ID T1K448_TETUR Unreviewed; 708 AA.
AC T1K448;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Acyl-coenzyme A oxidase {ECO:0000256|PIRNR:PIRNR000168};
OS Tetranychus urticae (Two-spotted spider mite).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Acariformes; Trombidiformes; Prostigmata; Eleutherengona; Raphignathae;
OC Tetranychoidea; Tetranychidae; Tetranychus.
OX NCBI_TaxID=32264 {ECO:0000313|EnsemblMetazoa:tetur05g01320.1, ECO:0000313|Proteomes:UP000015104};
RN [1] {ECO:0000313|Proteomes:UP000015104}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=London {ECO:0000313|Proteomes:UP000015104};
RA Rombauts S.;
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:tetur05g01320.1}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (JUN-2015) to UniProtKB.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- PATHWAY: Lipid metabolism; peroxisomal fatty acid beta-oxidation.
CC {ECO:0000256|ARBA:ARBA00004846}.
CC -!- SIMILARITY: Belongs to the acyl-CoA oxidase family.
CC {ECO:0000256|ARBA:ARBA00006288, ECO:0000256|PIRNR:PIRNR000168}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CAEY01001565; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; T1K448; -.
DR STRING; 32264.T1K448; -.
DR EnsemblMetazoa; tetur05g01320.1; tetur05g01320.1; tetur05g01320.
DR eggNOG; KOG0135; Eukaryota.
DR HOGENOM; CLU_014629_4_2_1; -.
DR OMA; ERASWWQ; -.
DR Proteomes; UP000015104; Unassembled WGS sequence.
DR GO; GO:0005777; C:peroxisome; IEA:InterPro.
DR GO; GO:0003997; F:acyl-CoA oxidase activity; IEA:InterPro.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0009058; P:biosynthetic process; IEA:UniProt.
DR GO; GO:0006635; P:fatty acid beta-oxidation; IEA:InterPro.
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; 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; IPR009075; AcylCo_DH/oxidase_C.
DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom_sf.
DR PANTHER; PTHR10909; ELECTRON TRANSPORT OXIDOREDUCTASE; 1.
DR PANTHER; PTHR10909:SF352; PEROXISOMAL ACYL-COENZYME A OXIDASE 3; 1.
DR Pfam; PF01756; ACOX; 1.
DR Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR Pfam; PF02770; Acyl-CoA_dh_M; 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|ARBA:ARBA00022827, ECO:0000256|PIRNR:PIRNR000168};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|PIRNR:PIRNR000168};
KW Reference proteome {ECO:0000313|Proteomes:UP000015104}.
FT DOMAIN 158..268
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 395..462
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT DOMAIN 510..698
FT /note="Acyl-CoA oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01756"
FT ACT_SITE 453
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000168-1"
FT BINDING 162
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000168-2"
FT BINDING 201
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000168-2"
SQ SEQUENCE 708 AA; 79357 MW; F3B122F9CB8132CE CRC64;
MLSPTDLDVD SVIECIPDWP KGPLDDARAK ATFDWKTMRL VLDGDTVVCF KHKVWSVLAN
DPIFKRTPWE EYNRDEERRL TFLRLKRLVD YKLASEEEYL NQPHKIPAFV QAVGQFSWSL
IVKRVLSYEY FIVSCKMDNG DRDNSLVDDI MNFNALGAIS ITELAHGSNT KELQTTATYD
PVNQTFILNT PRLEATKVWS GVLGQTATHV VVFAQLYTPD GACHGLHSFM VPVRDAKTYE
PYPGIRIGDM GGKVGLNGLD NGFMTFKNYP IPKAALMNRN SDVTQDGKYT LKVRDESKRF
GITLGVLSSG RIFIILFSIS NLQSALTIAV RYSAVRRQFG PSNGEEIPVL EYQSQQWRLI
PYIAASYVLQ NFFGSLFLDY VDFFVTAFNA TSDAQMDMGA EIHSLSSCGK AVATWMARDA
IQECRECCGG HGYLKAAGFG EIRNDHDANP TYEGDNNVLL QQTSNYLIKF YKEKVEEGHS
ISSYFGSVNY LDSIDSILST QCSGNLDTIP KVLDAYHFIV CYLLRSSYLK LANQTSTLGD
PFSAKNATQV YYLRSLAIVF FEAEALDRFQ RFIDEFPAPE EISVVLKQLG LLYGLWSIEK
HMSILYESGY FPQSSVKSSP QSSLLIGPST HIKETILRLC NELKDNAVAL VDSFAPPDHI
LNSSLGASDG RIYENIFAAL ENNTGAFIKP EWLEQISKST SASLKSKL
//
