ACAD2_CAEBR
ID ACAD2_CAEBR Reviewed; 408 AA.
AC A8WP91;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Probable medium-chain specific acyl-CoA dehydrogenase 2, mitochondrial {ECO:0000250|UniProtKB:Q22347};
DE Short=MCAD {ECO:0000250|UniProtKB:Q22347};
DE EC=1.3.8.7;
DE Flags: Precursor;
GN ORFNames=CBG00953;
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:CAP22297.2}
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}.
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DR EMBL; HE600951; CAP22297.2; -; Genomic_DNA.
DR AlphaFoldDB; A8WP91; -.
DR SMR; A8WP91; -.
DR STRING; 6238.CBG00953; -.
DR WormBase; CBG00953; CBP46189; WBGene00024257; -.
DR eggNOG; KOG0140; Eukaryota.
DR HOGENOM; CLU_018204_0_2_1; -.
DR InParanoid; A8WP91; -.
DR OMA; WRAAWMG; -.
DR OrthoDB; 589058at2759; -.
DR UniPathway; UPA00660; -.
DR Proteomes; UP000008549; Chromosome II.
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.
PE 3: Inferred from homology;
KW FAD; Fatty acid metabolism; Flavoprotein; Lipid metabolism; Mitochondrion;
KW Oxidoreductase; Reference proteome; Transit peptide.
FT TRANSIT 1..5
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 6..408
FT /note="Probable medium-chain specific acyl-CoA
FT dehydrogenase 2, mitochondrial"
FT /evidence="ECO:0000250|UniProtKB:Q22347"
FT /id="PRO_0000395328"
FT ACT_SITE 382
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P11310"
FT BINDING 143..152
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P11310"
FT BINDING 152
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11310"
FT BINDING 176..178
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P11310"
FT BINDING 263..266
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11310"
FT BINDING 291..293
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P11310"
FT BINDING 301..302
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P11310"
FT BINDING 355..359
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P11310"
FT BINDING 383
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11310"
FT BINDING 384..386
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P11310"
FT BINDING 394
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11310"
SQ SEQUENCE 408 AA; 44608 MW; 0880122A2AB967D3 CRC64;
MLSRLARTQI SRSALLSQTR QLSFDLNETQ KEIQAAALKF SKEVLVPNAA KFDESGEFPW
EIIRQAHSLG LMNPQIPEKY GGPGMTTLET TLIVEALSYG CTGLQLGIMG PSLAIAPVYI
AGNEEQKKKY LGALAAEPII ASYCVTEPGA GSDVNGVKTK CEKKGNEYII NGSKAWITGG
GHAKWFFVLA RSDPNPKTPA GKAFTAFIVD GDTSGITRGK KEKNMGQRCS DTRTITFEDV
RVPEENVLGP PGAGFKVAMS AFDMTRPGVA AGALGLSWRC LDESAKYALQ RKAFGTEIAN
HQAVQFMLSD MAINLELARL ITYKSATDVD NGVRSSYNAS KSASQRIPRI RRLLMLFRCN
GFNSEYPVEK LMRDAKIYQI YEGTSQIQRI VISRMLLGHV AQNGTSRM
