ACAD1_CAEBR
ID ACAD1_CAEBR Reviewed; 417 AA.
AC A8XNF0;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Probable medium-chain specific acyl-CoA dehydrogenase 1, mitochondrial {ECO:0000250|UniProtKB:Q22347};
DE Short=MCAD {ECO:0000250|UniProtKB:Q22347};
DE EC=1.3.8.7;
DE Flags: Precursor;
GN ORFNames=CBG15946;
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238;
RN [1] {ECO:0000312|EMBL:CAP34381.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16;
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R.M., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
CC -!- FUNCTION: This enzyme is specific for acyl chain lengths of 4 to 16.
CC {ECO:0000250|UniProtKB:P11310}.
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;
CC Evidence={ECO:0000250|UniProtKB:P11310};
CC -!- PATHWAY: Lipid metabolism; mitochondrial fatty acid beta-oxidation.
CC {ECO:0000250|UniProtKB:P11310}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P11310}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000250|UniProtKB:P11310}.
CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC {ECO:0000255}.
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; HE600995; CAP34381.1; -; Genomic_DNA.
DR RefSeq; XP_002643349.1; XM_002643303.1.
DR AlphaFoldDB; A8XNF0; -.
DR SMR; A8XNF0; -.
DR STRING; 6238.CBG15946; -.
DR PRIDE; A8XNF0; -.
DR EnsemblMetazoa; CBG15946.1; CBG15946.1; WBGene00036045.
DR GeneID; 8585343; -.
DR KEGG; cbr:CBG_15946; -.
DR CTD; 8585343; -.
DR WormBase; CBG15946; CBP23278; WBGene00036045; -.
DR eggNOG; KOG0140; Eukaryota.
DR HOGENOM; CLU_018204_0_2_1; -.
DR InParanoid; A8XNF0; -.
DR OMA; AMEELFW; -.
DR OrthoDB; 589058at2759; -.
DR UniPathway; UPA00660; -.
DR Proteomes; UP000008549; Chromosome X.
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; IBA:GO_Central.
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 3: Inferred from homology;
KW FAD; Fatty acid metabolism; Flavoprotein; Lipid metabolism; Mitochondrion;
KW Oxidoreductase; Reference proteome; Transit peptide.
FT TRANSIT 1..13
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 14..417
FT /note="Probable medium-chain specific acyl-CoA
FT dehydrogenase 1, mitochondrial"
FT /evidence="ECO:0000250|UniProtKB:Q22347"
FT /id="PRO_0000395327"
FT ACT_SITE 391
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P11310"
FT BINDING 148..157
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P11310"
FT BINDING 157
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11310"
FT BINDING 181..183
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P11310"
FT BINDING 268..271
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11310"
FT BINDING 296..298
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P11310"
FT BINDING 306..307
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P11310"
FT BINDING 364..368
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P11310"
FT BINDING 392
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11310"
FT BINDING 393..395
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P11310"
FT BINDING 403
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11310"
SQ SEQUENCE 417 AA; 44669 MW; A21A018375E2C863 CRC64;
MLSRFATTSL GLSRSATGVL ASQSRQISFD LSDTQKEIQA AALKFSKEVL VPNAAKFDES
GEFPWEIVRQ AHSLGLMNPQ IPEKYGGPGM TTLETALIVE ALSYGCTGLQ LGIMGPSLAI
APVYIAGNEE QKKKYLGALA AEPIIASYCV TEPGAGSDVN GVKTKCEKKG DEYIINGSKA
WITGGGHAKW FFVLARSDSD PKAPAGKAFT AFIVDGDTPG ISRGKKEKNM GQRCSDTRTI
TFEDVRVPAE NVLGAPGAGF KVAMGAFDMT RPGVAAGALG LAWRCLDESA KYALQRKAFG
TEIANHQAVQ FMLADMAVNL ELARLITYKS ATDVDNKVRS SYNASIAKCF AADTANQAAT
NAVQIFGGNG FNSEYPVEKL MRDAKIYQIY EGTSQIQRIV ISRMLLGHFA QNGTSRI
