ID A0A078ATD9_STYLE Unreviewed; 692 AA.
AC A0A078ATD9;
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=Contig4000.g4283 {ECO:0000313|EMBL:CDW85479.1};
GN ORFNames=STYLEM_14557 {ECO:0000313|EMBL:CDW85479.1};
OS Stylonychia lemnae (Ciliate).
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata; Spirotrichea;
OC Stichotrichia; Sporadotrichida; Oxytrichidae; Stylonychinae; Stylonychia.
OX NCBI_TaxID=5949 {ECO:0000313|EMBL:CDW85479.1, ECO:0000313|Proteomes:UP000039865};
RN [1] {ECO:0000313|EMBL:CDW85479.1, ECO:0000313|Proteomes:UP000039865}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=130c {ECO:0000313|EMBL:CDW85479.1,
RC ECO:0000313|Proteomes:UP000039865};
RA Swart Estienne;
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000256|ARBA:ARBA00004275}.
CC -!- SIMILARITY: Belongs to the acyl-CoA oxidase family.
CC {ECO:0000256|ARBA:ARBA00006288, ECO:0000256|PIRNR:PIRNR000168}.
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DR EMBL; CCKQ01013776; CDW85479.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A078ATD9; -.
DR EnsemblProtists; CDW85479; CDW85479; STYLEM_14557.
DR InParanoid; A0A078ATD9; -.
DR OMA; PMMRGKL; -.
DR OrthoDB; 5777at2759; -.
DR Proteomes; UP000039865; Unassembled WGS sequence.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
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; 1.10.540.10; Acyl-CoA dehydrogenase/oxidase, N-terminal domain; 1.
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; IPR029320; Acyl-CoA_ox_N.
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; IPR037069; AcylCoA_DH/ox_N_sf.
DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom_sf.
DR PANTHER; PTHR10909; ELECTRON TRANSPORT OXIDOREDUCTASE; 1.
DR PANTHER; PTHR10909:SF250; PEROXISOMAL ACYL-COENZYME A OXIDASE 1; 1.
DR Pfam; PF01756; ACOX; 1.
DR Pfam; PF14749; Acyl-CoA_ox_N; 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 Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW Flavoprotein {ECO:0000256|PIRNR:PIRNR000168};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Peroxisome {ECO:0000256|ARBA:ARBA00023140};
KW Reference proteome {ECO:0000313|Proteomes:UP000039865}.
FT DOMAIN 36..155
FT /note="Acyl-coenzyme A oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF14749"
FT DOMAIN 513..688
FT /note="Acyl-CoA oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01756"
FT ACT_SITE 454
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000168-1"
FT BINDING 161
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000168-2"
FT BINDING 210
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000168-2"
SQ SEQUENCE 692 AA; 78743 MW; 9FEF2E204014EA3C CRC64;
MESNKTSQEQ KPKVGSIKNK IVAQDLEEER KKANFDIKEL TESYFGGKEK LEQHNDHISV
MENDPILRNT EKWYDMTREE QIEHNFKRAR RTYEINKEKY YHNYEVSYIP WFSAMFQGIF
PFGLTMSMFS LCIQQLGDDE QVAKWLPLVK QMKMIGCYAQ TELGHGSNVA VILEQVQYFQ
GLETTATFDK EKDEFILNSP TITSTKFWPG ELGKFGGWAV VYAKMIINGK NHGVQPFMLQ
MRDTETYETL PGIECGDIGP KFGYASKDNG YLILKNVRIP RSNLLQRYVN VDREGHFTIK
GDLRSLYSVM MFIRVSIAIG AAKTLGVALT IGTRYAVVRR QFSTQDGTKI ERKLLDYQTH
QFKYTPLLAY TYAFNFTSLA LMEMHQQLLK DMKTGNFGLL DLAHHLSSGY KASYTRICYD
GIDTIRQSCG GAGFLAWSGL PTLQTDYAPN TTFEGDNTVM HQQSARLILK TIKNIQRGFK
PTGIFDYFNK FEELLSKKGQ VKGSADLLCL VNLENALAVR SAFKIKTTAM KMATSQLSEN
EKANSAFSVD MVSMAHAHIM YVTFKYFLNH IENHPYKCPK VKENLKNLAR VYALTELLQD
SVSLYETGFF TVGNAQHLLE AQKEAIAIVR PQMIPLVEAL AVPDSYIVSA IGNSYGDIYE
TQLEWAKNSK LNQTSVLPGI KEHILPILHG KL
//
