ID A0A0D2BA48_9EURO Unreviewed; 707 AA.
AC A0A0D2BA48;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=Acyl-coenzyme A oxidase {ECO:0000256|PIRNR:PIRNR000168};
GN ORFNames=PV05_10798 {ECO:0000313|EMBL:KIW49086.1};
OS Exophiala xenobiotica.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=348802 {ECO:0000313|EMBL:KIW49086.1, ECO:0000313|Proteomes:UP000054342};
RN [1] {ECO:0000313|EMBL:KIW49086.1, ECO:0000313|Proteomes:UP000054342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 118157 {ECO:0000313|EMBL:KIW49086.1,
RC ECO:0000313|Proteomes:UP000054342};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala xenobiotica CBS118157.";
RL Submitted (JAN-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}.
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DR EMBL; KN847323; KIW49086.1; -; Genomic_DNA.
DR RefSeq; XP_013309670.1; XM_013454216.1.
DR AlphaFoldDB; A0A0D2BA48; -.
DR STRING; 348802.A0A0D2BA48; -.
DR GeneID; 25332706; -.
DR HOGENOM; CLU_014629_3_1_1; -.
DR OrthoDB; 5777at2759; -.
DR UniPathway; UPA00661; -.
DR Proteomes; UP000054342; Unassembled WGS sequence.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
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; 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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Peroxisome {ECO:0000256|ARBA:ARBA00023140};
KW Reference proteome {ECO:0000313|Proteomes:UP000054342}.
FT DOMAIN 29..144
FT /note="Acyl-coenzyme A oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF14749"
FT DOMAIN 502..670
FT /note="Acyl-CoA oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01756"
FT ACT_SITE 444
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000168-1"
FT BINDING 150
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000168-2"
FT BINDING 189
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000168-2"
SQ SEQUENCE 707 AA; 79420 MW; 97277A02421045FD CRC64;
MADFTDKLRP AEPQGPSILA QERAGSSVNV EQLAHHLLSR NDFLPRQKKI LSILEPIPYF
CKKNQLNMAR PDRYHLGLAR AKTLRRLSLK HGWDRDDYIM ADYLTDEMGP YALQATMFAT
SIREQCNDEQ KAYWLPKVEN WEIIGCYAQT ELGHGSNVKG IECAARWDPK TKEFIIHSPT
ITASKWWNGA LGRTANHAIV VAQLLLPDSK TGKYKSYGPH QFIVQIRDMK TNKPLDGIVI
GDIGPKYGYP GMDNGYMLFD QFRVPHSALL SKYSGVDSEH GTYIRPENPA LVYGSLTFVR
AQIIMHARLV LARAVTVAVR YLSIRRQFAD RDAKDAGAPE QAVLNYPTVQ IRILPLLATT
FALHYTGEAM YKLYYGTREA IEKSGDFSRL AEMHAASSGL KSLCTTLAAD GIETCRRAMG
GHGFGGGSGM IALNNEYLSK PTVEGDNWMI TQQTAAYLIK RMTEVVKKPD MNPNETVDVQ
FQQFMTSRGR LHDYDILGHE SELVKAFKHR ASHQSYQAYH ARVVEKKPWT SMMIQLHRLS
RAHSESLLVS NFYTAVFEST PNPPLDATAI GVMKTLFKLF ALFTLDASAS EFLLSKALSV
DRLASVTPAI QDLMAQVRPH AVRLVDAWSI PDYLLESALG SYDGDVYNRL FHKAHKENPL
NKLTFNPDWK SEEIVMGEGE ANARRRLEAL ALGMMGHEQS ESVKAKL
//