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Database: UniProt
Entry: B3S878_TRIAD
LinkDB: B3S878_TRIAD
Original site: B3S878_TRIAD 
ID   B3S878_TRIAD            Unreviewed;       604 AA.
AC   B3S878;
DT   02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   02-SEP-2008, sequence version 1.
DT   24-JAN-2024, entry version 70.
DE   RecName: Full=Very long-chain specific acyl-CoA dehydrogenase, mitochondrial {ECO:0000256|ARBA:ARBA00040902};
DE            EC=1.3.8.9 {ECO:0000256|ARBA:ARBA00039034};
GN   ORFNames=TRIADDRAFT_30874 {ECO:0000313|EMBL:EDV21151.1};
OS   Trichoplax adhaerens (Trichoplax reptans).
OC   Eukaryota; Metazoa; Placozoa; Uniplacotomia; Trichoplacea; Trichoplacidae;
OC   Trichoplax.
OX   NCBI_TaxID=10228 {ECO:0000313|EMBL:EDV21151.1, ECO:0000313|Proteomes:UP000009022};
RN   [1] {ECO:0000313|EMBL:EDV21151.1, ECO:0000313|Proteomes:UP000009022}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Grell-BS-1999 {ECO:0000313|EMBL:EDV21151.1,
RC   ECO:0000313|Proteomes:UP000009022};
RX   PubMed=18719581; DOI=10.1038/nature07191;
RA   Srivastava M., Begovic E., Chapman J., Putnam N.H., Hellsten U.,
RA   Kawashima T., Kuo A., Mitros T., Salamov A., Carpenter M.L.,
RA   Signorovitch A.Y., Moreno M.A., Kamm K., Grimwood J., Schmutz J.,
RA   Shapiro H., Grigoriev I.V., Buss L.W., Schierwater B., Dellaporta S.L.,
RA   Rokhsar D.S.;
RT   "The Trichoplax genome and the nature of placozoans.";
RL   Nature 454:955-960(2008).
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(+) + 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(+) + 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 very-long-chain 2,3-saturated fatty acyl-CoA + H(+) +
CC         oxidized [electron-transfer flavoprotein] = a very-long-chain (2E)-
CC         enoyl-CoA + reduced [electron-transfer flavoprotein];
CC         Xref=Rhea:RHEA:19181, Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307,
CC         ChEBI:CHEBI:83724, ChEBI:CHEBI:83728; EC=1.3.8.9;
CC         Evidence={ECO:0000256|ARBA:ARBA00036538};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19182;
CC         Evidence={ECO:0000256|ARBA:ARBA00036538};
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   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004170};
CC       Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004170}.
CC       Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004637};
CC       Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004637}.
CC   -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00009347, ECO:0000256|RuleBase:RU362125}.
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DR   EMBL; DS985255; EDV21151.1; -; Genomic_DNA.
DR   RefSeq; XP_002116481.1; XM_002116445.1.
DR   AlphaFoldDB; B3S878; -.
DR   STRING; 10228.B3S878; -.
DR   EnsemblMetazoa; TriadT30874; TriadP30874; TriadG30874.
DR   GeneID; 6757693; -.
DR   KEGG; tad:TRIADDRAFT_30874; -.
DR   CTD; 6757693; -.
DR   eggNOG; KOG0137; Eukaryota.
DR   HOGENOM; CLU_018204_11_2_1; -.
DR   InParanoid; B3S878; -.
DR   OMA; LTYMVAG; -.
DR   OrthoDB; 275353at2759; -.
DR   PhylomeDB; B3S878; -.
DR   Proteomes; UP000009022; Unassembled WGS sequence.
DR   GO; GO:0000062; F:fatty-acyl-CoA binding; IBA:GO_Central.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0017099; F:very-long-chain-acyl-CoA dehydrogenase activity; IBA:GO_Central.
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; 2.
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   PANTHER; PTHR43884; ACYL-COA DEHYDROGENASE; 1.
DR   PANTHER; PTHR43884:SF11; VERY LONG-CHAIN SPECIFIC ACYL-COA DEHYDROGENASE, MITOCHONDRIAL; 1.
DR   Pfam; PF21343; ACAD9-ACADV_C; 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.
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}; Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00022792};
KW   Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU362125};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009022};
KW   S-nitrosylation {ECO:0000256|ARBA:ARBA00022799}.
FT   DOMAIN          68..159
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          163..265
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          277..423
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   604 AA;  66960 MW;  6FA24EA3EF467718 CRC64;
     MAINRLRLLS DQPIAIHHMD SSFALGVYCG NVKTQQLFPY PDALDDESKD TVKLMIDPLE
     KYFREVHDAS QCDLDEKLPK KSIEVLKELG ALGMQAPQEY GGMQLKRTQY ARISEIIGSF
     DLSIAVFMAG HQAIGYKGIV LFGNEQQKQK YLPSLATGDK IAAFCLTEPS AGSDANSIRS
     TAVLDDDGKH YILNGNKIWI SNGGIADVMT VFAQVPIKKN DSDKESQAVT AFIVERDFGG
     VTSGPPEKKM GIRSSNTTAV YFDDVKIPVE NVIGKVGEGF KVAMNILNEG RYAMGATMTG
     IIRTLMTKTI EHAKNRVQFG RHLIEYQSIQ EKIAQMGLTH YAVESVAYAV SNNMDRGIKE
     FQVEAAISKV LSSESAWKVS DDCIQILAGM GFMRENQAER FMRDARVCRI FEGANDVLRQ
     FIALNGIQYA GKNMKELQKA LQQPISNFGT LWNQGVKRSK RLIGKADSQE LLEVTAPELS
     DCAKMITQRI EEFGATIEKI LIQHGRNIVD QQFILTRIAN ATIDIYSMAA VLSRASKAIS
     SNLPTADHER LLASTLIDEC CERVEQNLAE AITKKSLDRF TAYSSIAKEV SENEGMATTR
     PLRF
//
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