ACAD9_RAT
ID ACAD9_RAT Reviewed; 625 AA.
AC B1WC61;
DT 18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 03-AUG-2022, entry version 108.
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|RGD:727973};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116 {ECO:0000312|EMBL:AAI62016.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 SUBUNIT.
RX PubMed=22982022; DOI=10.1016/j.cmet.2012.08.009;
RA Heide H., Bleier L., Steger M., Ackermann J., Drose S., Schwamb B.,
RA Zornig M., Reichert A.S., Koch I., Wittig I., Brandt U.;
RT "Complexome profiling identifies TMEM126B as a component of the
RT mitochondrial complex I assembly complex.";
RL Cell Metab. 16:538-549(2012).
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 (PubMed:22982022). 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
CC (PubMed:22982022) (By similarity). Interacts with TMEM70 and TMEM242
CC (By similarity). {ECO:0000250|UniProtKB:Q9H845,
CC ECO:0000269|PubMed:22982022}.
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:0000255|RuleBase:RU362125}.
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DR EMBL; AABR07010088; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC162016; AAI62016.1; -; mRNA.
DR RefSeq; NP_861433.2; NM_181768.2.
DR RefSeq; XP_006232331.1; XM_006232269.1.
DR AlphaFoldDB; B1WC61; -.
DR SMR; B1WC61; -.
DR IntAct; B1WC61; 2.
DR STRING; 10116.ENSRNOP00000019108; -.
DR iPTMnet; B1WC61; -.
DR PhosphoSitePlus; B1WC61; -.
DR jPOST; B1WC61; -.
DR PaxDb; B1WC61; -.
DR PeptideAtlas; B1WC61; -.
DR PRIDE; B1WC61; -.
DR Ensembl; ENSRNOT00000089353; ENSRNOP00000070329; ENSRNOG00000014178.
DR GeneID; 294973; -.
DR KEGG; rno:294973; -.
DR CTD; 28976; -.
DR RGD; 727973; Acad9.
DR eggNOG; KOG0137; Eukaryota.
DR GeneTree; ENSGT00940000157312; -.
DR HOGENOM; CLU_018204_11_2_1; -.
DR InParanoid; B1WC61; -.
DR OMA; HPHRATQ; -.
DR OrthoDB; 819314at2759; -.
DR TreeFam; TF105053; -.
DR Reactome; R-RNO-6799198; Complex I biogenesis.
DR PRO; PR:B1WC61; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000014178; Expressed in heart and 19 other tissues.
DR GO; GO:0030425; C:dendrite; ISO:RGD.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031966; C:mitochondrial membrane; ISO:RGD.
DR GO; GO:0005739; C:mitochondrion; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
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:RGD.
DR GO; GO:0070991; F:medium-chain-acyl-CoA dehydrogenase activity; ISO:RGD.
DR GO; GO:0017099; F:very-long-chain-acyl-CoA dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0046395; P:carboxylic acid catabolic process; IEA:UniProt.
DR GO; GO:0001676; P:long-chain fatty acid metabolic process; ISO:RGD.
DR GO; GO:0051791; P:medium-chain fatty acid metabolic process; ISO:RGD.
DR GO; GO:0032981; P:mitochondrial respiratory chain complex I assembly; ISO:RGD.
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_0000447709"
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:0000250|UniProtKB:Q8JZN5"
FT MOD_RES 482
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8JZN5"
FT MOD_RES 525
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8JZN5"
FT MOD_RES 525
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8JZN5"
SQ SEQUENCE 625 AA; 68843 MW; 38CAC363A3070F1A CRC64;
MSGYVLFSRG ATAAAAAARA SRVLRVFTER RRTLHTSLQS CSFAKELFLG HIQQKGVFPF
PEVSQEELSE INQFVGPLEK FFNEEVDSRK IDQEGKIPAD TLAKLKSLGL FGIQVPEEYG
GLGLSNTMYA RLGEIISMDA SITVTLAAHQ AIGLKGIILV GNEEQKAKYL PKLSSGEHIA
AFCLTEPASG SDAASIQTRA TLSEDKKYFV LNGSKVWITN GGLANIFTVF AKTEVVDSDG
SIKDKMTAFI VERDFGGITN GKPEDKLGIR GSNTCEVHFE NTRVPVENVL GEVGGGFKVA
MNILNSGRFS MGSAVAGMLK KLIEQTAEYA CTRKQFNRNL SEFGLIQEKF ALMAQKAYVM
ESMAYLTSGM LDQPGFPDCS IEAAMVKVFS SEAAWQCVSE ALQILGGSGY MKDYPYERML
RDARILLIFE GTNEILRLFI ALTGLQHAGR ILTSRIKELK SGNVTTVMET IGRKLRDSLG
RTVDLGLSSN IAVVHPSLGD SANKLEENVH YFGRTVETLL LRFGKTIVEE QLVLKRVANI
LINLYGMTAV LSRASRSIRI GLKNHDHEIL LANMFCVEAY FQNLFSLSQL DKYAPENLDE
QIKKVSQQIL EKRAYICAHP LDRAS
