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Database: UniProt
Entry: A0A0D7CQR5_9ACTN
LinkDB: A0A0D7CQR5_9ACTN
Original site: A0A0D7CQR5_9ACTN 
ID   A0A0D7CQR5_9ACTN        Unreviewed;       729 AA.
AC   A0A0D7CQR5;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:KIZ18589.1};
GN   ORFNames=SNA_08305 {ECO:0000313|EMBL:KIZ18589.1};
OS   Streptomyces natalensis ATCC 27448.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1240678 {ECO:0000313|EMBL:KIZ18589.1, ECO:0000313|Proteomes:UP000032458};
RN   [1] {ECO:0000313|EMBL:KIZ18589.1, ECO:0000313|Proteomes:UP000032458}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27448 {ECO:0000313|EMBL:KIZ18589.1,
RC   ECO:0000313|Proteomes:UP000032458};
RA   Mendes M.V., Beites T., Pires S., Santos C.L., Moradas-Ferreira P.;
RT   "Draft genome sequence of Streptomyces natalensis ATCC 27448, producer of
RT   the antifungal pimaricin.";
RL   Submitted (SEP-2014) 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:KIZ18589.1}.
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DR   EMBL; JRKI01000009; KIZ18589.1; -; Genomic_DNA.
DR   RefSeq; WP_044363967.1; NZ_JRKI01000009.1.
DR   AlphaFoldDB; A0A0D7CQR5; -.
DR   PATRIC; fig|1240678.4.peg.1740; -.
DR   Proteomes; UP000032458; 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: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          6..105
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          218..350
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
FT   DOMAIN          383..463
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          467..564
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          577..717
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   729 AA;  76720 MW;  774B0008FD8E0F93 CRC64;
     MGIGITQEHR DLAEATRGWA ARAVPPEEIR TLLDAPPQRH GRPAHWDRLA AQGLLGPHLP
     EADGGGGGAL LDLAVVLEEM GRAALPGPYL PTTLAAELLR RAGHRDLVRA LATGELLAAV
     ALGTGSLTAV QEADGYILDG TAPPVLAGGD ADVIVLAATA PTGPVWLAAD AATLTVRVQE
     SADPTRPVAE VSADGVLVPA ARLLAVDGAL VRDLAGVLFA AESCGTAGRA LETAAEHAAV
     REQFGRPIGQ FQAVKHLCAD MLVRCEQARA LVWDAARALD EPPAVRGLVA ALATATALDA
     AHTCAKDCIQ ILGGIGFTWE HDAHLHLRRA TVARQLLGSG DSHRLRAARH ATGGARRALR
     LDLPAEAAAH RTQARTVIDA ARGLDPAAAR RALAPTGYAA PHLPEPYGLG AGPVRQLAVQ
     QELREAGVEI SDLGIATWVI PSLIAHGTKE QQDRYLPPSL RGDLLWCQLF SEPEAGSDLA
     SLRTRAERVD GPGGGWRING QKVWTSAAQW ADHGILLART NPDAPRHKGL TFFLVDMKTP
     GIDIRPLKEI TGDALFNEVY FDDVLLPADA VVGEIDNGWK VARTTLDNER VHMADQLTFD
     TGLEALLERS ADLDGSVRAR VGALAAEAHA LGCIGLRTTL QQVSGLEPGA GAAVRKLVQT
     PHQQKVAELA LELLGPAGAV REGAGERALH GFLMSRCLTI AGGTTQVQLN VVAERLLGLP
     RDPEPRPLI
//
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