ID A0A193GF17_9BORD Unreviewed; 390 AA.
AC A0A193GF17;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=Acyl-CoA dehydrogenase {ECO:0008006|Google:ProtNLM};
GN ORFNames=BAU07_12965 {ECO:0000313|EMBL:ANN77884.1};
OS Bordetella flabilis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=463014 {ECO:0000313|EMBL:ANN77884.1, ECO:0000313|Proteomes:UP000091926};
RN [1] {ECO:0000313|EMBL:ANN77884.1, ECO:0000313|Proteomes:UP000091926}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AU10664 {ECO:0000313|EMBL:ANN77884.1,
RC ECO:0000313|Proteomes:UP000091926};
RA LiPuma J.J., Spilker T.;
RT "Complete genome sequences of Bordetella bronchialis and Bordetella
RT flabilis.";
RL Submitted (JUN-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; CP016172; ANN77884.1; -; Genomic_DNA.
DR RefSeq; WP_066658282.1; NZ_CP016172.1.
DR AlphaFoldDB; A0A193GF17; -.
DR STRING; 463014.BAU07_12965; -.
DR KEGG; bfz:BAU07_12965; -.
DR OrthoDB; 9770681at2; -.
DR Proteomes; UP000091926; 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 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}.
FT DOMAIN 8..119
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 123..217
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 229..381
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 390 AA; 42772 MW; BE5ADBDB38979729 CRC64;
MTLRNESDAE AAFRLEVRTW LREHVPPSLR HATFRPSPEQ AMQWYRTLSR RGWIAPHWPR
EYGGMGATPM EQLILMEEMA AAGTPDIPTQ GLNHIGPLLI ARGTPAQRER HLPAILAGET
IWCQGYSEPG AGSDLARLST RGEVRDGHLV INGHKIWTTW GHHADWMFAL VRTSTEGKPR
DGITFVLIPM STFGIRRRPI RTIAGDDEFA EVFLDDVAVP LDNVVGDVDR GWDVATAVLS
EERLRIGSPA QALRARERLR MMLRATPAEQ LSASVREEAV LAEVEVQALC AAYLEAAEAG
PGDTRGGGVE SAYLKLLATD TMHLLLDLVR RAAGPAAALR EPVRHGDDLL DATEMFLQAR
RLGIYGGSSE VQRGIIATRV LGLPAAGNKG
//
