ID A0R527_MYCS2 Unreviewed; 714 AA.
AC A0R527;
DT 09-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 104.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:ABK76151.1};
GN OrderedLocusNames=MSMEG_6041 {ECO:0000313|EMBL:ABK76151.1};
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196 {ECO:0000313|EMBL:ABK76151.1, ECO:0000313|Proteomes:UP000000757};
RN [1] {ECO:0000313|EMBL:ABK76151.1, ECO:0000313|Proteomes:UP000000757}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155 {ECO:0000313|Proteomes:UP000000757};
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000480; ABK76151.1; -; Genomic_DNA.
DR RefSeq; WP_011730994.1; NZ_SIJM01000017.1.
DR RefSeq; YP_890265.1; NC_008596.1.
DR AlphaFoldDB; A0R527; -.
DR STRING; 246196.MSMEG_6041; -.
DR PaxDb; 246196-MSMEI_5880; -.
DR GeneID; 66737325; -.
DR KEGG; msm:MSMEG_6041; -.
DR PATRIC; fig|246196.19.peg.5877; -.
DR eggNOG; COG1960; Bacteria.
DR OrthoDB; 3964153at2; -.
DR Proteomes; UP000000757; Chromosome.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
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; 2.
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; 2.
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; PTHR43292; ACYL-COA DEHYDROGENASE; 1.
DR PANTHER; PTHR43292:SF4; ACYL-COA DEHYDROGENASE FADE34; 1.
DR Pfam; PF00441; Acyl-CoA_dh_1; 2.
DR Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR Pfam; PF02771; Acyl-CoA_dh_N; 2.
DR SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 2.
DR SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 2.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Reference proteome {ECO:0000313|Proteomes:UP000000757}.
FT DOMAIN 10..96
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 205..331
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT DOMAIN 372..455
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 459..558
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 570..710
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 714 AA; 75177 MW; 9A036FC8B2D87A16 CRC64;
MSLLSAGAGT SEEFAARDMV RSWAAASGAV AAVRESETDP GAWRAAYQGF AELGIFGVAV
PDELGGAGST VADLAAMIDE AAAALVPGPV VTTALATLLV TDTGLLEALM SGERTAGVAL
SADVTVVDGR ASGTVEFVLG ADAAGVLLLP AGDDVLLLDA GADGVSVEPL TATDFSIPLA
RVELDNAPAE VLPVSRQRFS DLAATLLAAE AAGLARWTLN TATEYAKVRE QFGKPIGSFQ
AIKHMCAEML LRSEQIAVAA ADAAKAVAES DGSDSATQLS IAAAVAVATG IDAAKANAKD
CIQVLGGIGI TWEHDAHLYL RRAYGIAHFL GGSRRWVRRV AALTRQGARR DIDIDLESVA
DLRPEISAAV AEVAALPEEK RQVALAESGL LAPHWPKPYG RNASPAEQLL IDQELAAAEV
ERPDLVIGWW AVPTILEHGS PEQIEQFVPA TLRGDLFWCQ LFSEPGAGSD LAALRTKAVR
AEGPNGEPGW KLTGQKVWTS AAQNAHWGVC LARTDPDAPK HKGITYFLVD MKTPGIVIRP
LREITGDELF NEVFFDDVFV PDTMVVGTVN DGWRLARTTL ANERVAMAGG TALGNPMEEV
LRAVEAQPEF DPADQDRLGA LIVTAQVGSL LDQRIAQLAV SGQDTGAQAS ARKLIGVRYR
QALAEFHMEL TEGGGAVRNR EVHTFLNTRC LTIAGGTEQI LLTLAGERLL GLPR
//
