ID A0A0W8CC18_PHYNI Unreviewed; 660 AA.
AC A0A0W8CC18;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Acyl-coenzyme A oxidase {ECO:0000256|PIRNR:PIRNR000168};
GN ORFNames=AM587_10011133 {ECO:0000313|EMBL:KUF81605.1}, AM588_10007342
GN {ECO:0000313|EMBL:KUF92706.1};
OS Phytophthora nicotianae (Buckeye rot agent).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=4790 {ECO:0000313|EMBL:KUF81605.1, ECO:0000313|Proteomes:UP000052943};
RN [1] {ECO:0000313|Proteomes:UP000052943, ECO:0000313|Proteomes:UP000054636}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Race 0 {ECO:0000313|EMBL:KUF81605.1}, race 0
RC {ECO:0000313|Proteomes:UP000052943}, race 1
RC {ECO:0000313|Proteomes:UP000054636}, and Race 1
RC {ECO:0000313|EMBL:KUF92706.1};
RA Liu H., Ma X., Yu H., Fang D., Li Y., Wang X., Wang W., Dong Y., Xiao B.;
RT "Genomes and virulence difference between two physiological races of
RT Phytophthora nicotianae.";
RL Submitted (NOV-2015) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KUF81605.1}.
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DR EMBL; LNFO01004094; KUF81605.1; -; Genomic_DNA.
DR EMBL; LNFP01000447; KUF92706.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0W8CC18; -.
DR STRING; 4790.A0A0W8CC18; -.
DR EnsemblProtists; KUF81605; KUF81605; AM587_10011133.
DR EnsemblProtists; KUF92706; KUF92706; AM588_10007342.
DR OMA; ICTRFSA; -.
DR OrthoDB; 5777at2759; -.
DR Proteomes; UP000052943; Unassembled WGS sequence.
DR Proteomes; UP000054636; 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; 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; 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; PF00441; Acyl-CoA_dh_1; 1.
DR Pfam; PF02770; Acyl-CoA_dh_M; 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|ARBA:ARBA00022827, ECO:0000256|PIRNR:PIRNR000168};
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|PIRNR:PIRNR000168};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Peroxisome {ECO:0000256|ARBA:ARBA00023140};
KW Reference proteome {ECO:0000313|Proteomes:UP000052943}.
FT DOMAIN 26..139
FT /note="Acyl-coenzyme A oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF14749"
FT DOMAIN 141..250
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 371..444
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT DOMAIN 484..657
FT /note="Acyl-CoA oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01756"
FT ACT_SITE 430
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000168-1"
FT BINDING 145
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000168-2"
FT BINDING 184
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000168-2"
SQ SEQUENCE 660 AA; 73580 MW; FFA0C1ACDFAFDD4C CRC64;
MVVELKDLAP LLLKKERANG DIKPAVLTDV LRDGKAANAR RKELINVIER HPVLSDRNMM
FRNHTERYEF GLKKAYHYVK LLQDGGYTNP EDQQILYKAL GEPLGFDVHR AMFIPTLENQ
GTDEQRAKWL PLAKNYKIFG AYAQTELGHG SNVQGIETVA TYDKATQEFI IDSPTLTSRK
WWPGGLGKTA NHAIVHARLY LDGKDVGVQA FLVQIRSMED HQPLPGIEVG DIGPKVGFNG
VDNGYCAFHK IRIPRENMMM RYAKVLPDGT FVKPKSDKLV YLTMVQVRAY MIKTAGIQMG
AASTICTRFS AARIQGRTPD NKGEFQVLDY QNQQHKLFPL IAISYAALFA GVSLVEMHDS
ALDVIKKGGN SFGAKLAELH AVSSGLKAWL AERVSDGIET CRRLCGGHGF TQSSNLAHLF
AEMVGANTYE GTSDVLVQQH ARYLLKTLAS LPVDEESTKF LNNVKRYSDI KLRCKAQKSE
DFGNLELLLD AFQTRTARVV LALASKMKAT KNDGNACMVL MTRASAAHAE LILLEAFIRG
AQNLPASSEK DSVTQLCSLF GAWLITKSLG DFRQHDYLSS QQADLVRNQV VRLLPLIRKN
CVLLTDAWDF SDFELNSTIG RYDGDIYRAL VKRAADEPLN KSQIPDGYEM YLKPLIQSGL
//
