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Database: UniProt
Entry: A0A1B0AH42_GLOPL
LinkDB: A0A1B0AH42_GLOPL
Original site: A0A1B0AH42_GLOPL 
ID   A0A1B0AH42_GLOPL        Unreviewed;       692 AA.
AC   A0A1B0AH42;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=Acyl-coenzyme A oxidase {ECO:0000256|PIRNR:PIRNR000168};
OS   Glossina pallidipes (Tsetse fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Hippoboscoidea;
OC   Glossinidae; Glossina.
OX   NCBI_TaxID=7398 {ECO:0000313|EnsemblMetazoa:GPAI045574-PA, ECO:0000313|Proteomes:UP000092445};
RN   [1] {ECO:0000313|Proteomes:UP000092445}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IAEA {ECO:0000313|Proteomes:UP000092445};
RA   Aksoy S., Warren W., Wilson R.K.;
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:GPAI045574-PA}
RP   IDENTIFICATION.
RC   STRAIN=IAEA {ECO:0000313|EnsemblMetazoa:GPAI045574-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; A0A1B0AH42; -.
DR   STRING; 7398.A0A1B0AH42; -.
DR   EnsemblMetazoa; GPAI045574-RA; GPAI045574-PA; GPAI045574.
DR   VEuPathDB; VectorBase:GPAI045574; -.
DR   Proteomes; UP000092445; 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..689
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;  78340 MW;  D609E6D5AA612C7A CRC64;
     MAQNVDTSFI PDLPKGPLCA YRKRVNFDWK HLRLIFENEQ SLRIKYKVWK ILEHDPLFSQ
     PISTLPTDEQ KRICAMQTNR MKQLDLVPKE IEEKSFCEKT KYLMSINEAL HVYCPSLSVK
     IALGVGLFNN AIRAMGTERH KKYYEAAWHR EIVTCLAITE VSHGSNTKSI RTTATYDPTT
     QEFVINTPDF EAAKCWVGNL GKSATVAMTF ANLHTPDGVN QGLHGFLIPI RDPNTLQPYP
     GLLVGDIGEK IGLNGIDNGF VIFNNYRIPR ENLLNRTGDV TPEGIYESVF SEPGKVLGAA
     LESFSAGRIG IMQESVNTLS SAAVIAVRYA ALRKQFGPER NGPEIPIIEY QYHQWRIFPY
     LAAACVLKIA VQELTNEYLK IIERSQGDSN GFELLTQIVS EIHAIISSCK PMITWTARDA
     IQEAREACGG HGYLKASKLG DLRNDHDPSC TYEGDNNVLG QQASNWLLRQ WTDNVESPVG
     TANFLGNRKK LLQQKYEDVL EKDSIGSMNF IIRCYEWLMC YLLKTTSNRI SHDMQKGLNR
     FDARNNAQVY GAGEVSLVYA EYFCMTRFIE RFKQPDITQE YSTILRLIFE VYSMWCLDKH
     MTTYYVGGFA NSSKFADLVR TRLLSKCGEL KDISVSVADA LAPPDFALNS VIGKSDGLLY
     ENLQNVFMTN EGAFERPAWW QDIVIPKMKS KL
//
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