ID Q29JP9_DROPS Unreviewed; 722 AA.
AC Q29JP9; A0A6I8UI55;
DT 04-APR-2006, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2008, sequence version 2.
DT 27-MAR-2024, entry version 100.
DE RecName: Full=Acyl-coenzyme A oxidase {ECO:0000256|PIRNR:PIRNR000168};
GN Name=LOC4816232 {ECO:0000313|RefSeq:XP_001355853.2};
OS Drosophila pseudoobscura pseudoobscura (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=46245 {ECO:0000313|Proteomes:UP000001819, ECO:0000313|RefSeq:XP_001355853.2};
RN [1] {ECO:0000313|RefSeq:XP_001355853.2}
RP IDENTIFICATION.
RC STRAIN=MV2-25 {ECO:0000313|RefSeq:XP_001355853.2};
RC TISSUE=Whole body {ECO:0000313|RefSeq:XP_001355853.2};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- PATHWAY: Lipid metabolism; peroxisomal fatty acid beta-oxidation.
CC {ECO:0000256|ARBA:ARBA00004846}.
CC -!- SIMILARITY: Belongs to the acyl-CoA oxidase family.
CC {ECO:0000256|ARBA:ARBA00006288, ECO:0000256|PIRNR:PIRNR000168}.
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DR RefSeq; XP_001355853.2; XM_001355817.4.
DR AlphaFoldDB; Q29JP9; -.
DR STRING; 46245.Q29JP9; -.
DR EnsemblMetazoa; FBtr0287389; FBpp0285827; FBgn0081842.
DR GeneID; 4816232; -.
DR KEGG; dpo:4816232; -.
DR eggNOG; KOG0135; Eukaryota.
DR HOGENOM; CLU_014629_4_2_1; -.
DR InParanoid; Q29JP9; -.
DR OMA; ERASWWQ; -.
DR Proteomes; UP000001819; Chromosome 4.
DR Bgee; FBgn0081842; Expressed in insect adult head and 2 other cell types or tissues.
DR ExpressionAtlas; Q29JP9; baseline.
DR GO; GO:0005777; C:peroxisome; IEA:InterPro.
DR GO; GO:0003997; F:acyl-CoA oxidase activity; IEA:InterPro.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0009058; P:biosynthetic process; IEA:UniProt.
DR GO; GO:0006635; P:fatty acid beta-oxidation; IEA:InterPro.
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; 2.
DR InterPro; IPR006091; Acyl-CoA_Oxase/DH_mid-dom.
DR InterPro; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf.
DR InterPro; IPR012258; Acyl-CoA_oxidase.
DR InterPro; IPR002655; Acyl-CoA_oxidase_C.
DR InterPro; IPR036250; AcylCo_DH-like_C.
DR InterPro; IPR009075; AcylCo_DH/oxidase_C.
DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom_sf.
DR PANTHER; PTHR10909; ELECTRON TRANSPORT OXIDOREDUCTASE; 1.
DR PANTHER; PTHR10909:SF352; PEROXISOMAL ACYL-COENZYME A OXIDASE 3; 1.
DR Pfam; PF01756; ACOX; 1.
DR Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR PIRSF; PIRSF000168; Acyl-CoA_oxidase; 1.
DR SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 2.
DR SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRNR:PIRNR000168};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|PIRNR:PIRNR000168};
KW Reference proteome {ECO:0000313|Proteomes:UP000001819}.
FT DOMAIN 185..295
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 331..489
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT DOMAIN 537..712
FT /note="Acyl-CoA oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01756"
FT ACT_SITE 479
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000168-1"
FT BINDING 189
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000168-2"
FT BINDING 228
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000168-2"
SQ SEQUENCE 722 AA; 81133 MW; 78012FCC2E53DCFC CRC64;
MASTEDGHSA VNQINEILTS LSDYYSEADN GQQVGNIFDD KKIFPEFRSG PLDVYRQKAS
FCYKRMNVLL EGEEHIRLKH KVWQWMEQHP DYQREPEVAT LERTRELANK RQHLLWEQHF
FGVNEYLGTP HLLLAFGQAI FSYDFSSSVK FGLSNGMFPS TLVSNGSGRL GKYIAKISDN
RILGAYALTE FSHGTNALGM RTRATYDLKT KEFIIHTPDF EASKCWVGNL GKTCTHAIVY
AQLFVPDDKH QGLQAFLVPI RDERTLLPFP GVTVGDMGEK IGLNGIDNGF VSFNQYRIPK
ANLLSKAGDI DAQGNYNSPI KDERKRLGAS LGALSQGRVN ITAITYVALS KAVSIATRYG
ASRRQFGPNN SQTEWPVIEY QSQQYRLIPH LATTIALRVA TLWIGKENVD MTMKGFTGED
TSKAGMEIHA ISSALKPVAT WAARDGIQEC REACGGHGYL KAAGLGDLRN DNDANCTYEG
ENNTLIQQAS NWLISLRRGN ADFKAVSPLE TVSFLSDINS ILQTKAEERT PAQALDANNL
LKALNWLTAW QLETTVKRAE QLQREGKDAF ETRNNIQVFA AQKLSIIYGE RTIYYVFYKF
VNSLPASAEK QVLQQLLSFY GAHLVTKYSA IFYQGGYFRD SPHIELYQQG ILQLLPILKD
EAIALIDAIA PTDFILNSPL GMSDGNVYQH LQKTIVSTPG VFERPEWWRD VTYKDYLKRA
KL
//
