ID A0A1A9WHH4_9MUSC Unreviewed; 692 AA.
AC A0A1A9WHH4;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Acyl-coenzyme A oxidase {ECO:0000256|PIRNR:PIRNR000168};
OS Glossina brevipalpis.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Hippoboscoidea;
OC Glossinidae; Glossina.
OX NCBI_TaxID=37001 {ECO:0000313|EnsemblMetazoa:GBRI019912-PA, ECO:0000313|Proteomes:UP000091820};
RN [1] {ECO:0000313|Proteomes:UP000091820}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IAEA {ECO:0000313|Proteomes:UP000091820};
RA Aksoy S., Warren W., Wilson R.K.;
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:GBRI019912-PA}
RP IDENTIFICATION.
RC STRAIN=IAEA {ECO:0000313|EnsemblMetazoa:GBRI019912-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the acyl-CoA oxidase family.
CC {ECO:0000256|ARBA:ARBA00006288, ECO:0000256|PIRNR:PIRNR000168}.
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DR AlphaFoldDB; A0A1A9WHH4; -.
DR STRING; 37001.A0A1A9WHH4; -.
DR EnsemblMetazoa; GBRI019912-RA; GBRI019912-PA; GBRI019912.
DR VEuPathDB; VectorBase:GBRI019912; -.
DR OrthoDB; 5777at2759; -.
DR Proteomes; UP000091820; Unassembled WGS sequence.
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:SF223; ACYL-COENZYME A OXIDASE; 1.
DR PANTHER; PTHR10909; ELECTRON TRANSPORT OXIDOREDUCTASE; 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}.
FT DOMAIN 155..265
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 299..463
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT DOMAIN 508..686
FT /note="Acyl-CoA oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01756"
FT ACT_SITE 453
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000168-1"
FT BINDING 159
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000168-2"
FT BINDING 198
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000168-2"
SQ SEQUENCE 692 AA; 78429 MW; B84766D823DF8563 CRC64;
MAQNVDTSFI PDLPKGPLCA YRKRTNFDWK RLRLIFENEQ SLRIKYKVWK ILEHDPLFSQ
PISTLPTDEQ KRICAMQMNR MKQLDLVPKE IEEKSFCEKT KYLMSINEAL HIYCPSLSVK
IALGVGLFNN AIRAMGTERH KKYYEAAWHR EIVTCLAITE VSHGSNTKSI RTTATYDPST
QEFVINTPDF EAAKCWVGNL GKSATVAMTF ANLYTPDGVN QGLHGFLIPI RDPNTLQSYP
GLLVGDIGEK NGLNGIDNGF VIFNNYRIPR ENLLNRTGDV TREGVYESVF SEPGKVLGAA
LESFSAGRIG IMQESVNTLS SAAVIAVRYA ALRKQFGPER NGPDIPIIEY QLHQWRIFPY
LAAACILKIS VQELTNEYLK IIERSQADSN GFELLTQIVS EIHAIISSCK PMITWTARDA
IQEAREACGG HGYLKASKLG DLRNDHDPSC TYEGDNNVLG QQASNWLLKQ WTDNIESPVG
TANFLGNRKK LLQQKCENIL EEHTMESMNF IMHCYEWLLC YLLETTSNRI SNDMRRGLNR
FEARNNAQVY GAGKVSLVYA EYFCITRFIE RFKQPDITKE YATILKLIFD VYAMWCLDKH
MATYYVGDFA NGPKFADAVR MRLLSKCAEL KDISVSIADA LAPPDFALNS VIGKSDGLLY
ENLQNVFMTN EGAFERPAWW QDIIIPQSKS KL
//
