ACD11_RAT
ID ACD11_RAT Reviewed; 779 AA.
AC B3DMA2;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 94.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=14561759; DOI=10.1074/jbc.m305623200;
RA Kikuchi M., Hatano N., Yokota S., Shimozawa N., Imanaka T., Taniguchi H.;
RT "Proteomic analysis of rat liver peroxisome: presence of peroxisome-
RT specific isozyme of Lon protease.";
RL J. Biol. Chem. 279:421-428(2004).
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:0000269|PubMed:14561759}.
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; CH473954; EDL77362.1; -; Genomic_DNA.
DR EMBL; BC167762; AAI67762.1; -; mRNA.
DR RefSeq; NP_001101651.1; NM_001108181.1.
DR AlphaFoldDB; B3DMA2; -.
DR SMR; B3DMA2; -.
DR STRING; 10116.ENSRNOP00000036574; -.
DR iPTMnet; B3DMA2; -.
DR PhosphoSitePlus; B3DMA2; -.
DR jPOST; B3DMA2; -.
DR PaxDb; B3DMA2; -.
DR PeptideAtlas; B3DMA2; -.
DR PRIDE; B3DMA2; -.
DR Ensembl; ENSRNOT00000038383; ENSRNOP00000036574; ENSRNOG00000010940.
DR GeneID; 315973; -.
DR KEGG; rno:315973; -.
DR UCSC; RGD:1306270; rat.
DR CTD; 84129; -.
DR RGD; 1306270; Acad11.
DR eggNOG; KOG1469; Eukaryota.
DR GeneTree; ENSGT00940000160993; -.
DR HOGENOM; CLU_007526_3_0_1; -.
DR InParanoid; B3DMA2; -.
DR OMA; IWAPQIF; -.
DR OrthoDB; 1028522at2759; -.
DR PhylomeDB; B3DMA2; -.
DR Reactome; R-RNO-77289; Mitochondrial Fatty Acid Beta-Oxidation.
DR UniPathway; UPA00659; -.
DR PRO; PR:B3DMA2; -.
DR Proteomes; UP000002494; Chromosome 8.
DR Proteomes; UP000234681; Chromosome 8.
DR Bgee; ENSRNOG00000010940; Expressed in liver and 18 other tissues.
DR Genevisible; B3DMA2; RN.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0031966; C:mitochondrial membrane; ISO:RGD.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0005777; C:peroxisome; IDA:HGNC-UCL.
DR GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0004466; F:long-chain-acyl-CoA dehydrogenase activity; ISO:RGD.
DR GO; GO:0070991; F:medium-chain-acyl-CoA dehydrogenase activity; ISO:RGD.
DR GO; GO:0017099; F:very-long-chain-acyl-CoA dehydrogenase activity; ISO:RGD.
DR GO; GO:0033539; P:fatty acid beta-oxidation using acyl-CoA dehydrogenase; ISO:RGD.
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 1: Evidence at protein level;
KW Acetylation; FAD; Fatty acid metabolism; Flavoprotein; Lipid metabolism;
KW Membrane; Mitochondrion; Oxidoreductase; Peroxisome; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..779
FT /note="Acyl-CoA dehydrogenase family member 11"
FT /id="PRO_0000385188"
FT BINDING 503..513
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 511..513
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
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 537..539
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 539
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 628..631
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 656
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250"
FT BINDING 726..730
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250"
FT BINDING 726
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 754
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 755..757
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 757
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 175
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q80XL6"
FT MOD_RES 210
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80XL6"
FT MOD_RES 323
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q80XL6"
FT MOD_RES 368
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q80XL6"
FT MOD_RES 390
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q80XL6"
FT MOD_RES 765
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q80XL6"
SQ SEQUENCE 779 AA; 87371 MW; EB546C2A4FB29FA6 CRC64;
MEMDVTRDTV EVLPQHKFDI RSLEAYLNQH LPGFGSDHRA VLTVTQYRSG QSNPTFFLQK
GSQAYVLRKK PPGSLLPKAH KIDREFKVQK ALFSVGFPVP KPLLYCSNAS IIGTEFYVME
HVQGRIFRDF SIPGVSPAER AAIYVSLVET LAWLHSLDIH SLGLDRYGTG VGYCKRQVST
WTKQYQASAH QSIPAMDQLS TWLMRNLPDS DNEECLVHGD FKLDNIVFHP KECRVIAVLD
WELSTFGHPL SDLAHLSLFY FWPRTLPMIN RGSHIQENTG IPLMEELISI YCRRRGIDPN
LPNWNFFMAL SFFKLAGIAQ GVYSRYLMGN NSSEDSFLTA NTVQPLAETG LQLSRRTLST
VPPQADAKSR LFAQSRRGQE VLTRVKQFMK QHVFPAEKEV AEYYAQNGNS AEKWEHPLVI
EKLKEMAKAE GLWNLFLPAV SGLSQVDYAL IAEETGKCFF APDVFNCQAP DTGNMEVLHL
YGSEQQKQQW LEPLLRGDIT SVFCMTEPNV SSSDATNMEC SIQRDGGSYI VHGKKWWSSG
AGNPKCKIAV VLGRTESPSV SRHKVHSMIL VPMDTPGVEL IRPLSVFGYM DNVHGGHWEV
HFNHVRVPAS NLILGEGRGF EISQGRLGPG RIHHCMRSVG LAERILQIMC DRAVQREAFG
KKLYEHEVVA HWIAKSRIAI EEIRLLTLKA AHSIDTLGSA AARKEIAMIK VAAPKAVCKI
ADRAIQVHGG AGVSQDYPLA NMYAIIRTLR LADGPDEVHL SAIAKMELQD QARQLKARM
