ID Q5T4U5_HUMAN Unreviewed; 454 AA. AC Q5T4U5; DT 21-DEC-2004, integrated into UniProtKB/TrEMBL. DT 21-DEC-2004, sequence version 1. DT 27-MAR-2024, entry version 164. DE RecName: Full=Medium-chain specific acyl-CoA dehydrogenase, mitochondrial {ECO:0000256|ARBA:ARBA00019125}; DE EC=1.3.8.7 {ECO:0000256|ARBA:ARBA00012033}; GN Name=ACADM {ECO:0000313|EMBL:EAX06399.1, GN ECO:0000313|Ensembl:ENSP00000359871.5}; GN ORFNames=hCG_22915 {ECO:0000313|EMBL:EAX06399.1}; 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 {ECO:0000313|Ensembl:ENSP00000359871.5, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|EMBL:EAX06399.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=11181995; DOI=10.1126/science.1058040; RA Venter J.C., Adams M.D., Myers E.W., Li P.W., Mural R.J., Sutton G.G., RA Smith H.O., Yandell M., Evans C.A., Holt R.A., Gocayne J.D., Amanatides P., RA Ballew R.M., Huson D.H., Wortman J.R., Zhang Q., Kodira C.D., Zheng X.H., RA Chen L., Skupski M., Subramanian G., Thomas P.D., Zhang J., RA Gabor Miklos G.L., Nelson C., Broder S., Clark A.G., Nadeau J., RA McKusick V.A., Zinder N., Levine A.J., Roberts R.J., Simon M., Slayman C., RA Hunkapiller M., Bolanos R., Delcher A., Dew I., Fasulo D., Flanigan M., RA Florea L., Halpern A., Hannenhalli S., Kravitz S., Levy S., Mobarry C., RA Reinert K., Remington K., Abu-Threideh J., Beasley E., Biddick K., RA Bonazzi V., Brandon R., Cargill M., Chandramouliswaran I., Charlab R., RA Chaturvedi K., Deng Z., Di Francesco V., Dunn P., Eilbeck K., RA Evangelista C., Gabrielian A.E., Gan W., Ge W., Gong F., Gu Z., Guan P., RA Heiman T.J., Higgins M.E., Ji R.R., Ke Z., Ketchum K.A., Lai Z., Lei Y., RA Li Z., Li J., Liang Y., Lin X., Lu F., Merkulov G.V., Milshina N., RA Moore H.M., Naik A.K., Narayan V.A., Neelam B., Nusskern D., Rusch D.B., RA Salzberg S., Shao W., Shue B., Sun J., Wang Z., Wang A., Wang X., Wang J., RA Wei M., Wides R., Xiao C., Yan C., Yao A., Ye J., Zhan M., Zhang W., RA Zhang H., Zhao Q., Zheng L., Zhong F., Zhong W., Zhu S., Zhao S., RA Gilbert D., Baumhueter S., Spier G., Carter C., Cravchik A., Woodage T., RA Ali F., An H., Awe A., Baldwin D., Baden H., Barnstead M., Barrow I., RA Beeson K., Busam D., Carver A., Center A., Cheng M.L., Curry L., RA Danaher S., Davenport L., Desilets R., Dietz S., Dodson K., Doup L., RA Ferriera S., Garg N., Gluecksmann A., Hart B., Haynes J., Haynes C., RA Heiner C., Hladun S., Hostin D., Houck J., Howland T., Ibegwam C., RA Johnson J., Kalush F., Kline L., Koduru S., Love A., Mann F., May D., RA McCawley S., McIntosh T., McMullen I., Moy M., Moy L., Murphy B., RA Nelson K., Pfannkoch C., Pratts E., Puri V., Qureshi H., Reardon M., RA Rodriguez R., Rogers Y.H., Romblad D., Ruhfel B., Scott R., Sitter C., RA Smallwood M., Stewart E., Strong R., Suh E., Thomas R., Tint N.N., Tse S., RA Vech C., Wang G., Wetter J., Williams S., Williams M., Windsor S., RA Winn-Deen E., Wolfe K., Zaveri J., Zaveri K., Abril J.F., Guigo R., RA Campbell M.J., Sjolander K.V., Karlak B., Kejariwal A., Mi H., Lazareva B., RA Hatton T., Narechania A., Diemer K., Muruganujan A., Guo N., Sato S., RA Bafna V., Istrail S., Lippert R., Schwartz R., Walenz B., Yooseph S., RA Allen D., Basu A., Baxendale J., Blick L., Caminha M., Carnes-Stine J., RA Caulk P., Chiang Y.H., Coyne M., Dahlke C., Mays A., Dombroski M., RA Donnelly M., Ely D., Esparham S., Fosler C., Gire H., Glanowski S., RA Glasser K., Glodek A., Gorokhov M., Graham K., Gropman B., Harris M., RA Heil J., Henderson S., Hoover J., Jennings