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Database: UniProt
Entry: A0A0F5VWV9_9ACTN
LinkDB: A0A0F5VWV9_9ACTN
Original site: A0A0F5VWV9_9ACTN 
ID   A0A0F5VWV9_9ACTN        Unreviewed;       379 AA.
AC   A0A0F5VWV9;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:KKD06297.1};
GN   ORFNames=TN53_19220 {ECO:0000313|EMBL:KKD06297.1};
OS   Streptomyces sp. WM6386.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1415558 {ECO:0000313|EMBL:KKD06297.1, ECO:0000313|Proteomes:UP000033641};
RN   [1] {ECO:0000313|EMBL:KKD06297.1, ECO:0000313|Proteomes:UP000033641}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WM6386 {ECO:0000313|EMBL:KKD06297.1,
RC   ECO:0000313|Proteomes:UP000033641};
RA   Ju K.-S., Doroghazi J.R., Metcalf W.;
RL   Submitted (JAN-2015) 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:KKD06297.1}.
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DR   EMBL; JXTE01000029; KKD06297.1; -; Genomic_DNA.
DR   RefSeq; WP_046259779.1; NZ_JXTE01000029.1.
DR   AlphaFoldDB; A0A0F5VWV9; -.
DR   PATRIC; fig|1415558.3.peg.3617; -.
DR   OrthoDB; 8677713at2; -.
DR   Proteomes; UP000033641; 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   CDD; cd00567; ACAD; 1.
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; 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:SF20; ACYL-COA DEHYDROGENASE FADE28; 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:UP000033641}.
FT   DOMAIN          6..118
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          124..194
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          231..366
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   379 AA;  39671 MW;  6F01ADFAF03BA260 CRC64;
     MTLTFTEEHE ELRATVRRFL VDKAPSEAVR RTMESEEGHD PLLWRQMADQ LGLHGVALPP
     DCGGFGGGPV ELGIVLEELG RVLLPSPYFA TVALAGQALA ASGDDAAKAR WLPSIADGSL
     TGTLALAEES GSWNVQDVVA RADRADTGWR VSGTKMFVID GHSADLLLVV ARADTGPALF
     AVDSGAGGLT PPRPGTLDPT RRLARIDLDG ATALRVGPEG DATGYLRTVT DLAAVALAAE
     QIGGAQACLD AAVEYAKVRV QFGRPIGSFQ AVKHKCADML LKIESARSAA HHAMAVAAEG
     ADELPVAAAV AAAYCADTFT HVAKENIQIH GGIGYTWEHD AHLHLKRAKS SEQLFGSPAV
     HRGRLADLVG ISATTATEG
//
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