ACAD9_MOUSE
ID ACAD9_MOUSE Reviewed; 625 AA.
AC Q8JZN5; Q3ULL9; Q8BK76; Q8C0B5;
DT 03-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Complex I assembly factor ACAD9, mitochondrial {ECO:0000250|UniProtKB:Q9H845};
DE AltName: Full=Acyl-CoA dehydrogenase family member 9 {ECO:0000250|UniProtKB:Q9H845};
DE Short=ACAD-9 {ECO:0000250|UniProtKB:Q9H845};
DE EC=1.3.8.- {ECO:0000250|UniProtKB:Q9H845};
DE Flags: Precursor;
GN Name=Acad9 {ECO:0000312|MGI:MGI:1914272};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Medulla oblongata;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Kidney;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-482, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-96; LYS-242 AND LYS-525, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-525, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT identifies substrates of SIRT3 in metabolic pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
CC -!- FUNCTION: As part of the MCIA complex, primarily participates in the
CC assembly of the mitochondrial complex I and therefore plays a role in
CC oxidative phosphorylation. This moonlighting protein has also a
CC dehydrogenase activity toward a broad range of substrates with greater
CC specificity for long-chain unsaturated acyl-CoAs. However, in vivo, it
CC does not seem to play a primary role in fatty acid oxidation. In
CC addition, the function in complex I assembly is independent of the
CC dehydrogenase activity of the protein. {ECO:0000250|UniProtKB:Q9H845}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=eicosanoyl-CoA + H(+) + oxidized [electron-transfer
CC flavoprotein] = (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:0000250|UniProtKB:Q9H845};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47237;
CC Evidence={ECO:0000250|UniProtKB:Q9H845};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + octadecanoyl-CoA + oxidized [electron-transfer
CC flavoprotein] = (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:0000250|UniProtKB:Q9H845};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47241;
CC Evidence={ECO:0000250|UniProtKB:Q9H845};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + hexadecanoyl-CoA + oxidized [electron-transfer
CC flavoprotein] = (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:0000250|UniProtKB:Q9H845};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43449;
CC Evidence={ECO:0000250|UniProtKB:Q9H845};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=decanoyl-CoA + H(+) + oxidized [electron-transfer
CC flavoprotein] = (2E)-decenoyl-CoA + reduced [electron-transfer
CC flavoprotein]; Xref=Rhea:RHEA:48176, Rhea:RHEA-COMP:10685, Rhea:RHEA-
CC COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307,
CC ChEBI:CHEBI:61406, ChEBI:CHEBI:61430;
CC Evidence={ECO:0000250|UniProtKB:Q9H845};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48177;
CC Evidence={ECO:0000250|UniProtKB:Q9H845};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + nonanoyl-CoA + oxidized [electron-transfer
CC flavoprotein] = (2E)-nonenoyl-CoA + reduced [electron-transfer
CC flavoprotein]; Xref=Rhea:RHEA:48208, Rhea:RHEA-COMP:10685, Rhea:RHEA-
CC COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307,
CC ChEBI:CHEBI:76291, ChEBI:CHEBI:76292;
CC Evidence={ECO:0000250|UniProtKB:Q9H845};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48209;
CC Evidence={ECO:0000250|UniProtKB:Q9H845};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + oxidized [electron-transfer flavoprotein] +
CC pentadecanoyl-CoA = (2E)-pentadecenoyl-CoA + reduced [electron-
CC transfer flavoprotein]; Xref=Rhea:RHEA:48204, Rhea:RHEA-COMP:10685,
CC Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692,
CC ChEBI:CHEBI:58307, ChEBI:CHEBI:74309, ChEBI:CHEBI:77545;
CC Evidence={ECO:0000250|UniProtKB:Q9H845};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48205;
CC Evidence={ECO:0000250|UniProtKB:Q9H845};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + oxidized [electron-transfer flavoprotein] + undecanoyl-
CC CoA = reduced [electron-transfer flavoprotein] + trans-2-undecenoyl-
CC CoA; Xref=Rhea:RHEA:48200, Rhea:RHEA-COMP:10685, Rhea:RHEA-
CC COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307,
CC ChEBI:CHEBI:77547, ChEBI:CHEBI:77548;
CC Evidence={ECO:0000250|UniProtKB:Q9H845};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48201;
CC Evidence={ECO:0000250|UniProtKB:Q9H845};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-hexadecenoyl-CoA + H(+) + oxidized [electron-transfer
CC flavoprotein] = (2E,9Z)-hexadecadienoyl-CoA + reduced [electron-
CC transfer flavoprotein]; Xref=Rhea:RHEA:47304, Rhea:RHEA-COMP:10685,
