ID A0A2P8KMU5_9BURK Unreviewed; 405 AA.
AC A0A2P8KMU5;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:PSL84275.1};
GN ORFNames=C7T35_12395 {ECO:0000313|EMBL:PSL84275.1}, GXN78_36655
GN {ECO:0000313|EMBL:NDZ18275.1};
OS Variovorax sp. WS11.
OG Plasmid pVarWS11_2 {ECO:0000313|EMBL:NDZ18275.1}.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Variovorax.
OX NCBI_TaxID=1105204 {ECO:0000313|EMBL:PSL84275.1, ECO:0000313|Proteomes:UP000241151};
RN [1] {ECO:0000313|EMBL:PSL84275.1, ECO:0000313|Proteomes:UP000241151}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WS11 {ECO:0000313|EMBL:PSL84275.1,
RC ECO:0000313|Proteomes:UP000241151};
RA Crombie A.T., Mejia-Florez N.L., Murrell C.;
RT "Isoprene degraders from the Poplar phyllosphere.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:NDZ18275.1, ECO:0000313|Proteomes:UP000479786}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WS11 {ECO:0000313|EMBL:NDZ18275.1,
RC ECO:0000313|Proteomes:UP000479786};
RC PLASMID=pVarWS11_2 {ECO:0000313|EMBL:NDZ18275.1};
RA Dawson R.A., Larke-Mejia N.L., Crombie A.T., Ul-Haque M.F., Murrell J.C.;
RT "Isoprene oxidation by the Gram negative model bacterium Variovorax sp.
RT WS11.";
RL Submitted (FEB-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
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:PSL84275.1}.
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DR EMBL; JAAGOW010000005; NDZ18275.1; -; Genomic_DNA.
DR EMBL; PXZZ01000014; PSL84275.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P8KMU5; -.
DR OrthoDB; 9769473at2; -.
DR Proteomes; UP000241151; Unassembled WGS sequence.
DR Proteomes; UP000479786; 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 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};
KW Plasmid {ECO:0000313|EMBL:NDZ18275.1}.
FT DOMAIN 9..133
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 137..232
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 250..398
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 405 AA; 45342 MW; 56B730405CD21EC7 CRC64;
MFAEPSPKSA ELLQRLRAFF DQHIYPNEER YHREMDAFRR QGSPWQVVPL IEELKPKARA
AGLWNMFLPH PYEGHGGISN LDYAPLCEVM GRVSWSGEVF NCSAPDTGNM ETLERYATEP
QKQQWLKPLL AGEIRSAFLM TEPAVASSDA TNIQCSIRRD GEHYVINGRK WFSSGAGSPR
CKIFIVMGKT DPDAPRHAQQ SMVLVPRDTP GVTVARHLSV FGYDDAPHGH MEVVLENVRV
PVDSILLGEG RGFEIAQGRL GPGRIHHCMR SIGAAERALE LMCDRLQKRI AFGKPLAEQS
VWHERIAESR CMIDQARLLT LNAAWKMDTV GNKVARAEIA MIKVVAPNMS CKVVDWAIQA
HGGGGVSQDF WLAEAYAHQR TVRLVDGPDE VHRNAIAKLE LAKHR
//