ID   A0A2T7FUA0_9RHOB        Unreviewed;       757 AA.
AC   A0A2T7FUA0;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   RecName: Full=Acyl-CoA dehydrogenase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=DC363_12990 {ECO:0000313|EMBL:PVA05739.1};
OS   Thalassorhabdomicrobium marinisediminis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Thalassorhabdomicrobium.
OX   NCBI_TaxID=2170577 {ECO:0000313|EMBL:PVA05739.1, ECO:0000313|Proteomes:UP000244817};
RN   [1] {ECO:0000313|EMBL:PVA05739.1, ECO:0000313|Proteomes:UP000244817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BH-SD16 {ECO:0000313|EMBL:PVA05739.1,
RC   ECO:0000313|Proteomes:UP000244817};
RA   Ji X.;
RT   "Pelagivirga bohaiensis gen. nov., sp. nov., a bacterium isolated from the
RT   Bohai Sea.";
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   -!- 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:PVA05739.1}.
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DR   EMBL; QCYG01000008; PVA05739.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T7FUA0; -.
DR   OrthoDB; 9775090at2; -.
DR   Proteomes; UP000244817; 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; 2.
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; 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; 2.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000244817}.
FT   DOMAIN          6..99
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          219..339
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
FT   DOMAIN          399..487
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          493..586
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          600..744
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   757 AA;  80751 MW;  5E368C2090FACFAC CRC64;
     MDGAMTDEIQ MIRDAVARFL AGAGGLAPAR QAHDGAVNAA VWDGLAQDLQ LCGVTLPEEV
     GGLDMGLEAL VPLAREVGRV LSPAPFVSTV GVAGEVLRQL AQGTQADAQQ GRANGLLGQI
     AEGKLRATLA CFSSDRVTAT AEQDSYVLSG DVGPMQHGPG ADMLLVPACL EGQPVVFALR
     DWPEAPACDA FDPTRPVMAM RFTGFAVPQD TLLGSGATLQ AALDRASVAL AAEAAGAARG
     CFDLTAEYLS ERRQFGRTIA SFQAIKHRMA AQFVALNALD ALIDGAAAGN PVAGYEGRAA
     WALAREVQAA VASEAVQLHG GVGVTWEYAP HMFFKRARAQ LNWPKPPQQT FTAIGQALLD
     GDIPTLPQVE DTPFRSDVRT WMSQQLTGRF APLIDRGHAG DGDAEVELRK AWEAELAHGG
     WVGMGLPKED GGRGMSVADQ VAFHEEYARL GGPGRMGHIG EGLVAPTLVA FGTQDQKDRH
     LPGILEGRTF WAQGYSEPGA GSDLAAIRTK ARRCPETGDW LVTGQKIWTS LAHVSDWIFV
     LARAEEGSVG RKGLVFLLMP LHQDGIEIRP ITQMGGAAEF NEVFFDGARA SSADMIGGIG
     DGWKIAMALL GYERGISTLG QQMGFARELD QVVTVARSKP DAAHLTERLG RAWAGLRAMR
     HGAQAMLQAQ AEGRAGPEML GYKLEWSEWH RALGDLAMDV LGETASVWSD NPEVRRLQQL
     YLFSRADTIY GGTSEIQLNI IAEQGLNMPR EPRGAAT
//