D., Jordan C., Jordan J., RA Kasha J., Kagan L., Kraft C., Levitsky A., Lewis M., Liu X., Lopez J., RA Ma D., Majoros W., McDaniel J., Murphy S., Newman M., Nguyen T., Nguyen N., RA Nodell M., Pan S., Peck J., Peterson M., Rowe W., Sanders R., Scott J., RA Simpson M., Smith T., Sprague A., Stockwell T., Turner R., Venter E., RA Wang M., Wen M., Wu D., Wu M., Xia A., Zandieh A., Zhu X.; RT "The sequence of the human genome."; RL Science 291:1304-1351(2001). RN [2] {ECO:0000313|EMBL:EAX06399.1} RP NUCLEOTIDE SEQUENCE. RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|Ensembl:ENSP00000359871.5, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., RA Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., RA Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., RA Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R., RA Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., RA Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S., RA Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., RA Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., RA Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., RA Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S., McLaren S., Milne S., RA Mistry S., Moore M.J., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., RA Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., RA Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., RA Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., RA Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., RA Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., RA Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., RA Coulson A., Vaudin M., Sulston J.E., Durbin R., Hubbard T., Wooster R., RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., RA Beck S., Rogers J., Bentley D.R., Banerjee R., Bryant S.P., Burford D.C., RA Burrill W.D., Clegg S.M., Dhami P., Dovey O., Faulkner L.M., Gribble S.M., RA Langford C.F., Pandian R.D., Porter K.M., Prigmore E.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [4] {ECO:0007829|PubMed:19608861} 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 [5] {ECO:0007829|PubMed:21269460} 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., Burckstummer 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 [6] {ECO:0007829|PubMed:24275569} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. 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 [7] {ECO:0007829|PubMed:25944712} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; 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 [8] {ECO:0000313|Ensembl:ENSP00000359871.5} RP IDENTIFICATION. RG Ensembl; RL Submitted (NOV-2023) to UniProtKB. 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:0000256|ARBA:ARBA00001337}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43449; CC Evidence={ECO:0000256|ARBA:ARBA00001337}; CC -!- CATALYTIC ACTIVITY: CC Reaction=H(+) + hexanoyl-CoA + oxidized [electron-transfer CC flavoprotein] = (2E)-hexenoyl-CoA + reduced [electron-transfer CC flavoprotein]; Xref=Rhea:RHEA:43464, Rhea:RHEA-COMP:10685, Rhea:RHEA- CC COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, CC ChEBI:CHEBI:62077, ChEBI:CHEBI:62620; CC Evidence={ECO:0000256|ARBA:ARBA00001483}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43465; CC Evidence={ECO:0000256|ARBA:ARBA00001483}; CC -!