ID A0A157S8R8_9BORD Unreviewed; 396 AA.
AC A0A157S8R8;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:SAI66643.1};
DE EC=1.3.8.- {ECO:0000313|EMBL:SAI66643.1};
DE EC=1.3.8.1 {ECO:0000313|EMBL:SAI66643.1};
GN ORFNames=SAMEA3906486_01073 {ECO:0000313|EMBL:SAI66643.1};
OS Bordetella ansorpii.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=288768 {ECO:0000313|EMBL:SAI66643.1, ECO:0000313|Proteomes:UP000076848};
RN [1] {ECO:0000313|EMBL:SAI66643.1, ECO:0000313|Proteomes:UP000076848}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H050680373 {ECO:0000313|EMBL:SAI66643.1,
RC ECO:0000313|Proteomes:UP000076848};
RG Pathogen Informatics;
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
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; FKIF01000002; SAI66643.1; -; Genomic_DNA.
DR RefSeq; WP_066124503.1; NZ_FKIF01000002.1.
DR AlphaFoldDB; A0A157S8R8; -.
DR STRING; 288768.SAMEA3906486_01073; -.
DR OrthoDB; 9770681at2; -.
DR Proteomes; UP000076848; Unassembled WGS sequence.
DR GO; GO:0004085; F:butyryl-CoA dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; 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; 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; PTHR43292; ACYL-COA DEHYDROGENASE; 1.
DR PANTHER; PTHR43292:SF3; ACYL-COA DEHYDROGENASE FADE29; 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};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:SAI66643.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000076848}.
FT DOMAIN 6..120
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 125..219
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 231..393
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 396 AA; 43865 MW; E679F2D7B76BBD5A CRC64;
MDLNFSPEEL AFRDDVRDFL RQRLTPELAA KVRAGKHLSK AEMEGWHAEL HARGWLASHW
PEQYGGTGWS AAQKYLFDHE CALAGAPRIV PFGVSMLGPV LIKYGNEAQK RHWLPRILDG
SDWWCQGYSE PGAGSDLASL QTRAVRQGNE YIVNGQKTWT TLGQHANMIF CLVRTASDGR
PQEGISFLLI DMTTPGIELR PIRTLDGDHE VNEVFFSDVR VPVENLVGEE NRGWTCAKYL
LTYERTNIAG VGLSYAALAE LKEAASKAVR NGRPLTEDPL YAARLARVEI DLDNMRTTNL
RVIAASEHGA PGAESSMLKI RGTQIRQEIS SLMRRAAGPH GRAHDPRMLE AGDALGFGPE
GTEGSAARYF NLRKLSIFGG SNEIQRNIIS KMILGL
//
