ID A0A1H4H383_9BURK Unreviewed; 386 AA.
AC A0A1H4H383;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Acyl-CoA dehydrogenase/acyl-CoA dehydrogenase {ECO:0000313|EMBL:SEB15568.1};
GN ORFNames=SAMN05444680_11030 {ECO:0000313|EMBL:SEB15568.1};
OS Variovorax sp. YR216.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Variovorax.
OX NCBI_TaxID=1882828 {ECO:0000313|EMBL:SEB15568.1, ECO:0000313|Proteomes:UP000199122};
RN [1] {ECO:0000313|Proteomes:UP000199122}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YR216 {ECO:0000313|Proteomes:UP000199122};
RA Varghese N., Submissions S.;
RL Submitted (OCT-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; FNRO01000010; SEB15568.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H4H383; -.
DR STRING; 1882828.SAMN05444680_11030; -.
DR OrthoDB; 9770681at2; -.
DR Proteomes; UP000199122; Unassembled WGS sequence.
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:SF43; ACYL-COA DEHYDROGENASE; 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; PS00072; ACYL_COA_DH_1; 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}.
FT DOMAIN 6..117
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 122..213
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 225..374
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 386 AA; 42865 MW; 0317AC9D350C5C59 CRC64;
MDFALNDEQK MMIDTLRRFI AEELRPLEDR LENDGHIDRD TATTIHEKAK ALGLYALNMP
AELGGGGLSN LDRILCEEQF GHTTDYLIRR AFGNVYEPLL HCRGEQVARW LEPAVAGKRT
CAIAITEPGA GSDAAGIRTH AKKTGTGWVL NGGKHFISDG EWSDFFLVSA KTGEKEISMF
MVDKGLAGFS VGKDQKMMGI RGTPHLELFF DNVQLEDAAL LGERGQGFKL AMGALNVVRL
AQVGARAVGK ATHVLELMTA YANDRQQFGQ RIGDFQMVQQ MLADSVIEIN AARWMVYHAA
WMLDQGFDAR EQIAMVKVHA AETLGRVVDR AVQVFGGMGF CKELPIERYY RDARIYRIFD
GTSEIHRGVI AKSVIKKGAA LFDVHR
//
