ID A0A164TB57_9NOCA Unreviewed; 599 AA.
AC A0A164TB57;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:KZF13191.1};
GN ORFNames=A2J03_15210 {ECO:0000313|EMBL:KZF13191.1};
OS Rhodococcus sp. EPR-157.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=1813677 {ECO:0000313|EMBL:KZF13191.1, ECO:0000313|Proteomes:UP000077673};
RN [1] {ECO:0000313|EMBL:KZF13191.1, ECO:0000313|Proteomes:UP000077673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EPR-157 {ECO:0000313|EMBL:KZF13191.1,
RC ECO:0000313|Proteomes:UP000077673};
RA Ploux O.;
RL Submitted (MAR-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|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:KZF13191.1}.
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DR EMBL; LVCV01000018; KZF13191.1; -; Genomic_DNA.
DR RefSeq; WP_068368304.1; NZ_LVCV01000018.1.
DR AlphaFoldDB; A0A164TB57; -.
DR OrthoDB; 9807883at2; -.
DR Proteomes; UP000077673; 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; 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:SF3; ACYL-COA DEHYDROGENASE-RELATED; 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; 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|RuleBase:RU362125};
KW Reference proteome {ECO:0000313|Proteomes:UP000077673}.
FT DOMAIN 7..34
FT /note="Acyl-CoA dehydrogenase N-terminal bacteria"
FT /evidence="ECO:0000259|Pfam:PF12418"
FT DOMAIN 163..266
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 292..458
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT DOMAIN 477..594
FT /note="Acetyl-CoA dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12806"
SQ SEQUENCE 599 AA; 65488 MW; F31441E91C9F4235 CRC64;
MTTPPLSRRD IEFMLYEWLD VESLTTRPRF AEHSRDTFDA VLDLSADMAA KFFAPHNKLA
DAQEPTVGED GKVILTPEAK KALEVFAQAG LFAGAFDESL GGMQLPISVM RASVAWFQAS
NASTTGYPFL TVANANLLVA YATEQQIDAY VRPMLEGRFF GTMCLSEPQA GSSLADITTK
AVRQTDGSYR LTGTKMWISG GDHELSENIV HLVLAKIPGG GAGVKGISLF IVPKYVLDAD
GNPGERNDVA LVGLNHKMGN RGTTNALLNF GDGSYTPAGS SGAIGYLIGE PNRGLNYMFH
MMNEARIGVG FLATALGYAG YRQSVEYALT RTQGRSQTNR DPASKPISIV EHADVKRMLL
AQKAYVEGAL ALGLFCSNLV DEQDTLEDTD QRAEKTLLLD VLTPIAKSWP SQWCLRANDL
AIQVHGGYGY TRDYDVEQFY RDNRLNQIHE GTHGIQGLDL LGRKMTMQDG AGLDLLLSTI
GSTIDRAHNT GGEAAGLAIE LKAALDRTFE VTTNLRSEPD KACALANSSI YLEAVGHVVV
AWMWLEQFLV AGDLTGNFYD GKRQATRYFF RYELPSTTAQ FDLLDSLDRT SVEMSAQWF
//
