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Database: UniProt
Entry: A0A1V4K712_PATFA
LinkDB: A0A1V4K712_PATFA
Original site: A0A1V4K712_PATFA 
ID   A0A1V4K712_PATFA        Unreviewed;       431 AA.
AC   A0A1V4K712;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   RecName: Full=Long-chain specific acyl-CoA dehydrogenase, mitochondrial {ECO:0000256|ARBA:ARBA00014123};
DE            EC=1.3.8.8 {ECO:0000256|ARBA:ARBA00012040};
GN   Name=ACADL {ECO:0000313|EMBL:OPJ80214.1};
GN   ORFNames=AV530_002583 {ECO:0000313|EMBL:OPJ80214.1};
OS   Patagioenas fasciata monilis.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Columbiformes; Columbidae; Patagioenas.
OX   NCBI_TaxID=372326 {ECO:0000313|EMBL:OPJ80214.1, ECO:0000313|Proteomes:UP000190648};
RN   [1] {ECO:0000313|EMBL:OPJ80214.1, ECO:0000313|Proteomes:UP000190648}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BTP2013 {ECO:0000313|EMBL:OPJ80214.1};
RC   TISSUE=Blood {ECO:0000313|EMBL:OPJ80214.1};
RA   Soares A.E., Novak B.J., Rice E.S., O'Connell B., Chang D., Weber S.,
RA   Shapiro B.;
RT   "Band-tailed pigeon sequencing and assembly.";
RL   Submitted (FEB-2016) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OPJ80214.1}.
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DR   EMBL; LSYS01004331; OPJ80214.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V4K712; -.
DR   STRING; 372326.A0A1V4K712; -.
DR   UniPathway; UPA00660; -.
DR   Proteomes; UP000190648; 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:UP000190648};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT   DOMAIN          56..166
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          170..267
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          279..427
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   431 AA;  47818 MW;  4A2C68B07C0C5CE8 CRC64;
     MAARLLRLRG LVCAAGSRSF SAPASAQQAE QHGTKRLEPS SAKSLIDIGT RRIFSSDHDI
     FRESARKFFQ EEVLPFHAEW EKDGQVSREL WEKAGQHGLL GVAIAEKHGG IGGDILSSAV
     VWEEQMYVNC TGPGFSLHSD IVMPYIANYG SEEQIKRFIP QMVAGKCIGA IAMTEPGAGS
     DLQGIRTYAK KDGSDWILNG SKVFITNGWM SDVVIVVAIT NREARSPAHG ISLFLVENGT
     KGFIKGRKLQ KIGLKAQDTA ELFFEDVRLP ASALLGKENK GFYYLMAELP QERLLIADMA
     LAGCEFMFEE TRNYVRQRKA FGKTIAHLQT VQHKLAEMKT QICVGRAFMD NCLQLHADKR
     LDSPTASMAK YWSSDLQNSI ATQCVQLHGG WGYMWEYPIA KAFVDARVQP IYGGTNEIMK
     ELIARDIVSD N
//
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