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Database: UniProt
Entry: A0A087YA63_POEFO
LinkDB: A0A087YA63_POEFO
Original site: A0A087YA63_POEFO 
ID   A0A087YA63_POEFO        Unreviewed;       782 AA.
AC   A0A087YA63;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   RecName: Full=Acyl-CoA dehydrogenase family member 11 {ECO:0000256|ARBA:ARBA00040622};
OS   Poecilia formosa (Amazon molly) (Limia formosa).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC   Poecilia.
OX   NCBI_TaxID=48698 {ECO:0000313|Ensembl:ENSPFOP00000014916.1, ECO:0000313|Proteomes:UP000028760};
RN   [1] {ECO:0000313|Proteomes:UP000028760}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=female {ECO:0000313|Proteomes:UP000028760};
RA   Schartl M., Warren W.;
RL   Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSPFOP00000014916.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + hexacosanoyl-CoA + oxidized [electron-transfer
CC         flavoprotein] = (2E)-hexacosenoyl-CoA + reduced [electron-transfer
CC         flavoprotein]; Xref=Rhea:RHEA:48216, Rhea:RHEA-COMP:10685, Rhea:RHEA-
CC         COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307,
CC         ChEBI:CHEBI:64868, ChEBI:CHEBI:74281;
CC         Evidence={ECO:0000256|ARBA:ARBA00036134};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48217;
CC         Evidence={ECO:0000256|ARBA:ARBA00036134};
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         tricosanoyl-CoA = (2E)-tricosenoyl-CoA + reduced [electron-transfer
CC         flavoprotein]; Xref=Rhea:RHEA:48220, Rhea:RHEA-COMP:10685, Rhea:RHEA-
CC         COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307,
CC         ChEBI:CHEBI:90118, ChEBI:CHEBI:90119;
CC         Evidence={ECO:0000256|ARBA:ARBA00036394};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48221;
CC         Evidence={ECO:0000256|ARBA:ARBA00036394};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2,3-saturated acyl-CoA + H(+) + oxidized [electron-transfer
CC         flavoprotein] = a (2E)-enoyl-CoA + reduced [electron-transfer
CC         flavoprotein]; Xref=Rhea:RHEA:44704, Rhea:RHEA-COMP:10685, Rhea:RHEA-
CC         COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307,
CC         ChEBI:CHEBI:58856, ChEBI:CHEBI:65111;
CC         Evidence={ECO:0000256|ARBA:ARBA00036627};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44705;
CC         Evidence={ECO:0000256|ARBA:ARBA00036627};
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=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   -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC       {ECO:0000256|ARBA:ARBA00005005}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004370}.
CC       Mitochondrion membrane {ECO:0000256|ARBA:ARBA00004325}.
CC   -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00009347}.
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DR   EMBL; AYCK01006222; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AYCK01006223; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; A0A087YA63; -.
DR   STRING; 48698.ENSPFOP00000014916; -.
DR   Ensembl; ENSPFOT00000014938.1; ENSPFOP00000014916.1; ENSPFOG00000014717.1.
DR   eggNOG; KOG1469; Eukaryota.
DR   GeneTree; ENSGT00940000160993; -.
DR   OMA; LHGGHFE; -.
DR   Proteomes; UP000028760; Unassembled WGS sequence.
DR   GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
DR   CDD; cd05154; ACAD10_11_N-like; 1.
DR   CDD; cd01155; ACAD_FadE2; 1.
DR   Gene3D; 3.90.1200.10; -; 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; IPR041726; ACAD10_11_N.
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; IPR002575; Aminoglycoside_PTrfase.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   PANTHER; PTHR48083:SF13; ACYL-COA DEHYDROGENASE FAMILY MEMBER 11; 1.
DR   PANTHER; PTHR48083; MEDIUM-CHAIN SPECIFIC ACYL-COA DEHYDROGENASE, 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   Pfam; PF01636; APH; 1.
DR   SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028760}.
FT   DOMAIN          36..251
FT                   /note="Aminoglycoside phosphotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF01636"
FT   DOMAIN          381..500
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          504..608
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          620..767
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   782 AA;  86991 MW;  51CA2992354789E6 CRC64;
     MEDQLTSVRE QHKFNVGNLQ RYLYEKSLVS KNDTLTVRQY SAGQSNPTFL IQTPSRSYVL
     RKKPPGELLP GAHKVDREYR VQTALFSAGF PVPQPLLFCN EAEVIGTEFY LMEHHEQGRI
     FRDFQLPGMS PAQRTSVYTA AVENLAKLHS LDLPSLKLEG FGRGPGYCRR QVSTWTKQYT
     ASAHRDIPAV NELCDWLMRN LPDKDDEVTL VHGDYRLDNL IFHPTETRVM ASLDWELSTT
     GSPLADLAFF LVPLYCPTGL NIKSFIFNLQ EVEAGIPSPS DLISIYCRCR GIPSVSLPPL
     NFYLALSLFK AAAISQGIYA RYLLGNASAP DAAQYGQNVE PLAKAALQLA KSLSHVSDVF
     PASPLAGPAK DRLFPQTAKG QAVLQQVKDF MQQYVLPAQQ EVAEYYTKHS QSPLRWHAPK
     IIEDLKEKAK QAGLWNLFLP AVSGLTQLDY AYIAEEMGRC LFAPEVFNCQ APDTGNMEVL
     HMFGTEEQKK KWLEPLLSGE IRSCFCMTEP DVASSDGANM ECRLHRDKTT YIINGKKWWS
     SGAGSATCKV AIVMCRSSSE HGNSRHGQHS MVLVPMDTPG VKLIRPLTVF GHDDAIHGGH
     FEVHFENVRV PASNMILGEG RGFEIAQRRL GPGRLHHCMR AVGCAEQALE LLCQRAASRR
     TFGKNLYQHE VIAHWIAECR LMIEQTRLLT LSAAHALDAL GSRAARKQIA MIKVAAARMV
     CKVVDCAIQV HGGAGVSGDF PLAQMYSYAR TLRIADGPDE VHLSSIAILE LKDQLKQARA
     RL
//
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