ID V9XKM5_9NOCA Unreviewed; 349 AA.
AC V9XKM5;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:AHD22584.1};
GN ORFNames=Y013_19110 {ECO:0000313|EMBL:AHD22584.1};
OS Rhodococcus pyridinivorans SB3094.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=1435356 {ECO:0000313|EMBL:AHD22584.1, ECO:0000313|Proteomes:UP000018781};
RN [1] {ECO:0000313|EMBL:AHD22584.1, ECO:0000313|Proteomes:UP000018781}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB3094 {ECO:0000313|EMBL:AHD22584.1,
RC ECO:0000313|Proteomes:UP000018781};
RX PubMed=24874690;
RA Dueholm M.S., Albertsen M., D'Imperio S., Tale V.P., Lewis D.,
RA Nielsen P.H., Nielsen J.L.;
RT "Complete Genome of Rhodococcus pyridinivorans SB3094, a Methyl-Ethyl-
RT Ketone-Degrading Bacterium Used for Bioaugmentation.";
RL Genome Announc. 2:e00525-14(2014).
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; CP006996; AHD22584.1; -; Genomic_DNA.
DR RefSeq; WP_006550434.1; NC_023150.1.
DR AlphaFoldDB; V9XKM5; -.
DR GeneID; 29937804; -.
DR KEGG; rpy:Y013_19110; -.
DR PATRIC; fig|1435356.3.peg.3848; -.
DR eggNOG; COG1960; Bacteria.
DR HOGENOM; CLU_018204_5_2_11; -.
DR Proteomes; UP000018781; Chromosome.
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}.
FT DOMAIN 5..118
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 223..332
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 349 AA; 36932 MW; FFD515B1E75D63B3 CRC64;
MTFETEDRAA LRDSVRTLLA KHSDSAAVRR AITTGSGYDD ELWTMLVEQV GVAALAVPEE
YDGVGASWVE AHVVLEELGR TLTPSPFLGS AVLAAQTVLL SGDADAAARL LPGIAAGEVV
AVCWASATGW QRPGVSAEGN VLTGTAHYVL GGDIASTLLV LAADGDTVGL FEVDPETDGV
SRRRVPTMDP TRSLAEVSFS AVTGRRLSSS DDLVDRLRAS AAIALSAEQV GAAQAVLDLT
VDYAKNRKQF GRAIGSFQAL KHRMADMYAL VETARSMSYA AALSQDPQDA YAAKIYCSEA
FQQVASEAVQ LHGGIAITWE HDAQLFFKRA HGSAQLFGQP REYLSAISA
//
