ID   A0A372M855_9ACTN        Unreviewed;       649 AA.
AC   A0A372M855;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:RFU87029.1};
GN   ORFNames=DY218_09075 {ECO:0000313|EMBL:RFU87029.1};
OS   Streptomyces triticagri.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=2293568 {ECO:0000313|EMBL:RFU87029.1, ECO:0000313|Proteomes:UP000263094};
RN   [1] {ECO:0000313|EMBL:RFU87029.1, ECO:0000313|Proteomes:UP000263094}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NEAU-YY421 {ECO:0000313|EMBL:RFU87029.1,
RC   ECO:0000313|Proteomes:UP000263094};
RA   Han C.;
RT   "Isolation, diversity and antifungal activity of Actinobacteria from
RT   wheat.";
RL   Submitted (AUG-2018) 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:RFU87029.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; QUAK01000047; RFU87029.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A372M855; -.
DR   OrthoDB; 8876745at2; -.
DR   Proteomes; UP000263094; 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}.
FT   DOMAIN          65..170
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          175..271
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          283..441
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          627..649
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        13..28
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   649 AA;  71013 MW;  86B0D1F2399DBB37 CRC64;
     MSAAPSDSPG TPKVSEREAR QVAEAAREQD WRKPSFAKEL FLGRFRLDLI HPHPLPAADD
     VRRGEEFLAQ LRDFCETKVD SSRIEREARI PDEVIAGLKE LGALGMKIDQ KYGGLGLTQV
     YYNKALALVG SANPAIGALL SAHQSIGVPQ PLKIFGTQEQ KDTFLPRLAR TDISAFLLTE
     PDVGSDPARL ATTAVPDGDD YVLDGVKLWT TNGVVADLLV VMARVPKSDG HKGGISAFVV
     EADSAGITVE QRNAFMGLRG LENGVTRFHQ VRVPAANRIG PEGAGLKIAL TTLNTGRLSL
     PAMCVGAGKW SLKIAREWSA VREQWGRPVA KHEAVGSKIS FIAATTFALE AVLDLSSQMA
     DEDRNDIRIE AALAKLYGSE MAWLMADELV QIRGGRGFET AESLAARGER AVPVEQLLRD
     LRINRIFEGS TEIMHLLIAR EAVDAHLKVA GDLIDPEKSL GDKAKAGARA GGFYARWLPG
     LVAGPGQLPR SYAEFNPSGH RDLSGHLRFV ERTSRRLARS TFYAMSRWQG RMETKQAFLG
     RIVDIGAELF AMSAACVRAE LMRSEGEFGR EAYQLADVFC RQSRIRAEEL FERLWKNTDS
     VDHRIVDGVL GGAYTWLEQG IVDPSGEGPW IADASPGPSE HENQHRPIR
//