ID ACADM_CAEEL Reviewed; 417 AA. AC Q22347; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 27-MAR-2024, entry version 168. DE RecName: Full=Probable medium-chain specific acyl-CoA dehydrogenase 10, mitochondrial; DE Short=MCAD; DE EC=1.3.8.7; DE Flags: Precursor; GN Name=acdh-10; ORFNames=T08G2.3; OS Caenorhabditis elegans. OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae; OC Caenorhabditis. OX NCBI_TaxID=6239; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Bristol N2; RX PubMed=9851916; DOI=10.1126/science.282.5396.2012; RG The C. elegans sequencing consortium; RT "Genome sequence of the nematode C. elegans: a platform for investigating RT biology."; RL Science 282:2012-2018(1998). RN [2] RP TISSUE SPECIFICITY, AND INDUCTION. RX PubMed=18522834; DOI=10.1016/j.cmet.2008.04.012; RA Srinivasan S., Sadegh L., Elle I.C., Christensen A.G., Faergeman N.J., RA Ashrafi K.; RT "Serotonin regulates C. elegans fat and feeding through independent RT molecular mechanisms."; RL Cell Metab. 7:533-544(2008). CC -!- FUNCTION: This enzyme is specific for acyl chain lengths of 4 to 16. CC {ECO:0000250}. 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 -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250}; CC -!- PATHWAY: Lipid metabolism; mitochondrial fatty acid beta-oxidation. CC -!- SUBUNIT: Homotetramer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}. CC -!- TISSUE SPECIFICITY: Expressed in the epidermis and intestine. CC {ECO:0000269|PubMed:18522834}. CC -!- INDUCTION: By serotonin. {ECO:0000269|PubMed:18522834}. CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family. CC {ECO:0000305}. 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; FO080161; CCD61702.1; -; Genomic_DNA. DR PIR; T16838; T16838. DR RefSeq; NP_001294824.1; NM_001307895.1. DR AlphaFoldDB; Q22347; -. DR SMR; Q22347; -. DR DIP; DIP-25385N; -. DR STRING; 6239.T08G2.3.2; -. DR EPD; Q22347; -. DR PaxDb; 6239-T08G2-3-1; -. DR PeptideAtlas; Q22347; -. DR EnsemblMetazoa; T08G2.3.1; T08G2.3.1; WBGene00020366. DR GeneID; 24104866; -. DR KEGG; cel:CELE_T08G2.3; -. DR UCSC; T08G2.3.1; c. elegans. DR AGR; WB:WBGene00020366; -. DR WormBase; T08G2.3; CE07473; WBGene00020366; acdh-10. DR eggNOG; KOG0140; Eukaryota. DR GeneTree; ENSGT00970000196345; -. DR HOGENOM; CLU_018204_0_2_1; -. DR InParanoid; Q22347; -. DR OMA; KYDLAEH; -. DR OrthoDB; 275353at2759; -. DR PhylomeDB; Q22347; -. DR Reactome; R-CEL-77288; mitochondrial fatty acid beta-oxidation of unsaturated fatty acids. DR Reactome; R-CEL-77346; Beta oxidation of decanoyl-CoA to octanoyl-CoA-CoA. DR Reactome; R-CEL-77348; Beta oxidation of octanoyl-CoA to hexanoyl-CoA. DR UniPathway; UPA00660; -. DR PRO; PR:Q22347; -. DR Proteomes; UP000001940; Chromosome X. DR Bgee; WBGene00020366; Expressed in embryo and 4 other cell types or tissues. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell. DR GO; GO:0005739; C:mitochondrion; HDA:WormBase. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0070991; F:medium-chain-acyl-CoA dehydrogenase activity; IBA:GO_Central. DR GO; GO:0006635; P:fatty acid beta-oxidation; IEA:InterPro. DR GO; GO:0051793; P:medium-chain fatty acid catabolic process; IBA:GO_Central. 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:SF38; MEDIUM-CHAIN SPECIFIC ACYL-COA DEHYDROGENASE 10, MITOCHONDRIAL-RELATED; 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; 1. DR PIRSF; PIRSF016578; HsaA; 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 2: Evidence at transcript level; KW FAD; Fatty acid metabolism; Flavoprotein; Lipid metabolism; Mitochondrion; KW Oxidoreductase; Reference proteome; Transit peptide. FT TRANSIT 1..15 FT /note="Mitochondrion" FT /evidence="ECO:0000250" FT CHAIN 16..417 FT /note="Probable medium-chain specific acyl-CoA FT dehydrogenase 10, mitochondrial" FT /id="PRO_0000000507" FT ACT_SITE 391 FT /note="Proton acceptor" FT /evidence="ECO:0000250" FT BINDING 148..157 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250" FT BINDING 157 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 181..183 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250" FT BINDING 268..271 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 306..307 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250" FT BINDING 364..368 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250" FT BINDING 392 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 393..395 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250" SQ SEQUENCE 417 AA; 44818 MW; 98CE260E72C521BF CRC64; MLSRIATSSL GLSRSATGVI ATQSRQISFD LSETQKEIQD AALKFSKDVL VPNAAKFDES GEFPWEIVRQ AHSLGLMNPQ IPEKYGGPGM TTLETALIVE ALSYGCTGIQ LGIMGPSLAI APVYISGNEE QKKKYLGALA AEPIIASYCV TEPGAGSDVN GVKTKCEKKG DEYIINGSKA WITGGGHAKW FFVLARSDPN PKTPAGKAFT AFIVDGDTPG ITRGKKEKNM GQRCSDTRVI TFEDVRVPAE NVLGAPGAGF KVAMEAFDMT RPGVAAGALG LSWRCLDESA KYALERKAFG TVIANHQAVQ FMLADMAVNL ELARLITYKS ANDVDNKVRS SYNASIAKCF AADTANQAAT NAVQIFGGNG FNSEYPVEKL MRDAKIYQIY EGTSQIQRIV ISRMLLGHFA QNGTSRI //