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Database: UniProt
Entry: A0A091P6F7_LEPDC
LinkDB: A0A091P6F7_LEPDC
Original site: A0A091P6F7_LEPDC 
ID   A0A091P6F7_LEPDC        Unreviewed;       406 AA.
AC   A0A091P6F7;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Long-chain specific acyl-CoA dehydrogenase, mitochondrial {ECO:0000256|ARBA:ARBA00014123};
DE            EC=1.3.8.8 {ECO:0000256|ARBA:ARBA00012040};
DE   Flags: Fragment;
GN   ORFNames=N330_06410 {ECO:0000313|EMBL:KFQ03532.1};
OS   Leptosomus discolor (Madagascar cuckoo roller) (Cuculus discolor).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Coraciiformes; Leptosomidae; Leptosomus.
OX   NCBI_TaxID=188344 {ECO:0000313|EMBL:KFQ03532.1, ECO:0000313|Proteomes:UP000053001};
RN   [1] {ECO:0000313|EMBL:KFQ03532.1, ECO:0000313|Proteomes:UP000053001}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N330 {ECO:0000313|EMBL:KFQ03532.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(5Z)-tetradecenoyl-CoA + H(+) + oxidized [electron-transfer
CC         flavoprotein] = (2E,5Z)-tetradecadienoyl-CoA + reduced [electron-
CC         transfer flavoprotein]; Xref=Rhea:RHEA:47448, Rhea:RHEA-COMP:10685,
CC         Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692,
CC         ChEBI:CHEBI:58307, ChEBI:CHEBI:84650, ChEBI:CHEBI:87701;
CC         Evidence={ECO:0000256|ARBA:ARBA00000392};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47449;
CC         Evidence={ECO:0000256|ARBA:ARBA00000392};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(9Z)-octadecenoyl-CoA + H(+) + oxidized [electron-transfer
CC         flavoprotein] = (2E,9Z)-octadecadienoyl-CoA + reduced [electron-
CC         transfer flavoprotein]; Xref=Rhea:RHEA:47300, Rhea:RHEA-COMP:10685,
CC         Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57387,
CC         ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:77553;
CC         Evidence={ECO:0000256|ARBA:ARBA00000571};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47301;
CC         Evidence={ECO:0000256|ARBA:ARBA00000571};
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(+) + octadecanoyl-CoA + oxidized [electron-transfer
CC         flavoprotein] = (2E)-octadecenoyl-CoA + reduced [electron-transfer
CC         flavoprotein]; Xref=Rhea:RHEA:47240, Rhea:RHEA-COMP:10685, Rhea:RHEA-
CC         COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57394, ChEBI:CHEBI:57692,
CC         ChEBI:CHEBI:58307, ChEBI:CHEBI:71412;
CC         Evidence={ECO:0000256|ARBA:ARBA00000364};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47241;
CC         Evidence={ECO:0000256|ARBA:ARBA00000364};
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] +
CC         tetracosanoyl-CoA = (2E)-tetracosenoyl-CoA + reduced [electron-
CC         transfer flavoprotein]; Xref=Rhea:RHEA:47232, Rhea:RHEA-COMP:10685,
CC         Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692,
CC         ChEBI:CHEBI:58307, ChEBI:CHEBI:65052, ChEBI:CHEBI:74693;
CC         Evidence={ECO:0000256|ARBA:ARBA00001765};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47233;
CC         Evidence={ECO:0000256|ARBA:ARBA00001765};
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 long-chain 2,3-saturated fatty acyl-CoA + H(+) + oxidized
CC         [electron-transfer flavoprotein] = a long-chain (2E)-enoyl-CoA +
CC         reduced [electron-transfer flavoprotein]; Xref=Rhea:RHEA:17721,
CC         Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:83721,
CC         ChEBI:CHEBI:83727; EC=1.3.8.8;
CC         Evidence={ECO:0000256|ARBA:ARBA00001740};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17722;
CC         Evidence={ECO:0000256|ARBA:ARBA00001740};
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=docosanoyl-CoA + H(+) + oxidized [electron-transfer
CC         flavoprotein] = (2E)-docosenoyl-CoA + reduced [electron-transfer
CC         flavoprotein]; Xref=Rhea:RHEA:47228, Rhea:RHEA-COMP:10685, Rhea:RHEA-
CC         COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307,
CC         ChEBI:CHEBI:65059, ChEBI:CHEBI:74692;
CC         Evidence={ECO:0000256|ARBA:ARBA00000286};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47229;
CC         Evidence={ECO:0000256|ARBA:ARBA00000286};
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=eicosanoyl-CoA + H(+) + oxidized [electron-transfer
CC         flavoprotein] = (2E)-eicosenoyl-CoA + reduced [electron-transfer
CC         flavoprotein]; Xref=Rhea:RHEA:47236, Rhea:RHEA-COMP:10685, Rhea:RHEA-
CC         COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57380, ChEBI:CHEBI:57692,
CC         ChEBI:CHEBI:58307, ChEBI:CHEBI:74691;
CC         Evidence={ECO:0000256|ARBA:ARBA00000733};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47237;
CC         Evidence={ECO:0000256|ARBA:ARBA00000733};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974,
CC         ECO:0000256|RuleBase:RU362125};
CC   -!- PATHWAY: Lipid metabolism; mitochondrial fatty acid beta-oxidation.
CC       {ECO:0000256|ARBA:ARBA00005198}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
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}.
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DR   EMBL; KK669145; KFQ03532.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091P6F7; -.
DR   PhylomeDB; A0A091P6F7; -.
DR   UniPathway; UPA00660; -.
DR   Proteomes; UP000053001; Unassembled WGS sequence.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004466; F:long-chain-acyl-CoA dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0042758; P:long-chain fatty acid catabolic process; IEA:InterPro.
DR   CDD; cd01160; LCAD; 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; IPR034179; LCAD.
DR   PANTHER; PTHR43884; ACYL-COA DEHYDROGENASE; 1.
DR   PANTHER; PTHR43884:SF12; COMPLEX I ASSEMBLY FACTOR ACAD9, 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   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   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU362125};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|RuleBase:RU362125};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU362125};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053001};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT   DOMAIN          32..142
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          146..243
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          255..403
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFQ03532.1"
FT   NON_TER         406
FT                   /evidence="ECO:0000313|EMBL:KFQ03532.1"
SQ   SEQUENCE   406 AA;  45242 MW;  DE5FABF63E36734C CRC64;
     SPLQTEQHGT KRPEPSSAKS LIDIGTRRIF SSDHDIFRES ARKFFQEEVL PFHAEWEKDG
     QVSRELWEKA GQQGLLGVAI AEKHGGIGAD ILSSAVVWEE QMYVNCTGPG FSLHSDIVMP
     YIANYGSEEQ IKRFIPEMIA GKCIGAIAMT EPGAGSDLQG IRTYAKKDGS DWILNGSKVF
     ITNGWMSDVV IVVAVTNREA RSPAHGISLF LVENGTKGFI KGRKLNKIGL KAQDTAELFF
     EDVRLPASAL LGKENKGFYY LMAELPQERL LIADMALASC EFMFEETRNY VKQRKAFGKT
     VAHLQTVQHK LAEMKTQICV GRAFMDNCLQ LHADKRLDSS TASMAKYWSS DLQNSIATQC
     VQLHGGWGYM WEYPIAKAFV DARVQPIYGG TNEIMKELIA RDIVSD
//
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