ID A0A1G5A5Q8_9BURK Unreviewed; 776 AA.
AC A0A1G5A5Q8;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=Acyl-CoA dehydrogenase {ECO:0008006|Google:ProtNLM};
GN ORFNames=SAMN03159363_4948 {ECO:0000313|EMBL:SCX73220.1};
OS Variovorax sp. EL159.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Variovorax.
OX NCBI_TaxID=1566270 {ECO:0000313|EMBL:SCX73220.1, ECO:0000313|Proteomes:UP000199507};
RN [1] {ECO:0000313|EMBL:SCX73220.1, ECO:0000313|Proteomes:UP000199507}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EL159 {ECO:0000313|EMBL:SCX73220.1,
RC ECO:0000313|Proteomes:UP000199507};
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; FMUJ01000006; SCX73220.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G5A5Q8; -.
DR STRING; 1566270.SAMN03159363_4948; -.
DR OrthoDB; 9770681at2; -.
DR Proteomes; UP000199507; 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; 2.
DR Gene3D; 2.40.110.10; Butyryl-CoA Dehydrogenase, subunit A, domain 2; 2.
DR Gene3D; 1.20.140.10; Butyryl-CoA Dehydrogenase, subunit A, domain 3; 2.
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; PTHR43292; ACYL-COA DEHYDROGENASE; 1.
DR PANTHER; PTHR43292:SF3; ACYL-COA DEHYDROGENASE FADE29; 1.
DR Pfam; PF00441; Acyl-CoA_dh_1; 2.
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; 2.
DR SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 2.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 228..359
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT DOMAIN 401..508
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 512..610
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 623..772
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 776 AA; 83592 MW; 0DD0B7CD405FF53F CRC64;
MDTESLAAVR EAALDYFVRS RAIGRRRTRT EQPDGDEAQS WKDIVALGWP GMLAPESAGG
LALGLDGAAE ILRAAGEHVA PEPLLAVAGL SALLLARLDT PGAHALLREL VEGRSLPALA
WQESAGDLSA VPLACGCEVH GAQAGGVLLQ GEKLMVLPGA AASGWLVSAR GDDDAVLLWV
PRGTEGVSET LVPLVDGSQA ANLRFEQVVL PPGAVLAEGV AAQDALRYAL AAGQILQAAE
LLGAGQAMLA QTLVYLRTRS QFGKPIGSFQ ALQHRCVDMF IHLEVAQATL NEVLALAAQG
LSCNRLEAEA SRANARCTAA ALQASRAAVQ LHGAIGYTQE CDLSLFYKRA LCLSAWLGNV
TAHQRRHAAL TEEAGSTSGT TEAWTGEFPR QADWAAMPEP DFRRMVRGFL QQRYPQELRY
LSHRARWSEM REWYLTLSGQ GWIAPAWPQA HGGMGLPADK LIAWIEELEQ YGVARAPDQG
IVMIGPLLIQ HGTPEQQQRF LPRILSGEHV WCQGYSEPNA GSDLAGLRTE ALPARDAQGD
HFVVNGQKIW TTLAQDANHI FMLVRTDKDA RKQEGISFLL CDLRTPGITV RPIHTLAGEP
EFCEVFFDNV RVPAENLVGK LHGGWTIAKA LLGFERIFLG SPKQSQYALG QLARLAQARR
LFADPVFAQR FVALRLDVAD LTAAYTSFAD IVRAGKPLPA SVSLLKIWAS ETFHRIGALL
VEAGEEQGAV AGDQVLDGQT FNVLSPLIGS TAAMIYGGTN EIQRNILARQ VLDLPA
//