ID   A0A2S8LCR6_9MYCO        Unreviewed;       706 AA.
AC   A0A2S8LCR6;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:PQP49306.1};
GN   ORFNames=C6A82_10160 {ECO:0000313|EMBL:PQP49306.1};
OS   Mycobacterium sp. ITM-2016-00318.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=2099693 {ECO:0000313|EMBL:PQP49306.1};
RN   [1] {ECO:0000313|EMBL:PQP49306.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ITM-2016-00318 {ECO:0000313|EMBL:PQP49306.1};
RA   Meehan C.J., Cogneau S., Rigouts L., Shojaei H., Azadi D.;
RT   "Bioremediation-capable novel species from Iranian environmental samples:
RT   Mycobacterium khaydaluicum sp. nov., Mycobacterium meyganicum sp. nov.,
RT   Mycobacterium omidicum sp. nov., Mycobacterium seymaricum sp. nov.,
RT   Mycobacterium austroafricanum subspecies dezhpoolicum subsp. nov.";
RL   Submitted (FEB-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 dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00009347}.
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:PQP49306.1}.
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DR   EMBL; PUTV01001275; PQP49306.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S8LCR6; -.
DR   OrthoDB; 2431337at2; -.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
DR   Gene3D; 1.10.540.10; Acyl-CoA dehydrogenase/oxidase, N-terminal domain; 2.
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; 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; PTHR43292; ACYL-COA DEHYDROGENASE; 1.
DR   PANTHER; PTHR43292:SF4; ACYL-COA DEHYDROGENASE FADE34; 1.
DR   Pfam; PF00441; Acyl-CoA_dh_1; 2.
DR   Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR   Pfam; PF02771; Acyl-CoA_dh_N; 2.
DR   SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 2.
DR   SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 2.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630}.
FT   DOMAIN          9..94
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          208..336
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
FT   DOMAIN          368..453
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          457..551
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          563..702
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   706 AA;  74646 MW;  82616486A6A578E7 CRC64;
     MSQASATGTD EQFAARELVR SWAAGAKAVE AARRIENGEA DAWRAPYAGL AQLGIFGVAL
     PEECGGAGGT VDDLCAMVDE AAAAMVPGPI ATTAIATLVI PGSRAELLDA LASGERTAGL
     ALTADVKLDG GTASGTADCV LGGDSEGVLL LPAGDEFVLV DAAAGGVTVE PLTPTDFSRP
     LARVVLDGAV AEVLPAGRQR VEDIVATVHA AEAAGVARWT LQTATEYAKV REQFGKPIGS
     FQAVKHMCAE MLLRSEQVAV AAGDAARAAN GDDDAQLSIA ASVAAAAGIE MAKANAKDCI
     QVLGGIGITW EHDAHLYLRR AYGISQFLGG PSRWLRRVAT LTQRGVRREL HIDLASVEHL
     QPEIAAAVAD VAAQPVEKRQ IALAEAGLQA PHWPKPYGRD ASPAEQLLID RELADAGVER
     PDLVIGWWAA PTIIEHGSKE QIERFVPPTL SGELFWCQLF SEPGAGSDLA SLRMKAVRAE
     GGWKLTGQKV WTSRADRAQW GVCLARTDPD APKHKGITYF LVDMSTPGID IRPLREITGD
     DLFNEVFFDD VFVPDEMVVG QVNDGWRLAR TTLANERVAM AHGTALGNPM EEVLRTVAER
     DLDPAVQDGL GRLIIAAQVG SLLDQRIAEL AVGGADPGPQ ASARKLIGVR YRQALSEFRM
     DLSEGAGLVQ NKPVLDFLNV RCLTIAGGTE QILLTMAGER LLGLPR
//