ID A0A0P0SM54_9PSEU Unreviewed; 372 AA.
AC A0A0P0SM54;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Acyl-CoA dehydrogenase {ECO:0008006|Google:ProtNLM};
GN ORFNames=AD017_28540 {ECO:0000313|EMBL:ALL85698.1};
OS Pseudonocardia sp. EC080619-01.
OG Plasmid pBCI1-2 {ECO:0000313|EMBL:ALL85698.1,
OG ECO:0000313|Proteomes:UP000066228}.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Pseudonocardia.
OX NCBI_TaxID=1096856 {ECO:0000313|EMBL:ALL85698.1, ECO:0000313|Proteomes:UP000066228};
RN [1] {ECO:0000313|EMBL:ALL85698.1, ECO:0000313|Proteomes:UP000066228}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EC080619-01 {ECO:0000313|EMBL:ALL85698.1,
RC ECO:0000313|Proteomes:UP000066228};
RC PLASMID=Plasmid pBCI1-2 {ECO:0000313|Proteomes:UP000066228};
RX PubMed=26535611; DOI=10.1021/jacs.5b09794;
RA Van Arnam E.B., Sit C.S.;
RT "A Rebeccamycin Analog Provides Plasmid-Encoded Niche Defense.";
RL J. Am. Chem. Soc. 137:14272-14274(2015).
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}.
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DR EMBL; CP012185; ALL85698.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P0SM54; -.
DR KEGG; pecq:AD017_28540; -.
DR PATRIC; fig|1096856.3.peg.6268; -.
DR Proteomes; UP000066228; Plasmid pBCI1-2.
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; 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; 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; 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};
KW Plasmid {ECO:0000313|EMBL:ALL85698.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000066228}.
FT DOMAIN 4..117
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 233..365
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 372 AA; 38952 MW; 6D99C39F90CD8309 CRC64;
MRETEEQADL RAVVRRFLAE RADLTRVRTL MAGDGTVDQT VWKEITRGLG LVGLAVPELW
GGAGRGLAEE TVVLEEAGRA LYGGPYLAAS VLAPALLLEV GDEAACAAHL PAILAGDTLA
VPVVTSGTGE WSAGGGDLTA RADGTGGWTL GGVASHVVDA SAADLLLVVA GTTDGPALFA
VPTMGPGVTV TPQPGLDQTR GLARVELREA AGTRIGGRRV DTAVRELRDR AWVAVAAEQL
GVASRCLELS VDYATTRQQF GGPIGRFQAV KHLCADMYLT VEAARSVVLY AERAIDELLP
ERTVGAAMAR VWCSDAACRV AADTVQVHGG IGFTWESDVH LYFKRAEASA LLFGDPDDAA
EIVAAARLEE TR
//
