ID   A0A1H1U1Z4_9ACTN        Unreviewed;       647 AA.
AC   A0A1H1U1Z4;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Acyl-coenzyme A oxidase {ECO:0000313|EMBL:SDS66565.1};
GN   ORFNames=SAMN04488570_2396 {ECO:0000313|EMBL:SDS66565.1};
OS   Nocardioides scoriae.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Nocardioidaceae; Nocardioides.
OX   NCBI_TaxID=642780 {ECO:0000313|EMBL:SDS66565.1, ECO:0000313|Proteomes:UP000198859};
RN   [1] {ECO:0000313|Proteomes:UP000198859}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22127 {ECO:0000313|Proteomes:UP000198859};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) 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   ---------------------------------------------------------------------------
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; LT629757; SDS66565.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H1U1Z4; -.
DR   STRING; 642780.SAMN04488570_2396; -.
DR   OrthoDB; 1144545at2; -.
DR   Proteomes; UP000198859; Chromosome i.
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}.
FT   DOMAIN          23..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          500..640
FT                   /note="Acyl-CoA oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01756"
SQ   SEQUENCE   647 AA;  70563 MW;  B9EE09E5BEB373B9 CRC64;
     MSESPQVTVD VPALSRLLDG EHAEVRNLVR KNLVEQADVL DDQVHLDATA FRERVKDVIQ
     HMASTGATGL GFPQEHGGGG NVGASIAAFE TLAFGDLSVL VKAGVQFGLF GGAVLQLGTK
     RHHDAYLRDL IEARLLGCFA MTESGHGSNV QHLGTVATYD VETREFVITT TTESARKDYI
     GNAAAHASHA AVFAVLEIDG ESQGVHAFVV PIRDAEGHDL PGVRTGDDGA KMGLHGVDNG
     RLWFDGVRVP RENLLNRYAD VSEDGVYSSD IENPDRRFFT MLGTLVQGRV SVGGAGVSAS
     KVALTIAVKY ALKRRQFGAP GSDEEELLLD YGLHQRRLLP RLATSYALHF AQEVLVAQLH
     QASTDPDYPE RDRRALESRA AGTKALATWH ATDSIQEGRE ACGGAGYLAA NRFAALKADT
     DVFTTFEGDN HVLLQLVAKG LLTDYSTNFE ELDQFGVARF VADLAVETVI ERTAVHKLLE
     RLRDVLPSSD DGSDEPTLLD PDYQLAMLRW REEHVLSGVA RRLKRGIDGG TDPVAVFSQV
     QDHVIHAARS HMERLVLEAF TDKVAAASED PNHDVLAAVR DLYALSTIEA DRAWWMEHGR
     LSSARSKAVT REVNALCRRL RPVADDLVDG FAIPPEMLRA EMLEQGY
//