ID A0A1H7DSK3_9BURK Unreviewed; 423 AA.
AC A0A1H7DSK3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:SEK04394.1};
GN ORFNames=SAMN05518853_106402 {ECO:0000313|EMBL:SEK04394.1};
OS Variovorax sp. OK202.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Variovorax.
OX NCBI_TaxID=1884311 {ECO:0000313|EMBL:SEK04394.1, ECO:0000313|Proteomes:UP000199192};
RN [1] {ECO:0000313|EMBL:SEK04394.1, ECO:0000313|Proteomes:UP000199192}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OK202 {ECO:0000313|EMBL:SEK04394.1,
RC ECO:0000313|Proteomes:UP000199192};
RA de Groot N.N.;
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; FNZJ01000006; SEK04394.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H7DSK3; -.
DR Proteomes; UP000199192; 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}.
FT DOMAIN 8..137
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 142..243
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 255..404
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 423 AA; 46384 MW; 7ADC755CAEB3B6A3 CRC64;
MDFEYSAKTK DLQKRVQAFM DDHIYPAEAE YHAELAANTV AGKRWSALKT VEKLKEKAKA
QGLWNLFLPV DSASASGYAG AGLTNQEYAP LAEIMGAVPW ASEAFNCSAP DTGNMETIAR
YGSEEIKARW LKPLLEGQIR SAFAMTEPEV ASSDATNIST RIERQGDEYV INGHKWWISG
AADPRCAVFI TMGKSDPEAP RHSQQSMVIV PADAKGIRIV RPLNVMGYDD APHGHVEMYF
ENVRVPVDNI LLGEGRGFEI AQGRLGPGRI HHCMRLIGLA ERALELMCKR ASSRVAFGKT
VASQTVTQER IAEARCKIDM ARLLTLKAAW LMDVAGNKVA KNEIAMIKVV APSMACQVID
WAMQVHGGGG MCDDFPLAAA YAGARTLRFA DGPDEVHRNA IAKWELGKYA PNKADAEMPV
TRF
//