- CATALYTIC ACTIVITY: CC Reaction=H(+) + octanoyl-CoA + oxidized [electron-transfer CC flavoprotein] = (2E)-octenoyl-CoA + reduced [electron-transfer CC flavoprotein]; Xref=Rhea:RHEA:48180, Rhea:RHEA-COMP:10685, Rhea:RHEA- CC COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57386, ChEBI:CHEBI:57692, CC ChEBI:CHEBI:58307, ChEBI:CHEBI:62242; CC Evidence={ECO:0000256|ARBA:ARBA00001547}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48181; CC Evidence={ECO:0000256|ARBA:ARBA00001547}; CC -!- CATALYTIC ACTIVITY: CC Reaction=H(+) + oxidized [electron-transfer flavoprotein] + pentanoyl- CC CoA = (2E)-pentenoyl-CoA + reduced [electron-transfer flavoprotein]; CC Xref=Rhea:RHEA:43456, Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57389, ChEBI:CHEBI:57692, CC ChEBI:CHEBI:58307, ChEBI:CHEBI:86160; CC Evidence={ECO:0000256|ARBA:ARBA00023695}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43457; CC Evidence={ECO:0000256|ARBA:ARBA00023695}; 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:0000256|ARBA:ARBA00001236}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47317; CC Evidence={ECO:0000256|ARBA:ARBA00001236}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a medium-chain 2,3-saturated fatty acyl-CoA + H(+) + oxidized CC [electron-transfer flavoprotein] = a medium-chain (2E)-enoyl-CoA + CC reduced [electron-transfer flavoprotein]; Xref=Rhea:RHEA:14477, CC Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:83723, CC ChEBI:CHEBI:83726; EC=1.3.8.7; CC Evidence={ECO:0000256|ARBA:ARBA00034058}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14478; CC Evidence={ECO:0000256|ARBA:ARBA00034058}; 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:0000256|ARBA:ARBA00000121}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48177; CC Evidence={ECO:0000256|ARBA:ARBA00000121}; CC -!- CATALYTIC ACTIVITY: CC Reaction=dodecanoyl-CoA + H(+) + oxidized [electron-transfer CC flavoprotein] = (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 -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|ARBA:ARBA00001974, CC ECO:0000256|PIRSR:PIRSR634180-3, ECO:0000256|RuleBase:RU362125}; CC -!- PATHWAY: Lipid metabolism; mitochondrial fatty acid beta-oxidation. CC {ECO:0000256|ARBA:ARBA00005198}. CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix CC {ECO:0000256|ARBA:ARBA00004305}. CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family. CC {ECO:0000256|ARBA:ARBA00009347, ECO:0000256|RuleBase:RU362125}. 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; AL357314; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471059; EAX06399.1; -; Genomic_DNA. DR RefSeq; NP_001272972.1; NM_001286043.1. DR IntAct; Q5T4U5; 2. DR ProteomicsDB; 64489; -. DR Antibodypedia; 1642; 521 antibodies from 38 providers. DR DNASU; 34; -. DR Ensembl; ENST00000370834.9; ENSP00000359871.5; ENSG00000117054.15. DR GeneID; 34; -. DR UCSC; uc009wbr.5; human. DR CTD; 34; -. DR HGNC; HGNC:89; ACADM. DR VEuPathDB; HostDB:ENSG00000117054; -. DR GeneTree; ENSGT00940000158429; -. DR OrthoDB; 275353at2759; -. DR UniPathway; UPA00660; -. DR BioGRID-ORCS; 34; 15 hits in 1160 CRISPR screens. DR ChiTaRS; ACADM; human. DR GenomeRNAi; 34; -. DR Proteomes; UP000005640; Chromosome 1. DR Bgee; ENSG00000117054; Expressed in jejunal mucosa and 206 other cell types or tissues. DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell. DR GO; GO:0005739; C:mitochondrion; IDA:HPA. