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Database: UniProt
Entry: V9FE70_PHYPR
LinkDB: V9FE70_PHYPR
Original site: V9FE70_PHYPR 
ID   V9FE70_PHYPR            Unreviewed;       675 AA.
AC   V9FE70;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=Acyl-coenzyme A oxidase {ECO:0000256|PIRNR:PIRNR000168};
GN   ORFNames=F443_06541 {ECO:0000313|EMBL:ETI49765.1};
OS   Phytophthora parasitica P1569.
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=1317065 {ECO:0000313|EMBL:ETI49765.1, ECO:0000313|Proteomes:UP000018721};
RN   [1] {ECO:0000313|EMBL:ETI49765.1, ECO:0000313|Proteomes:UP000018721}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P1569 {ECO:0000313|EMBL:ETI49765.1,
RC   ECO:0000313|Proteomes:UP000018721};
RG   The Broad Institute Genomics Platform;
RA   Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA   Machado M., Johnson C.S., Arredondo F., Hong C., Coffey M., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA   Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA   Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA   Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA   Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Phytophthora parasitica P1569.";
RL   Submitted (NOV-2013) 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:ETI49765.1}.
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DR   EMBL; ANIZ01001092; ETI49765.1; -; Genomic_DNA.
DR   AlphaFoldDB; V9FE70; -.
DR   EnsemblProtists; ETI49765; ETI49765; F443_06541.
DR   eggNOG; KOG0136; Eukaryota.
DR   HOGENOM; CLU_014629_3_1_1; -.
DR   OrthoDB; 5473219at2759; -.
DR   Proteomes; UP000018721; 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:UP000018721}.
FT   DOMAIN          19..135
FT                   /note="Acyl-coenzyme A oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14749"
FT   DOMAIN          483..664
FT                   /note="Acyl-CoA oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01756"
FT   ACT_SITE        429
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000168-1"
FT   BINDING         142
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000168-2"
FT   BINDING         181
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000168-2"
SQ   SEQUENCE   675 AA;  75368 MW;  A1EDCCE8CAE42E72 CRC64;
     MMPSGCLEAE RKGSPVPARE LAFVLHKSKR NVERLERLEQ LLLQDPVFNH EKMNYLTRGE
     QYKRALQMSA RVEILARRNR LSEEDTEQLR LIFQGITSCS AATTLHTLMF IKNLGLLFTD
     EQQTRWMEMA KQWRMVGCYA QTELGHGSNV RGLETTATYI PATDEFEIHS PTLTSMKWWP
     GALARTANFG VVYARLLLGG KDYGVHNFMV QLRDLETHDA MPGVTLGDVG PKIGFNNVDN
     GYCSFNRVRI PRLNMGMRFA TVTREGKYVK NSDVPQEVLY FTMLQTRMVF IRSAGVNLAK
     ACTISIRYSA VRQQGYDANY PKSKEELSVL DYQTQQYRLF PLLAAAYAIV LTGNRVDDFS
     AALSEQMKSG EVSLLSVGHV MSCGLKVLTT DLATAGIETA RRACGGHGYL LSSGLPILLG
     DAAQTVTTEG DNLVLSIQTA RALLKILASY KKTGKVPEPM AFLGNIDKLP NATPRTQKQW
     LEPQNYVAAF EQRFLYQLRS YVQKISTESS ATAGLQNNSM DTLKLTNSYA NLVLVKTFAE
     AVQAPSTLTS EFLSSPAILN VVRLLCHLFA LTQLEATAGE FMESGCVFPS EMPIIRANIE
     ELLKLIRPHA VTLVDGFNFS DHTLNSTLGR YDGNVYEALY ESAQHDPLNH SSDKVALHEL
     LRPIRDEIAR SKSRL
//
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