ID E1T3L9_BURSG Unreviewed; 375 AA.
AC E1T3L9;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 24-JAN-2024, entry version 57.
DE SubName: Full=Acyl-CoA dehydrogenase domain-containing protein {ECO:0000313|EMBL:ADN58253.1};
GN OrderedLocusNames=BC1003_2300 {ECO:0000313|EMBL:ADN58253.1};
OS Burkholderia sp. (strain CCGE1003).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia.
OX NCBI_TaxID=640512 {ECO:0000313|EMBL:ADN58253.1};
RN [1] {ECO:0000313|EMBL:ADN58253.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CCGE1003 {ECO:0000313|EMBL:ADN58253.1};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Daligault H., Davenport K., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Jeffries C., Kyrpides N., Ivanova N., Ovchinnikova G.,
RA Martinez-Romero E., Rogel M.A., Auchtung J., Tiedje J.M., Woyke T.;
RT "Complete sequence of chromosome1 of Burkholderia sp. CCGE1003.";
RL Submitted (SEP-2010) 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; CP002217; ADN58253.1; -; Genomic_DNA.
DR AlphaFoldDB; E1T3L9; -.
DR STRING; 640512.BC1003_2300; -.
DR KEGG; bgf:BC1003_2300; -.
DR eggNOG; COG1960; Bacteria.
DR HOGENOM; CLU_018204_5_2_4; -.
DR OMA; DYRTIDN; -.
DR OrthoDB; 9770681at2; -.
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; 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; PTHR43884; ACYL-COA DEHYDROGENASE; 1.
DR PANTHER; PTHR43884:SF20; ACYL-COA DEHYDROGENASE FADE28; 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}.
FT DOMAIN 6..102
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 122..208
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 226..356
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 375 AA; 40485 MW; 968AC5AC891769B6 CRC64;
MDFTFNDEQQ QFADALRRYL DKSYGFEARQ AIVRSDAGVS EAHWAAFTEL GLTALPVPEA
QGGLNGGPVD MLVVMQELGR ALVVEPYWAT AVGIEALRLA GTGHGEDATL LQRAAQGEIK
LAVAFHEPHA RYDLFAVATA ASGTGEQQTL SGKKSVVLHG AQAQFWIVPA RANGEIALFV
VAREAAGVKL TEYRTIDGQR AATLVFDNTP ARRLGGLHSG AAALEHIADY ATLLLCAEAI
GALDALNTAT VEYTRTRQQF GQPIARFQVL QHRMVEMLIH TEQARSITYL AAMRYSSEDA
DERRRAISAA KVRVGQAARF VGQQAVQLHG GMGVTNEVAA AHLFKRLAII ETTLGDVDHH
LARFAALPGF VSTEV
//