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule. DR GO; GO:0070991; F:medium-chain-acyl-CoA dehydrogenase activity; IEA:UniProtKB-EC. DR GO; GO:0006635; P:fatty acid beta-oxidation; IEA:InterPro. DR CDD; cd01157; MCAD; 1. DR Gene3D; 1.10.540.10; Acyl-CoA dehydrogenase/oxidase, N-terminal domain; 1. DR Gene3D; 2.40.110.10; Butyryl-CoA Dehydrogenase, subunit A, domain 2; 1. DR Gene3D; 1.20.140.10; Butyryl-CoA Dehydrogenase, subunit A, domain 3; 1. DR InterPro; IPR006089; Acyl-CoA_DH_CS. DR InterPro; IPR006091; Acyl-CoA_Oxase/DH_mid-dom. DR InterPro; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf. DR InterPro; IPR036250; AcylCo_DH-like_C. DR InterPro; IPR009075; AcylCo_DH/oxidase_C. DR InterPro; IPR013786; AcylCoA_DH/ox_N. DR InterPro; IPR037069; AcylCoA_DH/ox_N_sf. DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom_sf. DR InterPro; IPR034180; MCAD. DR PANTHER; PTHR48083:SF2; MEDIUM-CHAIN SPECIFIC ACYL-COA DEHYDROGENASE, MITOCHONDRIAL; 1. DR PANTHER; PTHR48083; MEDIUM-CHAIN SPECIFIC ACYL-COA DEHYDROGENASE, MITOCHONDRIAL-RELATED; 1. DR Pfam; PF00441; Acyl-CoA_dh_1; 1. DR Pfam; PF02770; Acyl-CoA_dh_M; 1. DR Pfam; PF02771; Acyl-CoA_dh_N; 2. 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 1: Evidence at protein level; KW Acetylation {ECO:0000256|ARBA:ARBA00022990}; KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR634180-3}; KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630, KW ECO:0000256|RuleBase:RU362125}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, KW ECO:0000256|RuleBase:RU362125}; KW Proteomics identification {ECO:0007829|EPD:Q5T4U5, KW ECO:0007829|MaxQB:Q5T4U5}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}. FT DOMAIN 42..96 FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal" FT /evidence="ECO:0000259|Pfam:PF02771" FT DOMAIN 127..184 FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal" FT /evidence="ECO:0000259|Pfam:PF02771" FT DOMAIN 190..288 FT /note="Acyl-CoA oxidase/dehydrogenase middle" FT /evidence="ECO:0000259|Pfam:PF02770" FT DOMAIN 300..447 FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal" FT /evidence="ECO:0000259|Pfam:PF00441" FT ACT_SITE 434 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR634180-1" FT BINDING 191..200 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000256|PIRSR:PIRSR634180-3" FT BINDING 200 FT /ligand="octanoyl-CoA" FT /ligand_id="ChEBI:CHEBI:57386" FT /evidence="ECO:0000256|PIRSR:PIRSR634180-2" FT BINDING 224..226 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000256|PIRSR:PIRSR634180-3" FT BINDING 249 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR634180-2" FT BINDING 311..314 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR634180-2" FT BINDING 339..341 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000256|PIRSR:PIRSR634180-3" FT BINDING 349..350 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000256|PIRSR:PIRSR634180-3" FT BINDING 407..411 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000256|PIRSR:PIRSR634180-3" FT BINDING 435 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR634180-2" FT BINDING 436..438 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000256|PIRSR:PIRSR634180-3" FT BINDING 446 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR634180-2" SQ SEQUENCE 454 AA; 50271 MW; E71D822F35F96E2A CRC64; MAAGFGRCCR VLRSISRFHW RSQHTKANRQ REPGLGFSFE FTEQQKEFQA TARKFAREEI IPVAAEYDKT GEYPVPLIRR AWELGLMNTH IPENCDYSVC PLLEACTLYL DAFFLLLTGS NLNLHLNLGG LGLGTFDACL ISEELAYGCT GVQTAIEGNS LGQMPIIIAG NDQQKKKYLG RMTEEPLMCA YCVTEPGAGS DVAGIKTKAE KKGDEYIING QKMWITNGGK ANWYFLLARS DPDPKAPANK AFTGFIVEAD TPGIQIGRKE LNMGQRCSDT RGIVFEDVKV PKENVLIGDG AGFKVAMGAF DKTRPVVAAG AVGLAQRALD EATKYALERK TFGKLLVEHQ AISFMLAEMA MKVELARMSY QRAAWEVDSG RRNTYYASIA KAFAGDIANQ LATDAVQILG GNGFNTEYPV EKLMRDAKIY QIYEGTSQIQ RLIVAREHID KYKN //