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Database: UniProt
Entry: A0A158K811_9BURK
LinkDB: A0A158K811_9BURK
Original site: A0A158K811_9BURK 
ID   A0A158K811_9BURK        Unreviewed;       374 AA.
AC   A0A158K811;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:SAL77254.1};
GN   ORFNames=AWB68_05161 {ECO:0000313|EMBL:SAL77254.1};
OS   Caballeronia choica.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Caballeronia.
OX   NCBI_TaxID=326476 {ECO:0000313|EMBL:SAL77254.1, ECO:0000313|Proteomes:UP000054770};
RN   [1] {ECO:0000313|Proteomes:UP000054770}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Peeters C.;
RL   Submitted (JAN-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; FCON02000070; SAL77254.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A158K811; -.
DR   OrthoDB; 9769473at2; -.
DR   Proteomes; UP000054770; Unassembled WGS sequence.
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:SF44; BLR1022 PROTEIN; 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..118
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          126..211
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          225..367
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   374 AA;  39835 MW;  89D6768A9FDE1870 CRC64;
     MALLPNEEQR MLSVSAKAFL ADAAPVAHLR ALRDSSDAIG YSVSLWRDFA NQGYSGILVP
     ERFGGLGLSI VEAGLVAEEL GRNLTPSPFL STAVLGAVAL ERAGNEAQQK RLLPAIAEST
     TVLALATDEC ARHNPESVTL SAVRHGDGFA LNGEKIFVVD GHVAQTLIVS ARTSAHGMTL
     FLVDRDTAGV HIERAAMIDA HNAARVRLQD VKVDADAVLG AIDGGHGVLS QVLDHGRAIV
     AAQLVGAADA VFERTTTYLK ERRQFGRLIG EFQALQHRAA QWYVELELAR SMLTEALHAL
     AGRSADAGLM VARAKALACE AASLAVREGV QMHGGMGMTD ELDIGLFMKR VGVLQTLFGD
     TRFHLDRAAT LSGY
//
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