ID   A0A1C4SVP6_9ACTN        Unreviewed;       350 AA.
AC   A0A1C4SVP6;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:SCE51139.1};
GN   ORFNames=GA0115242_144321 {ECO:0000313|EMBL:SCE51139.1};
OS   Streptomyces sp. SolWspMP-5a-2.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1838281 {ECO:0000313|EMBL:SCE51139.1, ECO:0000313|Proteomes:UP000199131};
RN   [1] {ECO:0000313|EMBL:SCE51139.1, ECO:0000313|Proteomes:UP000199131}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SolWspMP-5a-2 {ECO:0000313|EMBL:SCE51139.1,
RC   ECO:0000313|Proteomes:UP000199131};
RA   Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00009347}.
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DR   EMBL; FMCI01000381; SCE51139.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1C4SVP6; -.
DR   OrthoDB; 2450120at2; -.
DR   Proteomes; UP000199131; 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   Gene3D; 1.10.540.10; Acyl-CoA dehydrogenase/oxidase, N-terminal domain; 1.
DR   Gene3D; 1.20.140.10; Butyryl-CoA Dehydrogenase, subunit A, domain 3; 1.
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:SF20; ACYL-COA DEHYDROGENASE FADE28; 1.
DR   Pfam; PF00441; Acyl-CoA_dh_1; 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};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022827}.
FT   DOMAIN          7..90
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          203..324
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   350 AA;  37283 MW;  6BD631EC3876F8F6 CRC64;
     MNNSDSEREL VVRTVQDILD ARPVTTDEGR RERWDADLWA LLADSDMTAV GIAETHGGAG
     GAFGDAAAIV SCLAAAGAAV PLAEHLLVVA PALAGTSLAP SDLMAPVTFA RGGQAVADGE
     GYYRLNGELP DVAWGDVASR AAVLVQVGTT GALVLAETHG HVVKRTANLA DEPRATLAFD
     DVRLPGVPLT AQQVEAIDAR MALARAVQLT GALHQVFDWT CEYARERTQF GRPLSDFPTV
     RTDLVRMAGE VAAATALTEA AVEAAPHNWD ILPAAAAKIR AGAAVEVVAR SAHQIHGAIG
     FTREHRLHHL TRRLWAWREE AGTERHWSQV LGGHLRPKHQ ALWPQLVDAV
//