ID A0A0L8I634_OCTBM Unreviewed; 663 AA.
AC A0A0L8I634;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Acyl-coenzyme A oxidase {ECO:0000256|PIRNR:PIRNR000168};
GN ORFNames=OCBIM_22033387mg {ECO:0000313|EMBL:KOF96829.1};
OS Octopus bimaculoides (California two-spotted octopus).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Cephalopoda;
OC Coleoidea; Octopodiformes; Octopoda; Incirrata; Octopodidae; Octopus.
OX NCBI_TaxID=37653 {ECO:0000313|EMBL:KOF96829.1};
RN [1] {ECO:0000313|EMBL:KOF96829.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=UCB-OBI-ISO-001 {ECO:0000313|EMBL:KOF96829.1};
RC TISSUE=Gonad {ECO:0000313|EMBL:KOF96829.1};
RA Tran T., Druce J.;
RT "MeaNS - Measles Nucleotide Surveillance Program.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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 -!- 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; KQ416479; KOF96829.1; -; Genomic_DNA.
DR RefSeq; XP_014790575.1; XM_014935089.1.
DR AlphaFoldDB; A0A0L8I634; -.
DR STRING; 37653.A0A0L8I634; -.
DR EnsemblMetazoa; Ocbimv22033387m; Ocbimv22033387m.p; Ocbimv22033387m.g.
DR EnsemblMetazoa; XM_014935089.1; XP_014790575.1; LOC106883939.
DR GeneID; 106883939; -.
DR KEGG; obi:106883939; -.
DR OMA; CYYISVK; -.
DR OrthoDB; 5777at2759; -.
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}.
FT DOMAIN 21..137
FT /note="Acyl-coenzyme A oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF14749"
FT DOMAIN 477..655
FT /note="Acyl-CoA oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01756"
FT ACT_SITE 425
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000168-1"
FT BINDING 143
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000168-2"
FT BINDING 182
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000168-2"
SQ SEQUENCE 663 AA; 75467 MW; BA5FC567DDF937B0 CRC64;
MTKYLNIHPN LIKERKGATF DPYTLTCLLW DGDEVVKHKR NLVALLENDP NLQDENLSDF
LSQEEKIDFA IKKTIYLFRK LGMNEKEYYM FLFQNFYPFQ QLGFPLHFVM FTSTLKLLCS
PEQANYWLPK ASNLEILGCY AQTELGHGTF LKGLETTAVY DPLNEEFVLN TPTTTSMKWW
SGQLGKVANY CIVIAQLYIM NKCYGIHPFI LQIRSLEDHS FMPGVITGDV GPKMALNSID
NGFMKLDNVR IPRNQLLMKY DQVLKDGTYI SGPNKKFMYA TMMTVRCTII MESAQNLAAA
CTIAVRYSVV RQQSEAEQGA GEQSVLNFQT QQYRLFSALS TTFALFFAWR SMNEACQQIL
TDASQGKTDQ FLFLHSFLAG LKAQSTWLAT KYIQTCRECC GGHGVSLASG LPLLESHTAV
SCTYEGDNTV MILQTGKFLL KCSRDISQGK NLVGFVSYLN ANYTTEHQDV DSNLHLPALL
KLCQHRSKRM LLYISKLVFE KINSGSSLEQ AFNIWSNEIK NMAIVVCQVY TMEKFIEAIG
QIKENRLASV LTDVCKFYCA FNIVENIGDF LQFNLLTVEQ VKLLKTAMYN QLSKIRPNAI
ALVDAFDFSD RFLHSALGRY DGQVYQALYD YAKLAPINSK EVHDSCKEYL LPFLKQQSLK
AQL
//
