ACADM_CAEEL
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 03-AUG-2022, entry version 161.
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}.
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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.T08G2.3.1; -.
DR EPD; Q22347; -.
DR PaxDb; Q22347; -.
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 CTD; 24104866; -.
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; WRAAWMG; -.
DR OrthoDB; 589058at2759; -.
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 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:0003995; F:acyl-CoA dehydrogenase activity; IBA:GO_Central.
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:0033539; P:fatty acid beta-oxidation using acyl-CoA dehydrogenase; IBA:GO_Central.
DR GO; GO:0051793; P:medium-chain fatty acid catabolic process; IBA:GO_Central.
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; 1.
DR SUPFAM; SSF56645; SSF56645; 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
