ID   A0A132SEU3_9MYCO        Unreviewed;       732 AA.
AC   A0A132SEU3;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:KWX57634.1};
GN   ORFNames=ASJ79_10930 {ECO:0000313|EMBL:KWX57634.1};
OS   Mycobacterium sp. NAZ190054.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=1747766 {ECO:0000313|EMBL:KWX57634.1, ECO:0000313|Proteomes:UP000070146};
RN   [1] {ECO:0000313|EMBL:KWX57634.1, ECO:0000313|Proteomes:UP000070146}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NAZ190054 {ECO:0000313|EMBL:KWX57634.1,
RC   ECO:0000313|Proteomes:UP000070146};
RA   Zhang Y., Guo Z.;
RL   Submitted (NOV-2015) 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:KWX57634.1}.
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DR   EMBL; LMVQ01000554; KWX57634.1; -; Genomic_DNA.
DR   RefSeq; WP_067961775.1; NZ_LMVQ01000554.1.
DR   AlphaFoldDB; A0A132SEU3; -.
DR   OrthoDB; 2431337at2; -.
DR   Proteomes; UP000070146; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000070146}.
FT   DOMAIN          7..98
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          221..344
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
FT   DOMAIN          382..470
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          474..564
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          580..726
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   732 AA;  78356 MW;  B0970A676FCF39C9 CRC64;
     MPIAILEEHN DLANSVRAFV ERVAPSEVLH DALENPVPNP PPYWKSAAEQ GLHGVHLAES
     VGGQGFGILE LAIVIAEFGY GAVPGPFVPS AIASALIAAH DPGAAVLRDL ASGEVIAAYA
     IDSGLTATRH GDGLVIRGEV RAVPCAAQAS LLVLPVAIES GEEWVVLDAA TLEIEPVRSV
     DPLRPVAHVR ANAVEVGPEE VGNRVLGNLS RGHARALMST LLSAEAIGVA RWATDTASAY
     AKIREQFGRP IGQLQAIKHK CANMIAETER ATAAVWDAAR AIDESRENPD AACEFAAAVA
     ATLAPVAAQH CAQDCIQVHG GIGFTWEHDT NVYYRRALVL AASFGRAADY PQQVVDLATT
     TGMRALNIDL DPETEKLRDE IRAEVAALKE IPREQRNAAI AEGGWVQPHL PVPWGRAATP
     IEQIIIAQEF ATGRVRRPQM GIAAWIIPSI VAFGTDDQKQ RFLPPTFRGE MIWCQLFSEP
     GAGSDLASLT TKATKVDGGW RITGQKIWTT GAQFSEWGAL LARTDPSAPK HAGITYFLLD
     MKSEGVEVKP LRELTGNAMF NTVFIDDVFV PDDMVLGEVN RGWEVSRNTL TNERVSIGSS
     EPPFLPSLDK FVEFIGEGQF DQIAQNHAGI LIAEGHAAKI LNMRSTLLTL AGGDPMPAAA
     ISKLLSMKTG QGYAEFAVSS FGTDAVVGDP EQLTGRWAEY LLASRATTIY GGTSEVQLNI
     IAERLLGLPR DP
//