ID A0A098Y766_9ACTN Unreviewed; 680 AA.
AC A0A098Y766;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Acyl-CoA oxidase {ECO:0000313|EMBL:KGH46294.1};
GN ORFNames=IN07_12675 {ECO:0000313|EMBL:KGH46294.1};
OS Modestobacter caceresii.
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Modestobacter.
OX NCBI_TaxID=1522368 {ECO:0000313|EMBL:KGH46294.1, ECO:0000313|Proteomes:UP000029713};
RN [1] {ECO:0000313|EMBL:KGH46294.1, ECO:0000313|Proteomes:UP000029713}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KNN45-2b {ECO:0000313|EMBL:KGH46294.1,
RC ECO:0000313|Proteomes:UP000029713};
RA Bukarasam K., Bull A., Girard G., van Wezel G., Goodfellow M.;
RT "Biosystematic studies on Modestobacter strains isolated from extreme
RT hyper-arid desert soil and from historic building.";
RL Submitted (JUL-2014) 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:KGH46294.1}.
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DR EMBL; JPMX01000053; KGH46294.1; -; Genomic_DNA.
DR RefSeq; WP_036336177.1; NZ_JPMX01000053.1.
DR AlphaFoldDB; A0A098Y766; -.
DR STRING; 1522368.IN07_12675; -.
DR OrthoDB; 1144545at2; -.
DR Proteomes; UP000029713; 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:UP000029713}.
FT DOMAIN 50..132
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 138..247
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 281..442
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT DOMAIN 502..640
FT /note="Acyl-CoA oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01756"
FT REGION 660..680
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 680 AA; 73611 MW; 4872EF201ED9CB55 CRC64;
MTSTPTPLPP VDPTRLTEVL DGRWAQVRRD SRAQLDDPRW APVYGESMAE ARERVTALAA
ELATTGRVAY GFPVEYGGAD DAGGSVTSIE MLALTDLSLM VKAGVQWGLF GGAVQALGTK
RQHDRYLPDI MSFALPGCFA MTETGHGSDV QQLRTTCTYD PATQTFDLHT PHEAARKDYI
GNAAKDGRMA VVFAQLITQG EGRGVHAFLV PIRAADGAPV PGVTIGDDGP KAGLLGVDNG
RLTFDHVSVP RDMLLDRYGQ VAADGTYTSS IENETRRFFT MLGTLVRGRV SVGGSAGSAT
KVALEIAVRY GDTRRQFSAP GEDREVVIND YLVHQRKLLP ALAKTYALSF AQEELTSTMH
DVLGSADVDE AAQRELESRA AGIKAVTTWH ATRTIQLCRE ACGGAGYLAE NRLPTLKADT
DVFTTFEGDN TVLMQLVAKG LLTGYRDAFG SLDGWGRAAF VAEQVRETVL ERTAARGLIQ
RLVDAVPGRD EDVSMLDRGW QLAAFEDREK HLLESAIRRL RGGAAAKKDR PFEIFNDVQD
HVLTMAEAHI DRVVLEAFVA GIERTTDPAA KALLARVCDL YALSTIEADK GWFLEHGRLT
PTRAKALTGV VNDLLKELRP HMRTLVDGFA IPESWLNCAI VAEEPGRQEA MAAHDAALRS
AGAQPQQDAT ATALEMAPAQ
//