CC Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692,
CC ChEBI:CHEBI:58307, ChEBI:CHEBI:61540, ChEBI:CHEBI:77549;
CC Evidence={ECO:0000250|UniProtKB:Q9H845};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47305;
CC Evidence={ECO:0000250|UniProtKB:Q9H845};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + heptadecanoyl-CoA + oxidized [electron-transfer
CC flavoprotein] = reduced [electron-transfer flavoprotein] + trans-2-
CC heptadecenoyl-CoA; Xref=Rhea:RHEA:48196, Rhea:RHEA-COMP:10685,
CC Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692,
CC ChEBI:CHEBI:58307, ChEBI:CHEBI:74307, ChEBI:CHEBI:77551;
CC Evidence={ECO:0000250|UniProtKB:Q9H845};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48197;
CC Evidence={ECO:0000250|UniProtKB:Q9H845};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9E)-octadecenoyl-CoA + H(+) + oxidized [electron-transfer
CC flavoprotein] = (2E,9E)-octadecadienoyl-CoA + reduced [electron-
CC transfer flavoprotein]; Xref=Rhea:RHEA:48192, Rhea:RHEA-COMP:10685,
CC Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692,
CC ChEBI:CHEBI:58307, ChEBI:CHEBI:77537, ChEBI:CHEBI:77552;
CC Evidence={ECO:0000250|UniProtKB:Q9H845};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48193;
CC Evidence={ECO:0000250|UniProtKB:Q9H845};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + H(+) + oxidized [electron-transfer
CC flavoprotein] = (2E,9Z)-octadecadienoyl-CoA + reduced [electron-
CC transfer flavoprotein]; Xref=Rhea:RHEA:47300, Rhea:RHEA-COMP:10685,
CC Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57387,
CC ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:77553;
CC Evidence={ECO:0000250|UniProtKB:Q9H845};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47301;
CC Evidence={ECO:0000250|UniProtKB:Q9H845};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoyl-CoA + H(+) + oxidized [electron-
CC transfer flavoprotein] = (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:0000250|UniProtKB:Q9H845};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48189;
CC Evidence={ECO:0000250|UniProtKB:Q9H845};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoyl-CoA + H(+) + oxidized
CC [electron-transfer flavoprotein] = (2E,4Z,7Z,10Z,13Z,16Z,19Z)-
CC docosaheptaenoyl-CoA + reduced [electron-transfer flavoprotein];
CC Xref=Rhea:RHEA:48184, Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307,
CC ChEBI:CHEBI:74298, ChEBI:CHEBI:77559;
CC Evidence={ECO:0000250|UniProtKB:Q9H845};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48185;
CC Evidence={ECO:0000250|UniProtKB:Q9H845};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + oxidized [electron-transfer flavoprotein] +
CC tetradecanoyl-CoA = (2E)-tetradecenoyl-CoA + reduced [electron-
CC transfer flavoprotein]; Xref=Rhea:RHEA:47316, Rhea:RHEA-COMP:10685,
CC Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57385,
CC ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:61405;
CC Evidence={ECO:0000250|UniProtKB:Q9H845};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47317;
CC Evidence={ECO:0000250|UniProtKB:Q9H845};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:Q9H845};
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with NDUFAF1 and ECSIT
CC (By similarity). Part of the mitochondrial complex I assembly/MCIA
CC complex that comprises at least the core subunits TMEM126B, NDUFAF1,
CC ECSIT and ACAD9 and complement subunits such as COA1 and TMEM186 (By
CC similarity). Interacts with TMEM70 and TMEM242 (By similarity).
CC {ECO:0000250|UniProtKB:B1WC61, ECO:0000250|UniProtKB:Q9H845}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:Q9H845}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q9H845}; Matrix side
CC {ECO:0000250|UniProtKB:Q9H845}. Note=Essentially associated with
CC membranes. {ECO:0000250|UniProtKB:Q9H845}.
CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; AK031820; BAC27565.1; -; mRNA.
DR EMBL; AK075984; BAC36096.1; -; mRNA.
DR EMBL; AK145423; BAE26429.1; -; mRNA.
DR EMBL; BC031137; AAH31137.1; -; mRNA.
DR EMBL; BC032213; AAH32213.1; -; mRNA.
DR EMBL; BC033277; AAH33277.1; -; mRNA.
DR CCDS; CCDS17310.1; -.
DR RefSeq; NP_766266.3; NM_172678.3.
DR AlphaFoldDB; Q8JZN5; -.
DR SMR; Q8JZN5; -.
DR BioGRID; 230821; 9.
DR DIP; DIP-59192N; -.
DR IntAct; Q8JZN5; 3.
DR STRING; 10090.ENSMUSP00000011492; -.
DR iPTMnet; Q8JZN5; -.
DR PhosphoSitePlus; Q8JZN5; -.
DR SwissPalm; Q8JZN5; -.
DR EPD; Q8JZN5; -.
DR jPOST; Q8JZN5; -.
DR MaxQB; Q8JZN5; -.
DR PaxDb; Q8JZN5; -.
DR PeptideAtlas; Q8JZN5; -.
DR PRIDE; Q8JZN5; -.
DR ProteomicsDB; 285632; -.
DR Antibodypedia; 33213; 176 antibodies from 24 providers.
