ID   A0A1I1NDI6_9RHOB        Unreviewed;       569 AA.
AC   A0A1I1NDI6;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=Acyl-CoA dehydrogenase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=SAMN04488094_111141 {ECO:0000313|EMBL:SFC92833.1};
OS   Tropicimonas isoalkanivorans.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Tropicimonas.
OX   NCBI_TaxID=441112 {ECO:0000313|EMBL:SFC92833.1, ECO:0000313|Proteomes:UP000198728};
RN   [1] {ECO:0000313|EMBL:SFC92833.1, ECO:0000313|Proteomes:UP000198728}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19548 {ECO:0000313|EMBL:SFC92833.1,
RC   ECO:0000313|Proteomes:UP000198728};
RA   de Groot N.N.;
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         ECO:0000256|RuleBase:RU362125};
CC   -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00009347, ECO:0000256|RuleBase:RU362125}.
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DR   EMBL; FOLG01000011; SFC92833.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I1NDI6; -.
DR   STRING; 441112.SAMN04488094_111141; -.
DR   OrthoDB; 9807883at2; -.
DR   Proteomes; UP000198728; 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; 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, 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:UP000198728}.
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..270
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          280..437
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
FT   DOMAIN          453..561
FT                   /note="Acetyl-CoA dehydrogenase-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12806"
SQ   SEQUENCE   569 AA;  59939 MW;  B2A4228AE6706314 CRC64;
     MSYRAPLSDF GFLLSHVVGF DRVQSTELFS EATEDMTTAI LVEAGRLCED VLAPVDRAGD
     TVPARLDGGQ VHSSPGFAEA YRAIAKGGWI CVAAPPAHGG MGLPLTLQTA INEMMSAACL
     SLQLNPMLTQ GQIEALEAHA SEEIKALYLP KLISGEWTGT MNLTESGAGS DVGALVTRAE
     PNEDGTYAII GQKIYITWGD AEFVDNVCHL VLARLPDSPP GTKGISLFLV PRHLPDATGV
     PCAVNSLRVV SLEHKLGLHG SPTCVMEYDR ATGWLIGDEN GGMAAMFTMM NNARLGVGCQ
     GIGIAEAATQ KAVAFALERK QGRVGGTGTI IEHPDVRRMV ATMKAETFAA RAIALANAVA
     IDMARATGEA EWAARAALLT PISKAHGTDI GHEVAQIGIQ VHGGMGYIEE TGAAQLARDV
     RVTQIYEGTN GIQAMDLTGR KMADGGRAAL ALLDEVTAQA ESARVSLPAM SGRVADAARA
     VRDLTEWLVQ QELRDRFAGC TAYLRALARV LGAHFHLAAA IAEGGTGPRT RLAAFFVARL
     LPEHGALIAQ VKAGADGLFD VTVEDLETT
//