ID O01590_CAEEL Unreviewed; 985 AA.
AC O01590;
DT 01-JUL-1997, integrated into UniProtKB/TrEMBL.
DT 01-NOV-1999, sequence version 2.
DT 24-JAN-2024, entry version 176.
DE RecName: Full=Acyl-CoA dehydrogenase family member 11 {ECO:0000256|ARBA:ARBA00040622};
GN Name=acds-10 {ECO:0000313|EMBL:CCD67873.1,
GN ECO:0000313|WormBase:K09H11.1};
GN ORFNames=CELE_K09H11.1 {ECO:0000313|EMBL:CCD67873.1}, K09H11.1
GN {ECO:0000313|WormBase:K09H11.1};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000313|EMBL:CCD67873.1, ECO:0000313|Proteomes:UP000001940};
RN [1] {ECO:0000313|EMBL:CCD67873.1, ECO:0000313|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000313|EMBL:CCD67873.1,
RC ECO:0000313|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RA Sulson J.E., Waterston R.;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
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: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
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; BX284605; CCD67873.1; -; Genomic_DNA.
DR PIR; D89057; D89057.
DR RefSeq; NP_504508.1; NM_072107.4.
DR AlphaFoldDB; O01590; -.
DR SMR; O01590; -.
DR DIP; DIP-26721N; -.
DR IntAct; O01590; 3.
DR STRING; 6239.K09H11.1.1; -.
DR EPD; O01590; -.
DR PaxDb; 6239-K09H11-1; -.
DR PeptideAtlas; O01590; -.
DR EnsemblMetazoa; K09H11.1.1; K09H11.1.1; WBGene00019599.
DR GeneID; 178962; -.
DR UCSC; K09H11.1; c. elegans.
DR AGR; WB:WBGene00019599; -.
DR WormBase; K09H11.1; CE21068; WBGene00019599; acds-10.
DR eggNOG; KOG1469; Eukaryota.
DR eggNOG; KOG3085; Eukaryota.
DR GeneTree; ENSGT00940000160993; -.
DR HOGENOM; CLU_007526_2_0_1; -.
DR InParanoid; O01590; -.
DR OMA; KNWNFYM; -.
DR OrthoDB; 276350at2759; -.
DR PhylomeDB; O01590; -.
DR Reactome; R-CEL-77289; Mitochondrial Fatty Acid Beta-Oxidation.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00019599; Expressed in larva and 3 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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:0033539; P:fatty acid beta-oxidation using acyl-CoA dehydrogenase; IBA:GO_Central.
DR CDD; cd05154; ACAD10_11_N-like; 1.
DR CDD; cd01155; ACAD_FadE2; 1.
DR CDD; cd02603; HAD_sEH-N_like; 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 Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 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; IPR036412; HAD-like_sf.
DR InterPro; IPR006439; HAD-SF_hydro_IA.
DR InterPro; IPR011945; HAD-SF_ppase_IA/epoxid_hydro_N.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR023198; PGP-like_dom2.
DR NCBIfam; TIGR02247; HAD-1A3-hyp; 1.
DR NCBIfam; TIGR01509; HAD-SF-IA-v3; 1.
DR PANTHER; PTHR48083:SF35; ACYL-COA DEHYDROGENASE FAMILY MEMBER 10; 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 Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00413; HADHALOGNASE.
DR SFLD; SFLDG01129; C1.5:_HAD__Beta-PGM__Phosphata; 1.
DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
PE 1: Evidence at protein level;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Proteomics identification {ECO:0007829|EPD:O01590,
KW ECO:0007829|PeptideAtlas:O01590};
KW Reference proteome {ECO:0000313|Proteomes:UP000001940}.
FT DOMAIN 250..487
FT /note="Aminoglycoside phosphotransferase"
FT /evidence="ECO:0000259|Pfam:PF01636"
FT DOMAIN 593..712
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 716..818
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 830..978
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 985 AA; 111664 MW; 36DC577D4DAAB0A6 CRC64;
MTIKAVIFDM GGVILPAPMH YWKSIEKTHN LRDGSVVETI ISKDFYPHFK LFETGRLTSE
DLDPLFTHIY NFQNNRVGDI LPIFVEVSSQ IQHTPLLPEM VELIKSLRLA GYRTILITNN
FYTDRARLLP TVPSQVGLLF DDVLESCRLG LRKPDTKIYE LALERSKLHP SDCVFLDDLG
SNLKSAKEMG ITTIKVVSSQ QAIHDLGNIL KLNFSYPPET RDCIPREVLP IEKINELITR
RTGTDNKVET IRKFRHGQSN PTYYIRTVRG SQYVLRKKPS GSLLPKAHQV DREFKIMNAL
QGLVPLPKTL LYDETTLDTS FYLMEYQKGR IFLKPSLPEL TPPERRRVYE EALKTLATIH
SVDYEKVGLQ DFGRTDGYMA RNLKRWSDSY QMAKTEEIQE MIKLEAYLKA NLPKSGKSTI
VHGDFRVDNL IIEENEIKVK GVLDWELSTI GDPLSDLATF LFVYYVPNRM ILLPGLGDYS
ESDLHRMGIP TIKECLELYA KYTNTEVVDP ELWTYYMAFV IFRFASIIQG VYKRSQLKNA
SSTEASQLGP LVRKLAAEGM QMISKVHASK SYGQLTIIPS GMSLKAQKYY EIVREIIQND
VIPLEQELLE YYEEGPHRWT IPHPKIEKLK EKSKSLGAWN LFISEHIDPE QKYGKGLTNV
EYAHICELMG RSIFAPEVFN CQAPDTGNME VLIKYGSEEQ KSKWLTPLLN GEIKSCFAMT
EPDVASSDAT NIQGSIVRVG NEYIINARKW FISNASHPKC RIAIFMGQVS GAKRSRNLQQ
SMILVPMQTE GVKIIRNTHV FGSQDAPGGH PEITFTNVRV PVGNMLLGEG KGFEIAQGRL
GPGRIHHAMR LIGHAERAID VIKDRLLTRI AFGRKLVQFD SLRKELALSR CEVEQARLLV
LKAAHMIDTV GPKEAKSEIA MIKVVAPNMA ISILDRAMQQ QGARGLTPFT PLASFYVWAR
SLRIADGPDA VHLETIAKIE MKSRL
//