DR DNASU; 229211; -.
DR Ensembl; ENSMUST00000011492; ENSMUSP00000011492; ENSMUSG00000027710.
DR GeneID; 229211; -.
DR KEGG; mmu:229211; -.
DR UCSC; uc008oze.1; mouse.
DR CTD; 28976; -.
DR MGI; MGI:1914272; Acad9.
DR VEuPathDB; HostDB:ENSMUSG00000027710; -.
DR eggNOG; KOG0137; Eukaryota.
DR GeneTree; ENSGT00940000157312; -.
DR HOGENOM; CLU_018204_11_2_1; -.
DR InParanoid; Q8JZN5; -.
DR OMA; HPHRATQ; -.
DR OrthoDB; 819314at2759; -.
DR PhylomeDB; Q8JZN5; -.
DR TreeFam; TF105053; -.
DR Reactome; R-MMU-6799198; Complex I biogenesis.
DR BioGRID-ORCS; 229211; 21 hits in 75 CRISPR screens.
DR ChiTaRS; Acad9; mouse.
DR PRO; PR:Q8JZN5; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q8JZN5; protein.
DR Bgee; ENSMUSG00000027710; Expressed in right kidney and 141 other tissues.
DR ExpressionAtlas; Q8JZN5; baseline and differential.
DR Genevisible; Q8JZN5; MM.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031966; C:mitochondrial membrane; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0000062; F:fatty-acyl-CoA binding; IBA:GO_Central.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0004466; F:long-chain-acyl-CoA dehydrogenase activity; ISO:MGI.
DR GO; GO:0070991; F:medium-chain-acyl-CoA dehydrogenase activity; ISO:MGI.
DR GO; GO:0017099; F:very-long-chain-acyl-CoA dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0006635; P:fatty acid beta-oxidation; IEA:UniProt.
DR GO; GO:0001676; P:long-chain fatty acid metabolic process; ISO:MGI.
DR GO; GO:0051791; P:medium-chain fatty acid metabolic process; ISO:MGI.
DR GO; GO:0032981; P:mitochondrial respiratory chain complex I assembly; ISO:MGI.
DR Gene3D; 1.10.540.10; -; 1.
DR Gene3D; 2.40.110.10; -; 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.
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; SSF47203; 2.
DR SUPFAM; SSF56645; SSF56645; 1.
DR PROSITE; PS00072; ACYL_COA_DH_1; 1.
DR PROSITE; PS00073; ACYL_COA_DH_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; FAD; Flavoprotein; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Oxidoreductase; Phosphoprotein;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..41
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 42..625
FT /note="Complex I assembly factor ACAD9, mitochondrial"
FT /id="PRO_0000000525"
FT ACT_SITE 430
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P49748"
FT MOD_RES 45
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9H845"
FT MOD_RES 96
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 242
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 482
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 525
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 525
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT CONFLICT 15
FT /note="A -> G (in Ref. 1; BAC27565)"
FT /evidence="ECO:0000305"
FT CONFLICT 53
FT /note="E -> K (in Ref. 2; AAH31137/AAH32213/AAH33277)"
FT /evidence="ECO:0000305"
FT CONFLICT 163
FT /note="E -> D (in Ref. 2; AAH31137/AAH32213/AAH33277)"
FT /evidence="ECO:0000305"
FT CONFLICT 540
FT /note="I -> V (in Ref. 1; BAC27565)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 625 AA; 68722 MW; 29567F60B52E6FEA CRC64;
MSGCVLLSRG ATAAAAAARA SRVLREFTAR RRPLHTSLQS CSFAKELFLG NIEQKGVFPF
PEVSQHELSE INQFVGPLEK FFTEEVDSRK IDQEGKIPVD TLEKLKSLGL FGIQVPEEYG
GLGLSNTMYA RLGEIISLDA SITVTLAAHQ AIGLKGIILV GNEEQKAKYL PKLSSGEHIA
AFCLTEPASG SDAASIQTRA TLSEDKKYFI LNGSKVWITN GGLANIFTVF AKTEVVDSDG
SKTDKMTAFI VERDFGGITN GKPEDKLGIR GSNTCEVHFE NTRVPVENVL GEVGGGFKVA
MNILNSGRFS MGSAVAGMLK KLIELTAEYA CTRKQFNRNL SEFGLIQEKF ALMAQKAYVM
ESMAYLTSGM LDQPGFPDCS IEAAMVKVFS SEAAWQCVSE ALQILGGSGY MKDYPYERML
RDARILLIFE GTNEILRLFI ALTGLQHAGR ILTSRIKELK SGNVTTVMET IGRKLRDSLG
RTVDLGLTGD LGVVHPSLGD SANKLEENVH YFGRTVETLL LRFGKNIVEE QLVLKRVANI
LINLYGMTAV LSRASRSIRI GLRNHDHEVL LANMFCVEAY FQNLFSLSQL DKNAPENLDE
QIKKVSRQIL EKRAYICAHP LDRAS
