ID F2LQD7_BURGS Unreviewed; 416 AA.
AC F2LQD7;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE SubName: Full=Acyl-CoA dehydrogenase domain protein {ECO:0000313|EMBL:AEA64640.1};
GN OrderedLocusNames=bgla_2g22060 {ECO:0000313|EMBL:AEA64640.1};
OS Burkholderia gladioli (strain BSR3).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia.
OX NCBI_TaxID=999541 {ECO:0000313|EMBL:AEA64640.1, ECO:0000313|Proteomes:UP000008316};
RN [1] {ECO:0000313|EMBL:AEA64640.1, ECO:0000313|Proteomes:UP000008316}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BSR3 {ECO:0000313|EMBL:AEA64640.1,
RC ECO:0000313|Proteomes:UP000008316};
RX PubMed=21478339; DOI=10.1128/JB.00420-11;
RA Seo Y.S., Lim J., Choi B.S., Kim H., Goo E., Lee B., Lim J.S., Choi I.Y.,
RA Moon J.S., Kim J., Hwang I.;
RT "Complete genome sequence of Burkholderia gladioli BSR3.";
RL J. Bacteriol. 193:3149-3149(2011).
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; CP002600; AEA64640.1; -; Genomic_DNA.
DR RefSeq; WP_013690966.1; NC_015376.1.
DR AlphaFoldDB; F2LQD7; -.
DR STRING; 999541.bgla_2g22060; -.
DR KEGG; bgd:bgla_2g22060; -.
DR eggNOG; COG1960; Bacteria.
DR HOGENOM; CLU_018204_1_2_4; -.
DR Proteomes; UP000008316; Chromosome 2.
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; PTHR48083:SF13; ACYL-COA DEHYDROGENASE FAMILY MEMBER 11; 1.
DR PANTHER; PTHR48083; MEDIUM-CHAIN SPECIFIC ACYL-COA DEHYDROGENASE, MITOCHONDRIAL-RELATED; 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 8..132
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 136..237
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 249..397
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 416 AA; 44786 MW; 528A2DFD271826E1 CRC64;
MDFTPTARSQ DFADRLSRFM RDEIAPAEAR YAAELTGGAD WRQWRQPPVM EALKQKARAA
GLWNLFLPEV EHGGAGLSNA EYAPLAEIMG HSFIAPEVFN CNAPDTGNME VLARYGTPGQ
QARWLAPLLA GEIRSAFCMT EPEVASSDAT NMRATATPDG DEFVLNGRKW WSTGIGHPHA
RVAIFMGLTD AEAEPHRRHT MVICPLDAKG VRIERMLPAF HHYDEPSGHG EVVFDQVRVP
ASNVILGPGR GFEIAQGRLG PGRIHHCMRA LGAAERALGL LCERAAARTA FGKPLAALGG
NADIVANLRM AIDQARLLTL KAAWTIDTQG VKAALSLISQ IKVVVPAVAQ QAADAAIQIH
GGAGVSDDVP LTHLYAYARV LRLADGPDEV HRGVVAKLEF KRQAGEQASR RAGAAA
//
