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Database: UniProt
Entry: A0A0D2BA48_9EURO
LinkDB: A0A0D2BA48_9EURO
Original site: A0A0D2BA48_9EURO 
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
//
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