ID   A0A078A4B1_STYLE        Unreviewed;       652 AA.
AC   A0A078A4B1;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=Acyl-coenzyme A oxidase {ECO:0000256|PIRNR:PIRNR000168};
GN   Name=Contig12915.g13773 {ECO:0000313|EMBL:CDW77002.1};
GN   ORFNames=STYLEM_5967 {ECO:0000313|EMBL:CDW77002.1};
OS   Stylonychia lemnae (Ciliate).
OC   Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata; Spirotrichea;
OC   Stichotrichia; Sporadotrichida; Oxytrichidae; Stylonychinae; Stylonychia.
OX   NCBI_TaxID=5949 {ECO:0000313|EMBL:CDW77002.1, ECO:0000313|Proteomes:UP000039865};
RN   [1] {ECO:0000313|EMBL:CDW77002.1, ECO:0000313|Proteomes:UP000039865}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=130c {ECO:0000313|EMBL:CDW77002.1,
RC   ECO:0000313|Proteomes:UP000039865};
RA   Swart Estienne;
RL   Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
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}.
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; CCKQ01005741; CDW77002.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A078A4B1; -.
DR   EnsemblProtists; CDW77002; CDW77002; STYLEM_5967.
DR   InParanoid; A0A078A4B1; -.
DR   OrthoDB; 5473219at2759; -.
DR   Proteomes; UP000039865; 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: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; 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; 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|PIRNR:PIRNR000168, ECO:0000256|PIRSR:PIRSR000168-2};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|PIRNR:PIRNR000168};
KW   Reference proteome {ECO:0000313|Proteomes:UP000039865}.
FT   DOMAIN          130..239
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          480..612
FT                   /note="Acyl-CoA oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01756"
FT   ACT_SITE        423
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000168-1"
FT   BINDING         134
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000168-2"
FT   BINDING         173
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000168-2"
SQ   SEQUENCE   652 AA;  75105 MW;  9C00D8F7E33A1FAE CRC64;
     MPSRIEDYQL NNHERSRPNA FIENSREDKR DLCNQQLIAL HNEILKRRIF TVEQIAKDPE
     TFLMTQQIKR DLDSAMLIKQ SIFTFSCALN LKIQNLDVHF GLYMKSVINL GTEKHWPLVM
     RAASLEDMAC FCMTELSHGS NVQGLKTRAT YDPSTREFIL NTPRDQDMKF WIGNLGKTAH
     IGVVFAQLHT QGKGQGVHAF VVPLRDRRTH QPLPGVLIGD CGAKIGHHGI DNGFLKFSDY
     RISKDALLDR FFQVADDGTY TSIIPTKGKR FAFVLSSLSF GRTMMAHATV NIGFYALNTA
     IRYGHLRRQF SNNMKIGADE SVLINYQLFQ YRLIPRLARC FVLRFGQDEL VSMYFDNRDK
     LTDPKFNGLK LFHALITFAK SHLSTCVHRD LEEVRQALGG LGYSQYSEIG PSINDHDINL
     TWEGDNKVLL QQTAKFVLKN AYNVMQNKPV QDENLAYLKE YFEDMDEYKA KITEDFKSND
     NIVRVFRGMT AQTTFKALMQ MQQQSQQKGM YQAYQESLPF SQNVLSVLFG ETFFIEAYLR
     RISNVKDKET RVIFDKLFHL YANYTIVDKS GDFRDQNFLS SEAINICKQN VIDLCSELKE
     ELIPLTEIAE IDNTNIFSYP DAYERFITKV VQAPNSFSKL ENRDIILKTR GI
//