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Database: UniProt
Entry: J2KCV0_9BURK
LinkDB: J2KCV0_9BURK
Original site: J2KCV0_9BURK 
ID   J2KCV0_9BURK            Unreviewed;       371 AA.
AC   J2KCV0;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:EJL78035.1};
GN   ORFNames=PMI12_01295 {ECO:0000313|EMBL:EJL78035.1};
OS   Variovorax sp. CF313.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Variovorax.
OX   NCBI_TaxID=1144315 {ECO:0000313|EMBL:EJL78035.1, ECO:0000313|Proteomes:UP000007277};
RN   [1] {ECO:0000313|EMBL:EJL78035.1, ECO:0000313|Proteomes:UP000007277}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CF313 {ECO:0000313|EMBL:EJL78035.1,
RC   ECO:0000313|Proteomes:UP000007277};
RX   PubMed=23045501; DOI=10.1128/JB.01243-12;
RA   Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA   Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT   "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT   sequences from diverse bacteria isolated from the rhizosphere and
RT   endosphere of Populus deltoides.";
RL   J. Bacteriol. 194:5991-5993(2012).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EJL78035.1}.
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DR   EMBL; AKIW01000020; EJL78035.1; -; Genomic_DNA.
DR   RefSeq; WP_007830269.1; NZ_AKIW01000020.1.
DR   AlphaFoldDB; J2KCV0; -.
DR   PATRIC; fig|1144315.3.peg.1288; -.
DR   Proteomes; UP000007277; 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; 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; 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:ARBA00022827}.
FT   DOMAIN          6..115
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          216..362
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   371 AA;  39965 MW;  10F23E7273B6D648 CRC64;
     MDFNFTDDQE QLRDAVRKWV DKGYDFERRR GIEAKGGFSR EAWDELAELG LGGLYISEDD
     GGLGMGPVAG MVVMEELGRG IVLEPFAQTL IAGAVLSGYA GADTKDSWLP RIAGGQAIVV
     LAYQERKARW RLDVCEATAA KSGDGYALTG AKSVVPVGDE ADAFLVPAKV GGKIALFLVE
     RSASGVEARG YGTQDGGRAA EVVFDKADAT LVTLDGLAAL EYAVDVGIAA TCAEAVGVMD
     KTMAVTVDYM NQRKQFGVAI STFQALRHRV ADMKMQLELA RSMSYYATLK LNAPADERRQ
     ALARAKYQLG VSMRFVAANS VQLHGGIGVT DEYIGSHYFR KLTQMEMTFG DTLHHLGEVS
     ARMQDTAGVF A
//
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