ID   A0A0N0NKK4_9EURO        Unreviewed;       651 AA.
AC   A0A0N0NKK4;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=Acyl-coenzyme A oxidase {ECO:0000256|PIRNR:PIRNR000168};
GN   ORFNames=AB675_1092 {ECO:0000313|EMBL:KPI38128.1};
OS   Phialophora attinorum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Phialophora.
OX   NCBI_TaxID=1664694 {ECO:0000313|EMBL:KPI38128.1, ECO:0000313|Proteomes:UP000038010};
RN   [1] {ECO:0000313|EMBL:KPI38128.1, ECO:0000313|Proteomes:UP000038010}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 131958 {ECO:0000313|EMBL:KPI38128.1,
RC   ECO:0000313|Proteomes:UP000038010};
RA   Moreno L.F., Stielow B.J., de Hoog S., Vicente V.A., Weiss V.A.,
RA   de Vries M., Cruz L.M., Souza E.M.;
RT   "Draft genome of the ant-associated black yeast Phialophora attae CBS
RT   131958.";
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the acyl-CoA oxidase family.
CC       {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:KPI38128.1}.
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DR   EMBL; LFJN01000020; KPI38128.1; -; Genomic_DNA.
DR   RefSeq; XP_017998091.1; XM_018139733.1.
DR   AlphaFoldDB; A0A0N0NKK4; -.
DR   STRING; 1664694.A0A0N0NKK4; -.
DR   GeneID; 28731602; -.
DR   OrthoDB; 5777at2759; -.
DR   UniPathway; UPA00661; -.
DR   Proteomes; UP000038010; Unassembled WGS sequence.
DR   GO; GO:0005777; C:peroxisome; IEA:InterPro.
DR   GO; GO:0003997; F:acyl-CoA oxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0033540; P:fatty acid beta-oxidation using acyl-CoA oxidase; IEA:UniProtKB-UniPathway.
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; 1.
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; 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; 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   Flavoprotein {ECO:0000256|PIRNR:PIRNR000168};
KW   Reference proteome {ECO:0000313|Proteomes:UP000038010}.
FT   DOMAIN          19..132
FT                   /note="Acyl-coenzyme A oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14749"
FT   ACT_SITE        409
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000168-1"
FT   BINDING         138
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000168-2"
FT   BINDING         177
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000168-2"
SQ   SEQUENCE   651 AA;  72457 MW;  D0928EAB7DFF1E21 CRC64;
     MERNVGQCRA VPQDAVRSDF AYYLWGGKER FRRREIALDV LKSNPEFAKT AATYSQARKD
     VWLRIARQSK QLVALKLRHQ WSTAQLLDVI TMTDWMMPIY PQYRIFMSNI ERQMSDQQKN
     VWLPMAERFE ILGCYCQTEL GHGSFVGGIE TTAVFDVHSD EFVIDSPTLS STKYWIGAAG
     VWATHGIVVA RLQIGDQDHG PHLFLVQLRD LESHQTLRGI NIYELGPKVH QGMLGMDNGA
     SVSREGTYLK PTNTKHAYGS MVTVRAQMAQ LTGWDLLKAV VVATHYTKFR KQFFTTADDK
     CDHEEVTVFE YSSVKSRLIP LLAKATALII VGQAIKEAYD NYTHTVLRTG DSSALEDLHL
     QTVASKVYGT EIASRGVEIS RIACGGHGYS ALAGFGRMYA HTVNAVTYEG DNYVISQQVT
     RAIAKHCRNG TKTLPPSIAY LSLLQSGSVA QEPHICSAAD WLSTAVQEWA LTARLASLVQ
     QYLDDTTTGK DTSYSSHALT MAHADYVYWA GFWRSVRALE GAETSFAPHF SLSILSEPHH
     PSLVHASQLS ITQLAHLRDA HRQAINDVAI QSIDTVISAY GLTEFELDSV LARTNRTPYE
     ALIDAAQSSE MSGEDMAEIW PAIVETTKLW RSKGLQSSAT ATTSSRMRGK L
//