ID   G7CLB9_MYCT3            Unreviewed;       417 AA.
AC   G7CLB9;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:EHI11195.1};
GN   ORFNames=KEK_19054 {ECO:0000313|EMBL:EHI11195.1};
OS   Mycolicibacterium thermoresistibile (strain ATCC 19527 / DSM 44167 / CIP
OS   105390 / JCM 6362 / NCTC 10409 / 316) (Mycobacterium thermoresistibile).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=1078020 {ECO:0000313|EMBL:EHI11195.1, ECO:0000313|Proteomes:UP000004915};
RN   [1] {ECO:0000313|EMBL:EHI11195.1, ECO:0000313|Proteomes:UP000004915}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19527 / DSM 44167 / CIP 105390 / JCM 6362 / NCTC 10409 /
RC   316 {ECO:0000313|Proteomes:UP000004915};
RG   Tuberculosis Structural Genomics Consortium;
RA   Ioerger T.R.;
RL   Submitted (NOV-2011) 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|ARBA:ARBA00009347, 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:EHI11195.1}.
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DR   EMBL; AGVE01000048; EHI11195.1; -; Genomic_DNA.
DR   AlphaFoldDB; G7CLB9; -.
DR   PATRIC; fig|1078020.3.peg.3755; -.
DR   eggNOG; COG1960; Bacteria.
DR   Proteomes; UP000004915; Unassembled WGS sequence.
DR   GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IEA:InterPro.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
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; 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; PTHR43884; ACYL-COA DEHYDROGENASE; 1.
DR   PANTHER; PTHR43884:SF12; COMPLEX I ASSEMBLY FACTOR ACAD9, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR   Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR   Pfam; PF02771; Acyl-CoA_dh_N; 1.
DR   PIRSF; PIRSF016578; HsaA; 2.
DR   SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
DR   PROSITE; PS00073; ACYL_COA_DH_2; 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|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU362125};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004915}.
FT   DOMAIN          32..143
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          147..247
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          262..406
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   417 AA;  44633 MW;  14ED49114D444785 CRC64;
     MYDIRRPGGV AIAPPGRTHK EKPMSTAEVS DEDFRQILRQ TREFVRTAVV PRELEILNED
     RVPDDLREQA KQMGLFGYAI PQQWGGLGLD LAQDVELAME LGYTSLALRS MFGTNNGIAG
     QVLVGFGTEE QKARWLEPIA SGEVVASFAL TEPGAGSNPA GLRSRAVRDG SGADADWIIN
     GQKRFITNAP VADLFVVFAR SRPADERGAG IAVFLVPADA PGVEVGAKDA KMGQEGAWTA
     DVTFTDVRVP ASALVGGEED IGYRAAMTSL ARGRVHIAAL AVGTAQRALD ESVAYAASAT
     QGGTPIGQFQ LVQAMLADQQ TGVMAGRALV RDAARKWVSG EDRRVAPSAA KLFCTEMAGQ
     VADLAVQIHG GTGYMREVPV ERIYRDVRLL RLYEGTSEIQ RLIIGGGLVK AAQRQTN
//