ID   A0A318EDM0_9GAMM        Unreviewed;       378 AA.
AC   A0A318EDM0;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   24-JAN-2024, entry version 12.
DE   SubName: Full=Alkylation response protein AidB-like acyl-CoA dehydrogenase {ECO:0000313|EMBL:PXV68330.1};
GN   ORFNames=C8D93_10425 {ECO:0000313|EMBL:PXV68330.1};
OS   Sinimarinibacterium flocculans.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Nevskiales; Nevskiaceae;
OC   Sinimarinibacterium.
OX   NCBI_TaxID=985250 {ECO:0000313|EMBL:PXV68330.1, ECO:0000313|Proteomes:UP000248330};
RN   [1] {ECO:0000313|EMBL:PXV68330.1, ECO:0000313|Proteomes:UP000248330}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 104150 {ECO:0000313|EMBL:PXV68330.1,
RC   ECO:0000313|Proteomes:UP000248330};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT   most valuable type-strain genomes for metagenomic binning, comparative
RT   biology and taxonomic classification.";
RL   Submitted (APR-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:PXV68330.1}.
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DR   EMBL; QICN01000004; PXV68330.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A318EDM0; -.
DR   OrthoDB; 9769473at2; -.
DR   Proteomes; UP000248330; Unassembled WGS sequence.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
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; PTHR43292; ACYL-COA DEHYDROGENASE; 1.
DR   PANTHER; PTHR43292:SF3; ACYL-COA DEHYDROGENASE FADE29; 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, 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:UP000248330}.
FT   DOMAIN          7..123
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          127..218
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          233..370
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   378 AA;  41265 MW;  F5A666BFB2185FE4 CRC64;
     MDFQWDAEQR AFRDTVRSFL AENLPADWES LAHGPGSESQ SAFSKTFCGA LAKAGLLVPH
     WPKRWGGRDA DAWTSFILAE EMWMAGEPRG GQYMNVNWIG PTLMRFGTEA QQDRYIPPIA
     RGETIWCQGF SEPEAGSDLA SLRTRAERCD GGYRLNGQKI WTSYAGHADT CFLLARTGIG
     KTGMSVFLVP MDTAGITVRQ IPSVIGEGDI HEVFFDDVFV PADALLGAEG QAWEIARNAL
     SLERVGIPRF ALAARMLRRA VAALKKADRY GHGAVEQSAR ALAACEAARL YSYQIVDQRR
     HGTPTGPEAS AARYATVMAE RLVGEFVVEH CPDALAGGDP LLLAHHQRAI VAGIASGAAE
     IQLNLIATEL LQLPREPR
//