ID R7WNI5_9NOCA Unreviewed; 380 AA.
AC R7WNI5;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:EOM76863.1};
GN ORFNames=Rrhod_1776 {ECO:0000313|EMBL:EOM76863.1};
OS Rhodococcus rhodnii LMG 5362.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=1273125 {ECO:0000313|EMBL:EOM76863.1, ECO:0000313|Proteomes:UP000013525};
RN [1] {ECO:0000313|EMBL:EOM76863.1, ECO:0000313|Proteomes:UP000013525}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 5362 {ECO:0000313|EMBL:EOM76863.1,
RC ECO:0000313|Proteomes:UP000013525};
RX PubMed=23788540;
RA Pachebat J.A., van Keulen G., Whitten M.M., Girdwood S., Del Sol R.,
RA Dyson P.J., Facey P.D.;
RT "Draft Genome Sequence of Rhodococcus rhodnii Strain LMG5362, a Symbiont of
RT Rhodnius prolixus (Hemiptera, Reduviidae, Triatominae), the Principle
RT Vector of Trypanosoma cruzi.";
RL Genome Announc. 1:e00329-13(2013).
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:EOM76863.1}.
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DR EMBL; APMY01000059; EOM76863.1; -; Genomic_DNA.
DR RefSeq; WP_010837838.1; NZ_APMY01000059.1.
DR AlphaFoldDB; R7WNI5; -.
DR PATRIC; fig|1273125.3.peg.1712; -.
DR eggNOG; COG1960; Bacteria.
DR OrthoDB; 9770681at2; -.
DR Proteomes; UP000013525; Unassembled WGS sequence.
DR GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IEA:InterPro.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; 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; IPR006089; Acyl-CoA_DH_CS.
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; 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:SF4; ACYL-COA DEHYDROGENASE FADE34; 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.
DR PROSITE; PS00072; ACYL_COA_DH_1; 1.
PE 3: Inferred from homology;
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Reference proteome {ECO:0000313|Proteomes:UP000013525}.
FT DOMAIN 13..126
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 130..225
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
SQ SEQUENCE 380 AA; 40882 MW; B5D2538244F3BFC1 CRC64;
MTRTVPAALP ESEALTTLRH EVRDFLTAEI ARGTFTPGVD TWLTQWDPEF TRALAERGWI
GMTIPTEYGG HGRTFLERYV VTEELLAVGA PVAAQWVADR QAAPSLLKFG TEAQKQRFLP
GIARGEISWA IGMSEPDSGS DLASVRTKAT RVDGGWRVDG TKLWTSGAHH ADAFFALART
APLDPAHRHD GLSQFVVLLD SPGVTIRPIL TMSGDHHFNE VHLDGVFVPD DLVLGTIGDG
WHQVTSELGY ERSGPERVLS TFALLAATAE EMRLGTVPTD SRLGRETARV HALRRMSFGV
AGALARGENA DLAASVVKIL GTGTEGDIAE LADDVRPGAD DSDEFGALVR AGVMQRPGFT
LRGGTSEILR GVLARGLGMR
//
