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
//