ID A0A0Q5VVH2_9ACTN Unreviewed; 684 AA.
AC A0A0Q5VVH2;
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 oxidase {ECO:0000313|EMBL:KQS60728.1};
GN ORFNames=ASG36_07570 {ECO:0000313|EMBL:KQS60728.1};
OS Geodermatophilus sp. Leaf369.
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Geodermatophilus.
OX NCBI_TaxID=1736354 {ECO:0000313|EMBL:KQS60728.1, ECO:0000313|Proteomes:UP000051830};
RN [1] {ECO:0000313|EMBL:KQS60728.1, ECO:0000313|Proteomes:UP000051830}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf369 {ECO:0000313|EMBL:KQS60728.1,
RC ECO:0000313|Proteomes:UP000051830};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQS60728.1, ECO:0000313|Proteomes:UP000051830}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf369 {ECO:0000313|EMBL:KQS60728.1,
RC ECO:0000313|Proteomes:UP000051830};
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 dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009347}.
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:KQS60728.1}.
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DR EMBL; LMQA01000001; KQS60728.1; -; Genomic_DNA.
DR RefSeq; WP_055761448.1; NZ_LMQA01000001.1.
DR AlphaFoldDB; A0A0Q5VVH2; -.
DR STRING; 1736354.ASG36_07570; -.
DR OrthoDB; 1144545at2; -.
DR Proteomes; UP000051830; 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; 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; 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; IPR013786; AcylCoA_DH/ox_N.
DR InterPro; IPR037069; AcylCoA_DH/ox_N_sf.
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 Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR Pfam; PF02771; Acyl-CoA_dh_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|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Reference proteome {ECO:0000313|Proteomes:UP000051830}.
FT DOMAIN 28..132
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 137..246
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 280..441
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT DOMAIN 501..644
FT /note="Acyl-CoA oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01756"
FT REGION 651..684
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 684 AA; 73927 MW; 9AB867A635811A58 CRC64;
MTSTPLPTTV DPARLTEVLD GRWAQVRRDA REQLGEEKYA PVYGETNAEA RERITGLTKD
LAATGRTALG FPRAYGGQED AGASVTSIEM LAFGDLSLMV KAGVQWGLFG GAVQLLGTER
HHERFLADII SADLMGCFAM TETGHGSDVQ QLRTTCTYDP ATETFDLHTP HDSARKDYIG
NAAKDGRMAV VFAQLVSGGE RHGVHAWLVP IRDEAGNALP GVTIGDDGAK AGLNGVDNGR
LSFDHVTVPR DMLLDRYGQV AADGTYTSSI ENETRRFFTM LGTLVRGRVS VGGSAGSATK
LALEIAVRYG DVRRQFAAPG EDREIVVNDY LVHQRKLLPA LTKTYALHFA QEELVSTMHD
VQGAADVDEA AQRELESRAA GLKAAQTWHA TATIQMAREA CGGAGYLAEN RLPALKADTD
VFTTFEGDNT VLLQLVAKGL LTGYRDAFGS LDGWGKAQFV ADQVRETVLE RTAARSLIAR
LVDAVPGRDE EVSLLDRGWQ LKAFEDREKH TLDGAIKRLR KGAATKGIKP FDIFNDVQDH
VLKTAVTHID RVVLEAFVAG IERATDPAAK ALLAKVCDLY ALTTIEADKG WFLEHGRLTP
TRAKALTGAV NQLLKELRPH MRTLVDAFAI PDAWVKSSIV DTEGARQEAM AAEDARVRAA
APAGESAVDT PDDTAVDLEM APAQ
//
