ID A0A1C1CIK4_9EURO Unreviewed; 721 AA.
AC A0A1C1CIK4;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=Acyl-coenzyme A oxidase {ECO:0000256|PIRNR:PIRNR000168};
GN Name=Acox1 {ECO:0000313|EMBL:OCT48364.1};
GN ORFNames=CLCR_03911 {ECO:0000313|EMBL:OCT48364.1};
OS Cladophialophora carrionii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC Cladophialophora.
OX NCBI_TaxID=86049 {ECO:0000313|EMBL:OCT48364.1, ECO:0000313|Proteomes:UP000094526};
RN [1] {ECO:0000313|Proteomes:UP000094526}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KSF {ECO:0000313|Proteomes:UP000094526};
RA Teixeira M.M., Souza R.C., Almeida L.G., Vicente V.A., de Hoog S.,
RA Bocca A.L., de Almeida S.R., Vasconcelos A.T., Felipe M.S.;
RL Submitted (JUL-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:OCT48364.1}.
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DR EMBL; LGRB01000012; OCT48364.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C1CIK4; -.
DR STRING; 86049.A0A1C1CIK4; -.
DR VEuPathDB; FungiDB:CLCR_03911; -.
DR VEuPathDB; FungiDB:G647_08502; -.
DR eggNOG; KOG0136; Eukaryota.
DR UniPathway; UPA00661; -.
DR Proteomes; UP000094526; 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:UP000094526}.
FT DOMAIN 20..136
FT /note="Acyl-coenzyme A oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF14749"
FT DOMAIN 506..696
FT /note="Acyl-CoA oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01756"
FT ACT_SITE 443
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000168-1"
FT BINDING 146
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000168-2"
FT BINDING 185
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000168-2"
SQ SEQUENCE 721 AA; 79131 MW; 62B28B0911B068D0 CRC64;
MALNHQKTLM AQARARGTFD TEALAQIIHG GAAALQQKRG AWSRVEEAVG ATDPDRLPDQ
YAHTSREDLY REGLQTGKAA WIDGVKHGHS LFDVITPRYG MSNASPFGIH YNLFGRTIDL
MGTPEQKRKW MPLVAQGRVN GAYIQTELGH GSNVAGIQTT ATFNPVDDTI VLHTPQLAAI
KYWPGSIGYS ATHGVVMARL LVPSPSGTAA GKPFKDYGIH PFLVQLRDPE TGQATPGLEL
GDIGLKPAYN QNDNGYLSFD NFKIPRTDML MGHCALGADG KFTRYLPAEA VYGTMLSSRT
FITFGAAFQL AYAVTIAIRY SVVREQGTLP FDSQGKASQD IPIIAYRSQQ YRLFSLLSSA
YAMSFASKIT RKIQDDLDAR LREGDYSTVT HAHGLMAGAK AWFTTVAADG AEDARKCCGG
HGYLNISGLP DIVNMVTACC TLEGDNMVMW QQTARYLMKV MDVFESVQPR TRRTLTESSQ
VPPEIAYLAN DPGILSPTPI DPASLKDLHH LSAIRAHYHV KTAHTALNEA VKEGTPKPQA
WNSYMLLLIR AAHAHISHFV LSSFYLALPT ISDAQIKPVL TQLCHLFALT QLFPQLPASS
PTTASLPPAF LYPRFEIIAS QQTNTLLEAI LPNAIALTDA WDFSDASLAS ALGCKDGDVY
ERLMSWTRQL PINARAKEAG GFDTRESWER YIKPALRIDL ERGTGRRAAD ERFGEGIRAR
L
//