ID A0A1X1YUB3_9MYCO Unreviewed; 650 AA.
AC A0A1X1YUB3;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Acyl-CoA oxidase {ECO:0000313|EMBL:ORW14679.1};
GN ORFNames=AWC17_00405 {ECO:0000313|EMBL:ORW14679.1};
OS Mycobacterium nebraskense.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=244292 {ECO:0000313|EMBL:ORW14679.1, ECO:0000313|Proteomes:UP000193781};
RN [1] {ECO:0000313|EMBL:ORW14679.1, ECO:0000313|Proteomes:UP000193781}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44803 {ECO:0000313|EMBL:ORW14679.1,
RC ECO:0000313|Proteomes:UP000193781};
RA Tarcisio F., Conor M., Antonella G., Elisabetta G., Giulia F.S., Sara T.,
RA Anna F., Clotilde B., Roberto B., Veronica D.S., Fabio R., Monica P.,
RA Olivier J., Enrico T., Nicola S.;
RT "The new phylogeny of the genus Mycobacterium.";
RL Submitted (JAN-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 -!- 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:ORW14679.1}.
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DR EMBL; LQPH01000179; ORW14679.1; -; Genomic_DNA.
DR RefSeq; WP_046183069.1; NZ_LQPH01000179.1.
DR AlphaFoldDB; A0A1X1YUB3; -.
DR STRING; 244292.ABW17_08045; -.
DR OrthoDB; 1144545at2; -.
DR Proteomes; UP000193781; 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}.
FT DOMAIN 50..129
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 134..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 501..631
FT /note="Acyl-CoA oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01756"
SQ SEQUENCE 650 AA; 71675 MW; 88DEDCF24334ADF2 CRC64;
MAPDTTTIAE QLRNALDGRW RDTRNQLRST MSEDLFRPHY TPNTVIARTK VAEQMRIMAA
FGAAADNFRK EHGGTGDIGA AITMIEMLAM SDLSLMVKAG VQWGLFGGAV ENLGTERHHE
AYVKKIISLE LRGCFAMTET GHGSDVQSLE TTATYDPATE EFVIDSPTPT ARKDYIGGAA
ETATMAAVFA QLITTEDGKP VQHGVHCLMV PIRDADGNDL PGVTTSDCEY KGGLPGVDNG
RIVFDHVRVP RVNLLNKYGD VAPDGTYTSP IENPNRRFFT MLGTLVRGRI TVGGSAGAAG
RVALDIATRY ALQRKQFSAP DDESEVLIMD YLVHQRRLFP LIAKSYALQF AQNELVSKCH
DIQTADAVDA DEQRELEARA AGLKAANTWH ASRAIQESRE ACGGAGYMAE NRLVALRGDT
DVFTTFEGDN HVLTQLVAKE LLTAYADDIR SMSPVEWVRF AANTVGERVV KRTAAETIIQ
TIVDARQDSE EEGSLFNRGT QIKMFEDREE YLLASVARRL QVKSKEMPEF DAFNAVQDHV
LHAASAHIDR VVLEAFVAGI DACPHEEARE LLGILCDLYA LSVIEDDKAW YIEHRYLSTE
RAKAVTRGIN DRCRALRPHA ETLVDGFGIP EQLRYAEMLH PENLPDAVTS
//
