ACD11_PONAB
ID ACD11_PONAB Reviewed; 781 AA.
AC Q5R778; Q5RFD1;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Acyl-CoA dehydrogenase family member 11;
DE Short=ACAD-11;
DE EC=1.3.8.- {ECO:0000250|UniProtKB:Q709F0};
GN Name=ACAD11;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Acyl-CoA dehydrogenase, that exhibits maximal activity
CC towards saturated C22-CoA. Probably participates in beta-oxydation and
CC energy production but could also play a role in the metabolism of
CC specific fatty acids to control fatty acids composition of cellular
CC lipids in brain. {ECO:0000250|UniProtKB:Q709F0}.
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:0000250|UniProtKB:Q709F0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44705;
CC Evidence={ECO:0000250|UniProtKB:Q709F0};
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:0000250|UniProtKB:Q709F0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47229;
CC Evidence={ECO:0000250|UniProtKB:Q709F0};
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:0000250|UniProtKB:Q709F0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47233;
CC Evidence={ECO:0000250|UniProtKB:Q709F0};
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:0000250|UniProtKB:Q709F0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47237;
CC Evidence={ECO:0000250|UniProtKB:Q709F0};
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:0000250|UniProtKB:Q709F0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48217;
CC Evidence={ECO:0000250|UniProtKB:Q709F0};
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:0000250|UniProtKB:Q709F0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48221;
CC Evidence={ECO:0000250|UniProtKB:Q709F0};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:Q709F0};
CC -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC {ECO:0000250|UniProtKB:Q709F0}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q709F0}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000250|UniProtKB:Q80XL6}.
CC Mitochondrion membrane {ECO:0000250|UniProtKB:Q709F0}.
CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; CR857227; CAH89526.1; -; mRNA.
DR EMBL; CR860240; CAH92382.1; -; mRNA.
DR RefSeq; NP_001126403.1; NM_001132931.2.
DR AlphaFoldDB; Q5R778; -.
DR SMR; Q5R778; -.
DR STRING; 9601.ENSPPYP00000015783; -.
DR Ensembl; ENSPPYT00000016405; ENSPPYP00000015783; ENSPPYG00000014106.
DR GeneID; 100173386; -.
DR KEGG; pon:100173386; -.
DR CTD; 84129; -.
DR eggNOG; KOG1469; Eukaryota.
DR GeneTree; ENSGT00940000160993; -.
DR HOGENOM; CLU_007526_3_0_1; -.
DR InParanoid; Q5R778; -.
DR OMA; IWAPQIF; -.
DR OrthoDB; 1028522at2759; -.
DR TreeFam; TF333953; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000001595; Chromosome 3.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0070991; F:medium-chain-acyl-CoA dehydrogenase activity; IEA:Ensembl.
DR GO; GO:0017099; F:very-long-chain-acyl-CoA dehydrogenase activity; IEA:Ensembl.
DR GO; GO:0033539; P:fatty acid beta-oxidation using acyl-CoA dehydrogenase; IEA:Ensembl.
DR CDD; cd05154; ACAD10_11_N-like; 1.
DR Gene3D; 1.10.540.10; -; 1.
DR Gene3D; 2.40.110.10; -; 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.
DR InterPro; IPR002575; Aminoglycoside_PTrfase.
DR InterPro; IPR011009; Kinase-like_dom_sf.
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; SSF47203; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR SUPFAM; SSF56645; SSF56645; 1.
PE 2: Evidence at transcript level;
KW Acetylation; FAD; Fatty acid metabolism; Flavoprotein; Lipid metabolism;
KW Membrane; Mitochondrion; Oxidoreductase; Peroxisome; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..781
FT /note="Acyl-CoA dehydrogenase family member 11"
FT /id="PRO_0000254147"
FT BINDING 505..515
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 513..515
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 515
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 539..541
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 541
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 630..633
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 658
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250"
FT BINDING 728..732
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250"
FT BINDING 728
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 756
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 757..759
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 759
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT MOD_RES 177
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q80XL6"
FT MOD_RES 325
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q80XL6"
FT MOD_RES 392
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q80XL6"
FT CONFLICT 5
FT /note="A -> T (in Ref. 1; CAH89526)"
FT /evidence="ECO:0000305"
FT CONFLICT 137
FT /note="V -> A (in Ref. 1; CAH92382)"
FT /evidence="ECO:0000305"
FT CONFLICT 723
FT /note="V -> I (in Ref. 1; CAH89526)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 781 AA; 87355 MW; CF99D673654FD3DA CRC64;
MKPGATGESD LAEVLPQHKF DSKSLEAYLN QHLSGFGAER EATLTIAQYR AGKSNPTFYL
QKGFQTYVLR KKPPGSLLPK AHQIDREFKV QKALFSIGFP VPKPILYCSD TSVIGTEFYI
MEHVQGRIFR DLTIPGVSPA ERSALYVAIV ETLAQLHSLN IQSLQLEGYG IGAGYCKRQV
STWTKQYQAA AHQDIPAMQQ LSEWLMKNLP DNDNEENLIH GDFRLDNIIF HPKECRVIAV
LDWELSTIGH PLSDLAHFSL FYFWPRTVPM INQGSYSEEN SGIPSMEELI SIYCRCRGIN
SSLPNWNFFL ALSYFKMAGI AQGVYSRYLL GNNSSEDSFL FANIVQPLAE TGLQLSKRTF
STVLPQIDTA GQLFVQTRKG QEVLIKVKHF MKQHILPAEK EVTEFYVQNE NSVDKWGKPL
VIDKLKEMAK AEGLWNLFLP AVSGLSQVDY ALIAEETGKC FFAPDVFNCQ APDTGNMEIL
HLYGSEEQKK QWLEPLLQGN ITSCFCMTEP DVASSDATNI ECSIQREEDS YVINGKKWWS
SGAGNPKCKI AIVLGRTQNT SLSRHKQHSM ILVPMNTPGV EIIRPLSVFG YTDNFHGGHF
EIHFNQVRVP ATNLILGEGR GFEISQGRLG PGRIHHCMRT VGLAERALQI MCERATQRIA
FKKKLYAHEV VAHWIAESRI AIEKIRLLTL KAAHSMDTLG SAGAKKEIAM IKVAAPRAVS
KIVDWAIQVC GGAGVSQDYP LANMYAITRV LRLADGPDEV HLSAIATMEL RDQAKRLTAK
I
