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Database: UniProt
Entry: K0T1I3_THAOC
LinkDB: K0T1I3_THAOC
Original site: K0T1I3_THAOC 
ID   K0T1I3_THAOC            Unreviewed;       761 AA.
AC   K0T1I3;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=Acyl-coenzyme A oxidase {ECO:0000256|PIRNR:PIRNR000168};
GN   ORFNames=THAOC_06939 {ECO:0000313|EMBL:EJK71600.1};
OS   Thalassiosira oceanica (Marine diatom).
OC   Eukaryota; Sar; Stramenopiles; Ochrophyta; Bacillariophyta;
OC   Coscinodiscophyceae; Thalassiosirophycidae; Thalassiosirales;
OC   Thalassiosiraceae; Thalassiosira.
OX   NCBI_TaxID=159749 {ECO:0000313|EMBL:EJK71600.1, ECO:0000313|Proteomes:UP000266841};
RN   [1] {ECO:0000313|EMBL:EJK71600.1, ECO:0000313|Proteomes:UP000266841}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCMP1005 {ECO:0000313|EMBL:EJK71600.1,
RC   ECO:0000313|Proteomes:UP000266841};
RX   PubMed=22835381; DOI=10.1186/gb-2012-13-7-r66;
RA   Lommer M., Specht M., Roy A.S., Kraemer L., Andreson R., Gutowska M.A.,
RA   Wolf J., Bergner S.V., Schilhabel M.B., Klostermeier U.C., Beiko R.G.,
RA   Rosenstiel P., Hippler M., Laroche J.;
RT   "Genome and low-iron response of an oceanic diatom adapted to chronic iron
RT   limitation.";
RL   Genome Biol. 13:R66-R66(2012).
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:EJK71600.1}.
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DR   EMBL; AGNL01007023; EJK71600.1; -; Genomic_DNA.
DR   AlphaFoldDB; K0T1I3; -.
DR   EnsemblProtists; EJK71600; EJK71600; THAOC_06939.
DR   eggNOG; KOG0136; Eukaryota.
DR   OMA; ICTRFSA; -.
DR   Proteomes; UP000266841; 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; IPR006091; Acyl-CoA_Oxase/DH_mid-dom.
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; PF02770; Acyl-CoA_dh_M; 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|ARBA:ARBA00022630,
KW   ECO:0000256|PIRNR:PIRNR000168};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Peroxisome {ECO:0000256|ARBA:ARBA00023140};
KW   Reference proteome {ECO:0000313|Proteomes:UP000266841}.
FT   DOMAIN          33..171
FT                   /note="Acyl-coenzyme A oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14749"
FT   DOMAIN          173..290
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          554..725
FT                   /note="Acyl-CoA oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01756"
FT   ACT_SITE        480
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000168-1"
FT   BINDING         177
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000168-2"
FT   BINDING         222
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000168-2"
SQ   SEQUENCE   761 AA;  83911 MW;  B83090C8D95E1307 CRC64;
     MQAGDEDPRE PGNRTPMTIN EDLAEERKSL SFNPRAITNF IDGSAEATLK RRQLESWITR
     DPTGVFSNAN NNYIHRTERH TRALAKFVRL VELCRQAGIG ADNAPREGDA VTHLEGEITC
     TPEFQTLVSA CSDDPFPTSL HFVMFLPNIM TLCDAEQQAT WLPLCRDWKM IGCYAQTELG
     HGSNIRALET TATFRSEAQG GMKGGEWVIN SPTLTSAKFW PGTLGKTANH AMVIAQLIDG
     EGKERGIHNF LVPLRSMETH ELLEGVETGD IGPKIGYNNM DNGFARFDNV RIPRRNMAMR
     FAVVNEDGKY SKVTGGKGSD AASKVAYITM MQVRAYIIHL SNESLAMACT IAIRYSAIRL
     QGYNADSRQA RNEFQVLDYR QQQYRLLPLL SASYAIYFTG KHVLARLKEV ERQLVAGSEK
     ITKTISQDIH ATTSALKSFA TTFTADGIED CRKACGGHGF LVASGLVELS NTYLQTCTVE
     GDNQMLPQQV VKVLLKLVGA VQSGDEELLK EYIGTDMEYL VVILVSLMEQ GGEIPTRSTF
     SFSLDSSVQD FRDVPNLLKA FQHRAACLIL DVAIELQTSM STATEQQAWN DALLSMARAS
     RAHAAYLLLR DFANGLEDEQ VKGSSSCLGP SEDKVLTQCL TLLALYWMDK FLDDFQQIQC
     ISPSSVPQMR GALLQMLTEL RPSAVGLCDA RDFSDFRLKS ALGRWDGDVY TAIMDSARND
     PLNTESSAAG VGLGYDESLH KLIAGGVGEY HKGVSGTISR L
//
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