ID   A0A0Q6QBH5_9MICO        Unreviewed;       675 AA.
AC   A0A0Q6QBH5;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:KQV08397.1};
GN   ORFNames=ASC63_06475 {ECO:0000313|EMBL:KQV08397.1};
OS   Leifsonia sp. Root112D2.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Leifsonia.
OX   NCBI_TaxID=1736426 {ECO:0000313|EMBL:KQV08397.1, ECO:0000313|Proteomes:UP000051914};
RN   [1] {ECO:0000313|EMBL:KQV08397.1, ECO:0000313|Proteomes:UP000051914}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root112D2 {ECO:0000313|EMBL:KQV08397.1,
RC   ECO:0000313|Proteomes:UP000051914};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQV08397.1, ECO:0000313|Proteomes:UP000051914}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root112D2 {ECO:0000313|EMBL:KQV08397.1,
RC   ECO:0000313|Proteomes:UP000051914};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SIMILARITY: Belongs to the acyl-CoA oxidase family.
CC       {ECO:0000256|ARBA:ARBA00006288}.
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:KQV08397.1}.
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DR   EMBL; LMCU01000001; KQV08397.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0Q6QBH5; -.
DR   STRING; 1736426.ASC63_06475; -.
DR   Proteomes; UP000051914; 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: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; 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:SF378; ACYL-COENZYME A OXIDASE-LIKE PROTEIN; 1.
DR   PANTHER; PTHR10909; ELECTRON TRANSPORT OXIDOREDUCTASE; 1.
DR   Pfam; PF01756; ACOX; 1.
DR   Pfam; PF00441; Acyl-CoA_dh_1; 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};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022827};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051914}.
FT   DOMAIN          365..440
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
FT   DOMAIN          504..638
FT                   /note="Acyl-CoA oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01756"
FT   REGION          638..675
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        645..675
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   675 AA;  73504 MW;  EBE47C9988FA4640 CRC64;
     MDAGVPATVN VPALSRQLLG SWPEVRLAAR EVAARPEMQR IDGLSMQEHR ERAFGQLKLL
     VDNGQVHRAF PKSLGGEEDH GGNIAGFEEL VTADPSLQIK SGVQWGLFGA AVLHLGTERH
     HTAFLPAIMS LAVPGAFAMT EIGHGSDVAS IATTATYIPE TQEFEIHTPF RAAWKEYNGN
     AAVDGKAAVV FAQLITQGVN HGVHAVYVPL RGDDGELLPG VSSEDDGLKG GLNGIDNGRL
     AFENVRVPRV NLLNRYGDVA EDGTYTSPIS SPGRRFFTML GTLVQGRVSL DGAAVAASKV
     GLAIAITYGN QRRQFTAGSD TDEEVLLDYQ RHQRRLLPRL ATTYAAGFAH DSLLVKFDEV
     FSNKAATDDE RQDLETLAAA LKSLSTWHAL DTLQEAREAC GGAGFMAENR LVGLRSDLDV
     YVTFEGDNNV LLQLVAKRLL TDYSRGFAKA DAGALARYVV KQAAGKAYHG SGLRGLAQTV
     ADFGSTARSV DQLRETNAQR ELLTDRVETM IADVAGRLRS ASKLPKQQAA DLFNSQQNEL
     IEAARAHGEL LQWEAFTDAL EQVTDAGTRQ VLVWLRDLFG LGLLEKHLAW YLIHGRLSPQ
     RAQAVSAYID RLVARLRPHA QDLVDAFGYT QEHLRAPVAS GAEAERQNEA REYYREERAS
     GTAPVDEKTL KPKKK
//