ID A0A067RG67_ZOONE Unreviewed; 721 AA.
AC A0A067RG67;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Acyl-coenzyme A oxidase {ECO:0000256|PIRNR:PIRNR000168};
GN ORFNames=L798_07731 {ECO:0000313|EMBL:KDR18054.1};
OS Zootermopsis nevadensis (Dampwood termite).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Polyneoptera; Dictyoptera; Blattodea; Blattoidea; Termitoidae;
OC Termopsidae; Zootermopsis.
OX NCBI_TaxID=136037 {ECO:0000313|EMBL:KDR18054.1, ECO:0000313|Proteomes:UP000027135};
RN [1] {ECO:0000313|EMBL:KDR18054.1, ECO:0000313|Proteomes:UP000027135}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Whole organism {ECO:0000313|EMBL:KDR18054.1};
RX PubMed=24845553; DOI=10.1038/ncomms4636;
RA Terrapon N., Li C., Robertson H.M., Ji L., Meng X., Booth W., Chen Z.,
RA Childers C.P., Glastad K.M., Gokhale K., Gowin J., Gronenberg W.,
RA Hermansen R.A., Hu H., Hunt B.G., Huylmans A.K., Khalil S.M.,
RA Mitchell R.D., Munoz-Torres M.C., Mustard J.A., Pan H., Reese J.T.,
RA Scharf M.E., Sun F., Vogel H., Xiao J., Yang W., Yang Z., Yang Z., Zhou J.,
RA Zhu J., Brent C.S., Elsik C.G., Goodisman M.A., Liberles D.A., Roe R.M.,
RA Vargo E.L., Vilcinskas A., Wang J., Bornberg-Bauer E., Korb J., Zhang G.,
RA Liebig J.;
RT "Molecular traces of alternative social organization in a termite genome.";
RL Nat. Commun. 5:3636-3636(2014).
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; KK852704; KDR18054.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A067RG67; -.
DR STRING; 136037.A0A067RG67; -.
DR EnsemblMetazoa; KDR18054; KDR18054; L798_07731.
DR eggNOG; KOG0135; Eukaryota.
DR InParanoid; A0A067RG67; -.
DR OMA; ERASWWQ; -.
DR OrthoDB; 5777at2759; -.
DR Proteomes; UP000027135; 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:UP000027135}.
FT DOMAIN 180..290
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 327..488
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT DOMAIN 536..713
FT /note="Acyl-CoA oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01756"
FT ACT_SITE 476
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000168-1"
FT BINDING 184
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000168-2"
FT BINDING 223
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000168-2"
SQ SEQUENCE 721 AA; 80576 MW; FBDA6AA72B2CCEEC CRC64;
MISSRKCMWM TGRSQVFLNG FVKKCFSSMT RRMGENELLP DFPPGPLDVY RKQASFDWKK
LKLFLEDETI TGFKMKIWGT LEADPLFQHP QSSLSLDEQR HLATRQMYRI KQYNFLPLEE
LAADIRKIFA MNSALFQMNP SFAVKFLLTF SMFSNTISSM GTARHYHFVE AIDEGTIGGC
FALTEISHGT NTKGLRTTAT YDPKTQEFII HTPDFEAAKC WVGSLGKCCT HAIIYAQLFT
ADGTNHGLHA FVVPIRNTKT LCAFPGVIVG DLGEKIALNG VDNGFVIFQN YRIPRENLLN
KTGDVSLEGQ YISTIKDPKK RMGASFGALS NGRVSIIGIC MSYLTSAVTI AVRYSAVRKQ
FGPENGNEFP VLEYQLQQSR LLPHLAAAFA MKIFSDYFNK IIGDFTVKTM MGDKSDEMAD
LGMEIHALSS AGKPLAGWTA KDAIQDCREA CGGHGYLKVS GLGDLRNAND ANCTYEGENN
VLLQQTSNWL LQLWNNKIRT RGGPISTPMG SADFLTNIDE ILKTRFVAKT VEETVNPEVL
LAAYKWLVCW LLQATANKIE SQNQIGKDMF SAKNDSQVFF AKTLSLAFIE HFILHNFLTH
ITSDGLDTQV KAVLLKLCSL YGAYSLEKHL VALYQGGYAV GSEPAQLLRD GILDLFSKLK
PEAVALVDVL APPDFVLNSV LGKSDGKVYQ NLQATLFQNP QVFERPSWWE DVVHWRQHSK
L
//
