GenomeNet

Database: UniProt
Entry: O01590_CAEEL
LinkDB: O01590_CAEEL
Original site: O01590_CAEEL 
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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
//
DBGET integrated database retrieval system