ID A0A1X9NJY6_9GAMM Unreviewed; 593 AA.
AC A0A1X9NJY6;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:ARN75177.1};
GN ORFNames=BST96_14260 {ECO:0000313|EMBL:ARN75177.1};
OS Oceanicoccus sagamiensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Spongiibacteraceae; Oceanicoccus.
OX NCBI_TaxID=716816 {ECO:0000313|EMBL:ARN75177.1, ECO:0000313|Proteomes:UP000193450};
RN [1] {ECO:0000313|EMBL:ARN75177.1, ECO:0000313|Proteomes:UP000193450}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 107125 {ECO:0000313|EMBL:ARN75177.1,
RC ECO:0000313|Proteomes:UP000193450};
RA Kumagai Y.;
RT "Trade-off between light-utilization and light-protection in marine
RT flavobacteria.";
RL Submitted (NOV-2016) 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}.
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DR EMBL; CP019343; ARN75177.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X9NJY6; -.
DR STRING; 716816.BST96_14260; -.
DR KEGG; osg:BST96_14260; -.
DR OrthoDB; 9807883at2; -.
DR Proteomes; UP000193450; Chromosome.
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; 1.
DR InterPro; IPR025878; Acyl-CoA_dh-like_C_dom.
DR InterPro; IPR020953; Acyl-CoA_DH_N_bac.
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; PTHR42803; ACYL-COA DEHYDROGENASE; 1.
DR PANTHER; PTHR42803:SF1; BROAD-SPECIFICITY LINEAR ACYL-COA DEHYDROGENASE FADE5; 1.
DR Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR Pfam; PF12806; Acyl-CoA_dh_C; 1.
DR Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR Pfam; PF02771; Acyl-CoA_dh_N; 1.
DR Pfam; PF12418; AcylCoA_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|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU362125};
KW Reference proteome {ECO:0000313|Proteomes:UP000193450}.
FT DOMAIN 3..34
FT /note="Acyl-CoA dehydrogenase N-terminal bacteria"
FT /evidence="ECO:0000259|Pfam:PF12418"
FT DOMAIN 41..158
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 163..272
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 282..453
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT DOMAIN 466..583
FT /note="Acetyl-CoA dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12806"
SQ SEQUENCE 593 AA; 64213 MW; B2030C6DE4E45E80 CRC64;
MADYKAPLRD IRFVLDELLD ADQHYASLSG TEEFNQELRD AILEEGAKFS EQTLAPLRQS
GDQEGCTWSE EGVTTPSGFA DAYQQFVEGG WPGLSMPEQF GGQGLPASVD LVLSELLGQA
NHAWSMYPGL SAGCRETLIA HGTEQQQQDY LLKMVSGEWT GTMCLTEPQG GSDLSFLRTK
AEDNGDGSYA ITGTKIFISS GEHDMSENII HVVLARLPGA PEGTKGISLF IVPKFNVNAD
GSLGERNPVS CGSLEHKMGI HGNATCVMNF DGAKGYLIGK ENEGLKCMFT FMNTARVGTA
LQGLNHAEVA LQGAMAYALD REAGRSLTGP KAADRPADKL IVHADVRRML LTIRAFSEGN
RAFIHYLSQQ VDKEHRGSEE QQKEGSAILA FLTPIAKGFM TEVGIEAASH GIQVYGGHGY
ISEWGMEQNM RDARISTLYE GTTGIQSLDL IGRKIMADGG ANFGNFIAMI SKDIATMDAE
FAEPLQAMVK EWAELAGFIG AQAGKSMDEI GAASVDFLMY SGYVVLAWLW GRMGTLANAK
GTDDIFYKGK VATARFYFDK ILPRTESHKA TIEKGADTLM SLDDSDFEAL AAL
//
