ID T1IV85_STRMM Unreviewed; 657 AA.
AC T1IV85;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Acyl-coenzyme A oxidase {ECO:0000256|PIRNR:PIRNR000168};
OS Strigamia maritima (European centipede) (Geophilus maritimus).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Myriapoda; Chilopoda;
OC Pleurostigmophora; Geophilomorpha; Linotaeniidae; Strigamia.
OX NCBI_TaxID=126957 {ECO:0000313|EnsemblMetazoa:SMAR005078-PA, ECO:0000313|Proteomes:UP000014500};
RN [1] {ECO:0000313|Proteomes:UP000014500}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Brora {ECO:0000313|Proteomes:UP000014500};
RA Richards S.R., Qu J., Jiang H., Jhangiani S.N., Agravi P., Goodspeed R.,
RA Gross S., Mandapat C., Jackson L., Mathew T., Pu L., Thornton R., Saada N.,
RA Wilczek-Boney K.B., Lee S., Kovar C., Wu Y., Scherer S.E., Worley K.C.,
RA Muzny D.M., Gibbs R.;
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:SMAR005078-PA}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (FEB-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}.
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DR EMBL; JH431578; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; T1IV85; -.
DR STRING; 126957.T1IV85; -.
DR EnsemblMetazoa; SMAR005078-RA; SMAR005078-PA; SMAR005078.
DR eggNOG; KOG0135; Eukaryota.
DR HOGENOM; CLU_014629_4_2_1; -.
DR OMA; VWAQLYT; -.
DR OrthoDB; 5777at2759; -.
DR PhylomeDB; T1IV85; -.
DR Proteomes; UP000014500; 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:UP000014500}.
FT DOMAIN 144..254
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 388..449
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT DOMAIN 491..652
FT /note="Acyl-CoA oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01756"
FT ACT_SITE 435
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000168-1"
FT BINDING 148
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000168-2"
FT BINDING 187
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000168-2"
SQ SEQUENCE 657 AA; 73712 MW; 6F95329993C957E9 CRC64;
MAFKFATHEP LTPFRAKASF NWKNMKLYIE DEETLAIKEK IFQDLILHNV LNSIHPDKEK
ADDLKRHTYN LSAYCSLNYD KFIKPFETNL AKTLPSLFFV FCLNHAVSYK VGLSRLVSVT
ILKSIGTSTE KAIENISSGK WHSCISLTEI GHGSNLMNLQ TTATYDAKTK TFVLHSPTIE
AWKCWSGNLG KGATHALVLA QLYTPDGQCH GIHWFFTPVR DPNTLKPYPG VIVGDMGEKI
GINGLDNGFM AFTNYHIPKK TLLNGISDVT LDGQFVTKVP NHVKRFALTA SNLNASRTCI
LGLTCFGMHT QSIIIAIRYA FAAGKSETSI NCPHQQLRLF PHLSSAYVLG IVVKSFLENL
WNYQSKVFTD GIDDEKLYVE AADTHVIVTG LKAITTSAAA KCIQEAIEYC GGHAYLEAAG
LGTLRNDIDA NVTLEGDNNI LLQQISKTLL KLSQNKQKAK EQSNLGLYDF IEEMDATLDR
KCDNNRLEMT PEVIKSAYNW LLCYLLNECS MKMASNMTNG ANSFDAFNKI QVYDCNVLSN
AFMENFIITR YFEWLNQNKP PEDCQSPLIN LGLLYSFCCL EKHMLALCKE QYFSWDAVDI
VQNYILNLCD RLKDDAVSLA DVLAPPDEML NSILGKSDGE INKRVVASYM NNLQRPK
//
