ID   A0A2G5II30_9ACTN        Unreviewed;       414 AA.
AC   A0A2G5II30;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:PIB04302.1};
GN   ORFNames=B1C81_33425 {ECO:0000313|EMBL:PIB04302.1};
OS   Streptomyces sp. HG99.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1958787 {ECO:0000313|EMBL:PIB04302.1, ECO:0000313|Proteomes:UP000231274};
RN   [1] {ECO:0000313|EMBL:PIB04302.1, ECO:0000313|Proteomes:UP000231274}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HG99 {ECO:0000313|EMBL:PIB04302.1,
RC   ECO:0000313|Proteomes:UP000231274};
RA   Li Y.;
RT   "Diversity and bioprospecting of biosynthetic gene clusters of culturable
RT   actinobacteria from Tibetan Plateau, China.";
RL   Submitted (FEB-2017) 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}.
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:PIB04302.1}.
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DR   EMBL; MVDM01000034; PIB04302.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G5II30; -.
DR   Proteomes; UP000231274; Unassembled WGS sequence.
DR   GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IEA:InterPro.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
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; 1.
DR   InterPro; IPR006089; Acyl-CoA_DH_CS.
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.
DR   PROSITE; PS00073; ACYL_COA_DH_2; 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|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU362125};
KW   Reference proteome {ECO:0000313|Proteomes:UP000231274}.
FT   DOMAIN          9..115
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          126..223
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          263..408
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   414 AA;  44819 MW;  07C2ECB0F0B5F57D CRC64;
     MAEFTMELND EQKEVRDWLH GFAADVIRPA AAEWDEREET PWPVIQEAAK VGIYSLDFYA
     QQYFDPTGLG IPMAMEELFW GDAGIALSIV GTGLAAVGVL ANGTEEQIGT WIPQMYGDAN
     DVKVAAFCSS EPDAGSDVAS MRTRAVYDEA KDEWVLNGTK TWATNGGIAG VHVVVAVVDA
     ELGSKGHASF IVPPNTPGLS QGQKFKKHGI RASHTAEVVL ENVRVPGSCL LGGKEKLDER
     LARARERSEM GVPPAEGWGR VKNAAMATFE ASRPAVGAMA VGTARAAYEV ALDYATTREQ
     FGRPIIDNQG VAFQLADMRT SIDAARLLVW RASWMAVNGK PFTAAEGSMS KLFASETAKK
     VTAQAIQILG GNGYTREYPV ERMHRDSAIY TIFEGTSEIQ RLVIARTLSG MPIR
//