ID A0A1X0U9G0_9NOCA Unreviewed; 604 AA.
AC A0A1X0U9G0;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=Acyl-CoA dehydrogenase {ECO:0008006|Google:ProtNLM};
GN ORFNames=BJI47_23060 {ECO:0000313|EMBL:ORI13511.1};
OS Rhodococcus sp. 1168.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=2018041 {ECO:0000313|EMBL:ORI13511.1, ECO:0000313|Proteomes:UP000192546};
RN [1] {ECO:0000313|EMBL:ORI13511.1, ECO:0000313|Proteomes:UP000192546}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1168 {ECO:0000313|EMBL:ORI13511.1,
RC ECO:0000313|Proteomes:UP000192546};
RA Nahar A.;
RT "Metabolic and lipid synthesis pathways analysis of sub-Antarctic
RT Rhodococcus luteus.";
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}.
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:ORI13511.1}.
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DR EMBL; MKKY01000091; ORI13511.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X0U9G0; -.
DR OrthoDB; 3666321at2; -.
DR Proteomes; UP000192546; 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 CDD; cd00567; ACAD; 1.
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; PTHR43884; ACYL-COA DEHYDROGENASE; 1.
DR PANTHER; PTHR43884:SF19; ACYL-COA DEHYDROGENASE FADE4-RELATED; 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|RuleBase:RU362125};
KW Reference proteome {ECO:0000313|Proteomes:UP000192546}.
FT DOMAIN 36..127
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 133..242
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 255..405
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 604 AA; 65152 MW; BF05D3D7F83F28CE CRC64;
MTFGAVDSGA DLGSDPARSI DELERRLEVL LESVDMQSVE DLDDADEFPT ELIAALDRLG
VQRCYVPTQF GGLLDDYSNA GRIVRALSRV DVTLAVAHGK TFLGAVSAWV AGDERQRERL
AQLICEGKQI SWGLTERARG SDLLSGEVRA DTAEMQVDSS RTGDEPDTAG FRLYGEKWLI
NNATRGHAVC VLARTRDGGT ARGYSLFLVE KSELDTASFD TLPKEPTHGI RGADISGISF
DGAFVPARTL VGPEGHGLEI VLKALQLTRT MCCYLSLGAS DHALAMTARF ARARVLYGRS
LGDLPAARTV LVESFGGHLL AEALTVVASR SLHALPGEQS ALAAASKYLV PSTVEKSLLD
LRRLMGARSL VPGLGSDGTL YKVERDHRIV SLFDGNTVVN LNTIVSQFSV LLWKNTARTT
QDEIDFRICT TIAEPLPALD LARLSLVPRR GLGLLANLES SVTALGCLLD RQHDGQAYAL
RCAEVLVRTV ETLSQQTRLL DRDPVEVPTA AFVAAEQLSA CIAGAAAIQI YLNNPPTGPL
WSDALWLQLA LHTALDRIGV RSSVPIDSID AGYSVLLDQL DHRSHPTIFD ATTSASVKQE
RVNT
//