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Database: UniProt
Entry: C5AML1_BURGB
LinkDB: C5AML1_BURGB
Original site: C5AML1_BURGB 
ID   C5AML1_BURGB            Unreviewed;       379 AA.
AC   C5AML1;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 79.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:ACR31062.1};
GN   OrderedLocusNames=bglu_2g06260 {ECO:0000313|EMBL:ACR31062.1};
OS   Burkholderia glumae (strain BGR1).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia.
OX   NCBI_TaxID=626418 {ECO:0000313|EMBL:ACR31062.1, ECO:0000313|Proteomes:UP000002187};
RN   [1] {ECO:0000313|EMBL:ACR31062.1, ECO:0000313|Proteomes:UP000002187}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGR1 {ECO:0000313|EMBL:ACR31062.1,
RC   ECO:0000313|Proteomes:UP000002187};
RX   PubMed=19329631; DOI=10.1128/JB.00349-09;
RA   Lim J., Lee T.H., Nahm B.H., Choi Y.D., Kim M., Hwang I.;
RT   "Complete genome sequence of Burkholderia glumae BGR1.";
RL   J. Bacteriol. 191:3758-3759(2009).
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; CP001504; ACR31062.1; -; Genomic_DNA.
DR   RefSeq; WP_012733457.1; NC_012721.2.
DR   AlphaFoldDB; C5AML1; -.
DR   STRING; 626418.bglu_2g06260; -.
DR   GeneID; 58139051; -.
DR   KEGG; bgl:bglu_2g06260; -.
DR   PATRIC; fig|626418.3.peg.867; -.
DR   eggNOG; COG1960; Bacteria.
DR   HOGENOM; CLU_018204_0_2_4; -.
DR   Proteomes; UP000002187; Chromosome 2.
DR   GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IEA:InterPro.
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; IPR006089; Acyl-CoA_DH_CS.
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:SF12; COMPLEX I ASSEMBLY FACTOR ACAD9, 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   PIRSF; PIRSF016578; HsaA; 2.
DR   SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
DR   PROSITE; PS00073; ACYL_COA_DH_2; 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   Reference proteome {ECO:0000313|Proteomes:UP000002187}.
FT   DOMAIN          6..117
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          122..216
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          229..378
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   379 AA;  40827 MW;  19A657B87252CAE1 CRC64;
     MDALYTEDQR MIRDTVRDFS TEVLAPNAAQ WDQDGALPDG VVAQLGELGL LGMVVPAEWE
     GSYTDYTAYA LAVEEIAAGC ASCSTLMSVQ NSVCCGPILS YGTDAQRDRW LRGLASGRMI
     GSFCLTEPQA GSEANNLRTR AVLKDGRWVL DGSKQFISNA SRAAVAIVFA MTDPELGKRG
     LSAFIVPTDT PGFQVGKPEK KLGIRASDTC PITLEHCEIP EENLLGARGE GLKIALSNLE
     GGRIGIAAQA VGIARAAFDK ARRYAAERTQ FGKPIAEHQA IAEKLADMAT QLNAARLLVH
     HAARLRTAGL PCLSEASQAK LFASEMSEAV CSAAIQIHGG YGYLADYEVE RHYRDARITQ
     IYEGTSEVQR MVIARQLLA
//
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