ID   A0A1A9BM36_9ACTN        Unreviewed;       643 AA.
AC   A0A1A9BM36;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Acyl-CoA dehydrogenase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=GA0115233_100819 {ECO:0000313|EMBL:SBT89247.1};
OS   Streptomyces sp. DI166.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1839783 {ECO:0000313|EMBL:SBT89247.1, ECO:0000313|Proteomes:UP000198690};
RN   [1] {ECO:0000313|Proteomes:UP000198690}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DI166 {ECO:0000313|Proteomes:UP000198690};
RA   Varghese N., Submissions Spin;
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974,
CC         ECO:0000256|RuleBase:RU362125};
CC   -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00009347, ECO:0000256|RuleBase:RU362125}.
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DR   EMBL; FLSP01000008; SBT89247.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1A9BM36; -.
DR   STRING; 1839783.GA0115233_100819; -.
DR   OrthoDB; 8876745at2; -.
DR   Proteomes; UP000198690; Unassembled WGS sequence.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
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; 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; 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; PTHR43884; ACYL-COA DEHYDROGENASE; 1.
DR   PANTHER; PTHR43884:SF12; COMPLEX I ASSEMBLY FACTOR ACAD9, MITOCHONDRIAL-RELATED; 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   SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU362125};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|RuleBase:RU362125};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU362125};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198690}.
FT   DOMAIN          60..166
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          171..267
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          279..437
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          621..643
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   643 AA;  70576 MW;  58ADEA418978DE78 CRC64;
     MSAPTTKPTV TEREARQVAE AAREQDWRKP SFAKELFLGR FRLDLIHPHP MPTDEATQRG
     EEFLAKLRDF LETKVDGALI EREARIPDEV ITGLKEIGAL GMKIDTKYGG LGLGQVYYNK
     ALALAGSASP AIGVLLSAHQ SIGVPQPLKL FGTPEQKERF LPRCARTDIS AFLLTEPDVG
     SDPARLAASA VPDGDDYILD GVKLWTTNGV VADLLVVMAR VPKSEGHKGG ITAFVVETNS
     PGITVENRNA FMGLRGIENG VTRFHQVRVP AANRIGPEGA GLKIALTTLN TGRLSLPASC
     VAAGKWCLKI AREWSAAREQ WGKPVAHHEA VGAKISFIAA TTFALEAVTD LASQMADEDR
     NDIRIEGALA KLYASEMGWL MADELVQIRG GRGFETADSL RARGERGVPA EQMLRDLRIN
     RIFEGSTEIM HLLIAREAVD AHLSVAGDLI DPDKSLQQKA KAGAGAGVFY AKWLPKLVAG
     QGQLPYAYGD FKHEVDLATH LRYVERTSRK LARSTFYAMS RWQGRMETKQ GFLGRIVDIG
     AELFAMSAVC VRAEHLRAQG EHGREAYQLA DAFCRQSRLR IEELFGRLWH NTDDLDRTVV
     KGVMSGTYEW LEDGIVDPST DGPWIADATP GPSERENVHR EIR
//