ARBA00036538}; 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:0000256|ARBA:ARBA00001486}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47297; CC Evidence={ECO:0000256|ARBA:ARBA00001486}; 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:0000256|ARBA:ARBA00000733}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47237; CC Evidence={ECO:0000256|ARBA:ARBA00000733}; CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|ARBA:ARBA00001974, CC ECO:0000256|RuleBase:RU362125}; CC -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}. CC -!- SUBUNIT: Homodimer. Homodimerizes after import into the mitochondrion. CC {ECO:0000256|ARBA:ARBA00046812}. CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane CC {ECO:0000256|ARBA:ARBA00004637}; Peripheral membrane protein CC {ECO:0000256|ARBA:ARBA00004637}. CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family. CC {ECO:0000256|ARBA:ARBA00009347, ECO:0000256|RuleBase:RU362125}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:OAF66255.1}. 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; LWCA01000988; OAF66255.1; -; Genomic_DNA. DR AlphaFoldDB; A0A177AW90; -. DR Proteomes; UP000078046; Unassembled WGS sequence. DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell. DR GO; GO:0000062; F:fatty-acyl-CoA binding; IEA:TreeGrafter. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0017099; F:very-long-chain fatty acyl-CoA dehydrogenase activity; IEA:TreeGrafter. DR FunFam; 1.20.140.10:FF:000008; acyl-CoA dehydrogenase family member 9, 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; 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: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. PE 3: Inferred from homology; KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU362125}; KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832}; KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630, KW ECO:0000256|RuleBase:RU362125}; KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098}; KW Membrane {ECO:0000256|ARBA:ARBA00023136}; KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128}; KW Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792}; KW Oxidoreductase {ECO:0000256|RuleBase:RU362125}; KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}; KW Reference proteome {ECO:0000313|Proteomes:UP000078046}; KW S-nitrosylation {ECO:0000256|ARBA:ARBA00022799}. FT DOMAIN 82..173 FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal" FT /evidence="ECO:0000259|Pfam:PF02771" FT DOMAIN 177..279 FT /note="Acyl-CoA oxidase/dehydrogenase middle" FT /evidence="ECO:0000259|Pfam:PF02770" FT DOMAIN 291..436 FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal" FT /evidence="ECO:0000259|Pfam:PF00441" FT DOMAIN 482..602 FT /note="ACAD9/ACADV-like C-terminal" FT /evidence="ECO:0000259|Pfam:PF21343" SQ SEQUENCE 611 AA; 67978 MW; 45D7AE8985F4E012 CRC64; MFQTILSLCR LRGMTKILYS NGFQARFKSD FKTSDSFVLN LFANKIVTNK IFPYPKALTD SQREELELMV PQIDKSYGEM LNADEMDRTS KISNEIFKFL GEQGAFGIQI PTKYGGLGFT NTQFAKLTEV MAKFDLSILI MLGAHQSIGL KGILLYGTEE QKKKYLPKLA TGEHIAAYCL TEPSSGSDAN SIRSKAVLSN DKSHYILNGS KIWITNGGIA KIFTVFAQVP IKDEKTGETK NRVTAFIVER EFQGVTSGKA EDKMGIRSCN TTELYFDNVK IPVANVLGEV GNGFKVAVNI LNSGRFAMCT SLAGAMKAAI KMAVNHAATR VQFGNTLDKY GSVQEKLYKM AALQYTAESV GYLLAGIMDQ GQKEFQMESA IGKIFASEAA WNVVDEAIQI HGGMGFMREL GLERVLRDLR IFRIFEGAND VLRLFISLTG CQYAGKNLMH MARSSPMDII KKQGKRLFGS YDTSIIDNCT DQLKGSANDI SFVMNLFGIS VEKLLLKYKK EIIHEQMLLS RISNAVIDIF TSVAVLSRVN KTIDENLPSK QHEILLSKII IFEAMKRAKH NLNIVIMKNA KDANMFNEIS QISKNIIENE GVLQGHPTNI I //