ID A0A0R3P250_DROPS Unreviewed; 701 AA.
AC A0A0R3P250; A0A6I8VB49;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Acyl-coenzyme A oxidase {ECO:0000256|PIRNR:PIRNR000168};
GN Name=LOC4816232 {ECO:0000313|RefSeq:XP_015037004.1};
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_015037004.1};
RN [1] {ECO:0000313|RefSeq:XP_015037004.1}
RP IDENTIFICATION.
RC STRAIN=MV2-25 {ECO:0000313|RefSeq:XP_015037004.1};
RC TISSUE=Whole body {ECO:0000313|RefSeq:XP_015037004.1};
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_015037004.1; XM_015181518.2.
DR AlphaFoldDB; A0A0R3P250; -.
DR SMR; A0A0R3P250; -.
DR EnsemblMetazoa; FBtr0368026; FBpp0330870; FBgn0081842.
DR GeneID; 4816232; -.
DR Proteomes; UP000001819; Chromosome 4.
DR Bgee; FBgn0081842; Expressed in insect adult head and 2 other cell types or tissues.
DR ExpressionAtlas; A0A0R3P250; 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 164..274
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 310..468
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT DOMAIN 516..691
FT /note="Acyl-CoA oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01756"
FT ACT_SITE 458
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000168-1"
FT BINDING 168
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000168-2"
FT BINDING 207
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000168-2"
SQ SEQUENCE 701 AA; 78834 MW; 82840C8BDB7C635B CRC64;
MVAINEADNG QQVGNIFDDK KIFPEFRSGP LDVYRQKASF CYKRMNVLLE GEEHIRLKHK
VWQWMEQHPD YQREPEVATL ERTRELANKR QHLLWEQHFF GVNEYLGTPH LLLAFGQAIF
SYDFSSSVKF GLSNGMFPST LVSNGSGRLG KYIAKISDNR ILGAYALTEF SHGTNALGMR
TRATYDLKTK EFIIHTPDFE ASKCWVGNLG KTCTHAIVYA QLFVPDDKHQ GLQAFLVPIR
DERTLLPFPG VTVGDMGEKI GLNGIDNGFV SFNQYRIPKA NLLSKAGDID AQGNYNSPIK
DERKRLGASL GALSQGRVNI TAITYVALSK AVSIATRYGA SRRQFGPNNS QTEWPVIEYQ
SQQYRLIPHL ATTIALRVAT LWIGKENVDM TMKGFTGEDT SKAGMEIHAI SSALKPVATW
AARDGIQECR EACGGHGYLK AAGLGDLRND NDANCTYEGE NNTLIQQASN WLISLRRGNA
DFKAVSPLET VSFLSDINSI LQTKAEERTP AQALDANNLL KALNWLTAWQ LETTVKRAEQ
LQREGKDAFE TRNNIQVFAA QKLSIIYGER TIYYVFYKFV NSLPASAEKQ VLQQLLSFYG
AHLVTKYSAI FYQGGYFRDS PHIELYQQGI LQLLPILKDE AIALIDAIAP TDFILNSPLG
MSDGNVYQHL QKTIVSTPGV FERPEWWRDV TYKDYLKRAK L
//
