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Database: UniProt
Entry: A0A1A0QRY7_9MYCO
LinkDB: A0A1A0QRY7_9MYCO
Original site: A0A1A0QRY7_9MYCO 
ID   A0A1A0QRY7_9MYCO        Unreviewed;       741 AA.
AC   A0A1A0QRY7; A0A1X0CYJ7;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:ORA65138.1};
GN   ORFNames=BST23_15140 {ECO:0000313|EMBL:ORA65138.1};
OS   Mycolicibacterium elephantis.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=81858 {ECO:0000313|EMBL:ORA65138.1, ECO:0000313|Proteomes:UP000192772};
RN   [1] {ECO:0000313|EMBL:ORA65138.1, ECO:0000313|Proteomes:UP000192772}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FI-09383 {ECO:0000313|EMBL:ORA65138.1,
RC   ECO:0000313|Proteomes:UP000192772};
RA   Tortoli E., Trovato A., Cirillo D.M.;
RT   "The new phylogeny of genus Mycobacterium.";
RL   Submitted (FEB-2017) 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   -!- 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:ORA65138.1}.
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DR   EMBL; MVHP01000016; ORA65138.1; -; Genomic_DNA.
DR   RefSeq; WP_064891087.1; NZ_MVHP01000016.1.
DR   AlphaFoldDB; A0A1A0QRY7; -.
DR   STRING; 81858.BST23_15140; -.
DR   OrthoDB; 3964153at2; -.
DR   Proteomes; UP000192772; Unassembled WGS sequence.
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}.
FT   DOMAIN          6..97
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          226..351
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
FT   DOMAIN          391..479
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          483..576
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          589..735
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   741 AA;  79319 MW;  AEC813FD326E9EBA CRC64;
     MPIAITTEHN DLADSVRSLV ERVAPSEVLH EALETPIPNP PPYWKTAAEQ GLQGVHLAES
     VGGQGFGILE LAIVLAEFGY GAVPGPFVPS AIASALISAH DPDAKLLNDL ASGNAIATYA
     IDSGLTATRH GEDDSPSLVI RGEVRAVPAA AQASVLVLPV AGLEEGTSGS KWVVLDADQL
     EIEPVKSVDP LRPVAHVRAN AVEVGDDRVL HNLNPTLARA LITTLLSAEC IGVARWATDT
     ASEYAKIREQ FGRPIGQFQA VKHKCANMIA ETERATAAVW DAARAIDEAS DGGENSAQES
     AFEFAAAVAA TLAPVAAQNC AQDCIQVHGG IGFTWEHDTN VYYRRALVLA ASFGRLADYP
     QQVVDVATST GLRQLNIDLD PETEKLRDEI RAEVAALKAI PREERNTAIA EGGWVQPHLP
     KPWGRSAGPV EQIIIAQEFE TGRVKRPAMG IAAWIIPSIV AFGTDEQKQR FLPPTFRGEM
     IWCQLFSEPG AGSDLASLST KATKVDGGWR ITGQKIWTTG AQHSHWGALL ARTDPSAPKH
     NGITYFLLDM KSKGVEVKPL RELTGNAMFN TVFLDDVFVP DDMVLGEVNR GWEVSRNTLT
     AERVSIGSSE PPFLANLNGF VEFIKDGQFD QIEQNHAGHL IAEGYAAKVL NMRSTLLTLA
     GGDPMPAAAI SKLLSMKTGQ GYAEFAVASF GTDGAIAEPG EIQGTWLEYL LGSRATTIYG
     GTTEVQLNII AERLLGLPRD P
//
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