ID A0A368T9V6_9ACTN Unreviewed; 652 AA.
AC A0A368T9V6;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Acyl-CoA oxidase {ECO:0000313|EMBL:RCV61547.1};
GN ORFNames=DEF24_04010 {ECO:0000313|EMBL:RCV61547.1};
OS Marinitenerispora sediminis.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Nocardiopsaceae; Marinitenerispora.
OX NCBI_TaxID=1931232 {ECO:0000313|EMBL:RCV61547.1, ECO:0000313|Proteomes:UP000253318};
RN [1] {ECO:0000313|EMBL:RCV61547.1, ECO:0000313|Proteomes:UP000253318}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TPS81 {ECO:0000313|EMBL:RCV61547.1,
RC ECO:0000313|Proteomes:UP000253318};
RA Ng Z.Y., Tan G.Y.A.;
RT "Novel actinobacteria from marine sediment.";
RL Submitted (APR-2018) 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:RCV61547.1}.
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; QEIN01000018; RCV61547.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A368T9V6; -.
DR OrthoDB; 1144545at2; -.
DR Proteomes; UP000253318; 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; 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: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 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:UP000253318}.
FT DOMAIN 136..245
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 279..443
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT DOMAIN 505..641
FT /note="Acyl-CoA oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01756"
SQ SEQUENCE 652 AA; 71214 MW; 8F1C6F90827C53C8 CRC64;
MAITTEPDRI DVEALRTLLD GRWAHVRRLA RDTLRGELFA PVYGLDMAAH RERVARQLAA
LAETEIPSYG FPASVGGRDD VGASMVAFEM LVCDLSLMVK VGVQWGLFGG AVQSLGTEPH
HRAYLAKIMS VELPGCFAMT ETGHGSDVQR LRTTAEYDRA AEEFVVTTPD EAARKDYIGN
AARDGRMAVV FAQLVTRGER HGVHALLVPI RDEAGRPLPG VRIEDCGPKA GLNGVDNGRL
WFDRVRVPRA ALLNRYGDVD ADGTYRSPIA NPNRRFFTML GTLVRGRISV AGGANSAAKA
ALAIAVRYAD ARRQFERPGG EGPASEVPLL DYLAHQRRLL PALATSYALH FAQEELVSTL
HDGWTGTPLD EHRQRELEAR AAGLKAVATW HTTRTVQECR EACGGAGYLA ENRLPQLKAD
SDVYTTFEGD NTVLLQLVAK GLLTNYREEF GSLDAFGMAR FAAGQFVGAV IERTAARALI
DRLVGAAPGR GEEADLYDRA WQYRLLEDRE RHVVEGLARR LRGAGSDPAT AFAAFNDAQD
HVLKAGRAHV DRVVLEAFIA AIDRCVNPDA RWVLDRLCDL YVLSLVEADR AWFLEHGRLT
PARAKAVTAA VNSLCRRLRP HAAALIDAFG LPDAWLAAPI ALGAEVDRRR GG
//