ID   A0A3F2V4N2_9GAMM        Unreviewed;       417 AA.
AC   A0A3F2V4N2;
DT   16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT   16-JAN-2019, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:RLP54416.1};
GN   ORFNames=D6160_10300 {ECO:0000313|EMBL:RLP54416.1};
OS   Ketobacter sp.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Ketobacteraceae; Ketobacter.
OX   NCBI_TaxID=2083498 {ECO:0000313|EMBL:RLP54416.1, ECO:0000313|Proteomes:UP000280615};
RN   [1] {ECO:0000313|EMBL:RLP54416.1, ECO:0000313|Proteomes:UP000280615}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BinD {ECO:0000313|EMBL:RLP54416.1};
RA   Xu J.;
RT   "Metagenomic reconstruction reveals the metabolic diversity of the novel
RT   genus Ketobacter and the trajectory of genomic evolution within the
RT   Alcanivoraceae family.";
RL   Submitted (SEP-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974,
CC         ECO:0000256|RuleBase:RU362125};
CC   -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00009347, ECO:0000256|RuleBase:RU362125}.
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:RLP54416.1}.
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DR   EMBL; RAHY01000007; RLP54416.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3F2V4N2; -.
DR   Proteomes; UP000280615; Unassembled WGS sequence.
DR   GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IEA:InterPro.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
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:SF12; COMPLEX I ASSEMBLY FACTOR ACAD9, 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.
DR   PROSITE; PS00072; ACYL_COA_DH_1; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU362125};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|RuleBase:RU362125};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU362125};
KW   Reference proteome {ECO:0000313|Proteomes:UP000280615}.
FT   DOMAIN          5..44
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          150..250
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          270..414
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   417 AA;  45999 MW;  34F523AE515C76F6 CRC64;
     MIEWSESQRM LRTAVRQFVE KEIAPNLETL EHGDTPPYDV LRKFLRSFGI DAMARQRFEA
     DIAKAKAKEA GEASEADESE KDPAMVEMMR GEETAMRLIP AIELCRFCPG MVTAMGVSMG
     LTAGTIMSRG TIAQKERWAA DLLTMDKIGA WAITEPNSGS DAFGSMKATC KRDGKGGYIL
     NGNKTFITNG PYADTLVFIC KLDEPGVEPP QRKVLSFILD SGMEGLVQSK PFRKMGIHSS
     PTGELFLQDV KAGPERLLGE SEEISYRSGV KDTFSAERSG VAAMALGITE RCLELSVRYA
     KERVQFGKPI GEFQLIQAKL AKMEVARINL ENLVFRYIET SAKGRSMTLA EASAMKLYAA
     QTAVEVAMEA VQIHGGNGYM AEYQVEQLAR DAKILQIYGG TDEIQITHIA REMLSRD
//