ID   A0A255HJS7_9BURK        Unreviewed;       596 AA.
AC   A0A255HJS7;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:OYO26504.1};
GN   ORFNames=CD932_25085 {ECO:0000313|EMBL:OYO26504.1};
OS   Janthinobacterium sp. PC23-8.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Janthinobacterium.
OX   NCBI_TaxID=2012679 {ECO:0000313|EMBL:OYO26504.1, ECO:0000313|Proteomes:UP000216749};
RN   [1] {ECO:0000313|EMBL:OYO26504.1, ECO:0000313|Proteomes:UP000216749}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PC23-8 {ECO:0000313|EMBL:OYO26504.1,
RC   ECO:0000313|Proteomes:UP000216749};
RA   Kim H.J., Triplett B.A.;
RL   Submitted (JUN-2017) 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}.
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:OYO26504.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; NJGY01000004; OYO26504.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A255HJS7; -.
DR   OrthoDB; 9770681at2; -.
DR   Proteomes; UP000216749; 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; IPR025878; Acyl-CoA_dh-like_C_dom.
DR   InterPro; IPR020953; Acyl-CoA_DH_N_bac.
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; PTHR42803; ACYL-COA DEHYDROGENASE; 1.
DR   PANTHER; PTHR42803:SF1; BROAD-SPECIFICITY LINEAR ACYL-COA DEHYDROGENASE FADE5; 1.
DR   Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR   Pfam; PF12806; Acyl-CoA_dh_C; 1.
DR   Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR   Pfam; PF02771; Acyl-CoA_dh_N; 1.
DR   Pfam; PF12418; AcylCoA_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   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          2..33
FT                   /note="Acyl-CoA dehydrogenase N-terminal bacteria"
FT                   /evidence="ECO:0000259|Pfam:PF12418"
FT   DOMAIN          78..156
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          161..269
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          283..448
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
FT   DOMAIN          465..591
FT                   /note="Acetyl-CoA dehydrogenase-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12806"
SQ   SEQUENCE   596 AA;  63268 MW;  B65DEDC9699FBAB7 CRC64;
     MSYQAPLKDM LFVMNELAGL ADIHTLPGCE DATPDTAEAV LEENAKFCGA VVAPLNWPSD
     KEPSFWHDGQ VTTSKGFKEA FKAYGEAGWQ GVQHPTEFGG QGLPKLLATP CIEMLNAASI
     SFALVALLSD GAIEALLTAG SDEQKAVYLE KLVSGQWTGT MNLTEPQAGS DLAAVRTRAV
     PQGDGTYKVF GTKIFITYGE HDLAENIVHL VLARTPDAPA GVKGISLFIV PKFLVNADGS
     LGERNDAHCV SIEHKLGIKA SPTAVLQFGD HGGAIGTLVG EENRGLEYMF IMMNAARFGV
     GLQGIGLAER AYQQAVAFAK DRVQSRDLAG SAAPVSIIHH PDVRRMLMSM RSQTEAARAL
     AYVGAAISDV AHHHPDAQVR AESLATYEYL VPIIKGWSTE MSQDVARDGV QVHGGMGFIE
     ETGAAQHYRD AKILTIYEGT TAIQANDLVG RKTVRDGGAV AKAIIAQVRA TEAQLGELTG
     ADFQAMQRHL AEGSAALEAV VEYMVANIKT DIKAVFAGSV PYLKLAGIVL GGWQMARAAV
     AAQQKLGEGS GDAAFYKAKI STARFFADHI LSQAPGLRAT IVDGSAGVMA LSEEQF
//