ID   A0A1E3SNU0_9MYCO        Unreviewed;       781 AA.
AC   A0A1E3SNU0;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:ODR03855.1};
GN   ORFNames=BHQ21_19720 {ECO:0000313|EMBL:ODR03855.1};
OS   Mycobacterium sherrisii.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium simiae complex.
OX   NCBI_TaxID=243061 {ECO:0000313|EMBL:ODR03855.1, ECO:0000313|Proteomes:UP000094224};
RN   [1] {ECO:0000313|Proteomes:UP000094224}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BC1_M4 {ECO:0000313|Proteomes:UP000094224};
RA   Greninger A.L., Jerome K.R., Mcnair B., Wallis C., Fang F.;
RL   Submitted (SEP-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   -!- 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:ODR03855.1}.
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DR   EMBL; MIHC01000039; ODR03855.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1E3SNU0; -.
DR   STRING; 243061.AWC25_16555; -.
DR   Proteomes; UP000094224; Unassembled WGS sequence.
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   CDD; cd00567; ACAD; 1.
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; 2.
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:SF3; ACYL-COA DEHYDROGENASE FADE29; 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};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000094224}.
FT   DOMAIN          7..119
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          224..364
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
FT   DOMAIN          390..492
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          496..584
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          602..761
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   781 AA;  82854 MW;  9DB0788A35F8BC86 CRC64;
     MSFMPGEDAE SLREVVRQFL EKRSPETEVR RLMETTAGYD PVVWTQAAVE LGLHGLVLPE
     HHGGGGASPV ELGVVFEEMG SVLFCGPFLA TVGLAATALL EIGDEQAQAA YLPDIAAGKT
     VATLAWSGDE PTASTLRASC DGNNWRVSGT ADIVIDGASA DLVLVAARTA RGLTLFAVQG
     NDTNLTRTPL MTMDSTRKLT ELTFDFTAAT LIGSDGAATS AMRRTADLAA LYLAAEQLGG
     ATRVLATTVD YARTRVQFGR PIGSFQAIKH RCADMLVDVE AARSVVWHGL WTAVHDPARL
     SLSAALARSL ASDAYQRVAT DSLQIHGGIG FTWEHPAHLY LKRAKSTQLL LGSPARHRAR
     LATQLGGDVS PRPIAAKPVL SANAGVVALQ AEVDEFLAAN PVPPTTDPLA DRVFREARFD
     AGLAMVHFGV GYGGRGLDAS LQSAVEERFA DAGAVDHGAR NVIGLGMALP TIHAHGTEMQ
     RARFLRPGFS GEHIWCQLFS EPTAGSDLAA LATRAVPDGD DFVVTGQKVW TSLGHVADWG
     ILLARTDPDV PKHKGLTFFL LDMKSPGVEV RPLRQLTGEA EFNEVFLTEV RIPGANVLGT
     VGKGWQVAMT TLANERVALG GRPATRGSGP IGQAVATYQQ AVAAGRVDPV LTDRLASLWA
     RAEAARLTNV RAAAQVGRVP GPEGSIAKLQ MAELNKAIYE LCVDLSGSAG LLVDGYIDKA
     PDFASVHGGG DVRKAYLRSL ANSIEGGTSE VLRNILGERV LGLPGEPRVD RDIPWKEVRR
     S
//