ID   A0A1H0V545_9BURK        Unreviewed;       598 AA.
AC   A0A1H0V545;
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=SAMN05216303_106313 {ECO:0000313|EMBL:SDP73226.1};
OS   Rhodoferax sp. OV413.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Rhodoferax.
OX   NCBI_TaxID=1855285 {ECO:0000313|EMBL:SDP73226.1, ECO:0000313|Proteomes:UP000199151};
RN   [1] {ECO:0000313|Proteomes:UP000199151}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OV413 {ECO:0000313|Proteomes:UP000199151};
RA   Varghese N., Submissions S.;
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; FNJA01000006; SDP73226.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H0V545; -.
DR   STRING; 1855285.SAMN05216303_106313; -.
DR   OrthoDB; 9764895at2; -.
DR   Proteomes; UP000199151; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199151}.
FT   DOMAIN          3..23
FT                   /note="Acyl-CoA dehydrogenase N-terminal bacteria"
FT                   /evidence="ECO:0000259|Pfam:PF12418"
FT   DOMAIN          82..160
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          165..273
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          284..452
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
FT   DOMAIN          473..593
FT                   /note="Acetyl-CoA dehydrogenase-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12806"
SQ   SEQUENCE   598 AA;  64574 MW;  CB9A392B038A7BA3 CRC64;
     MPSYTPPLRD MQFVMHEVLK VTDDLKLCPQ HADTDADTIN AVLEEGGKFA SEVAFPLNIS
     GDEEGCTLDK TTHEVTAPKG FKEAYAQYVQ GGWAALSCDP AYGGQGLPFV VNQCFYEMLN
     SANQAWTMYP GLSHGAYEAL QAHGTDAQKA LYLPKLTSGE WTGTMCLTEP HCGTDLGLLR
     TKAEPLADGS YAITGNKIFI SAGEHDMAEN IVHLVLARLP DAPVGSKGIS LFAVPKFHVS
     ADGTLGKRNG IYCGGLEHKM GIHGNATAQM VLEGAIGTLV GQPNKGLAAM FVMMNAARLG
     VGNQSLGLTE VAYQNALAYA KDRIQMRSLS GTKAKDKPAD PIIVHPDVRK MLLTAKAYAE
     GGRALGIFCG VLLDKEHSHP DEKVRADSGE MLALLTPIVK AFLTDNGHIS TNACMQVFGG
     HGFIKEWGME QYVRDNRINM IYEGTNTIQS LDLLGRKVLG NNGATLKKFG RLVAALVEEE
     GVNEKMAEFI TPIAILGDQV TKLTTELGFK GFQNADEVGA AAVDYLRVAG HLVFGYFWAR
     MAQVALREIA AGNTDQFYLA KVQTARFYFA KLFPETATLM RTMRTGSKAL MDTDAALA
//