ID   A0A495X1T7_9PSEU        Unreviewed;       566 AA.
AC   A0A495X1T7;
DT   05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   SubName: Full=Alkylation response protein AidB-like acyl-CoA dehydrogenase {ECO:0000313|EMBL:RKT67519.1};
GN   ORFNames=DFJ66_0694 {ECO:0000313|EMBL:RKT67519.1};
OS   Saccharothrix variisporea.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Saccharothrix.
OX   NCBI_TaxID=543527 {ECO:0000313|EMBL:RKT67519.1, ECO:0000313|Proteomes:UP000272729};
RN   [1] {ECO:0000313|EMBL:RKT67519.1, ECO:0000313|Proteomes:UP000272729}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 43911 {ECO:0000313|EMBL:RKT67519.1,
RC   ECO:0000313|Proteomes:UP000272729};
RA   Klenk H.-P.;
RT   "Sequencing the genomes of 1000 actinobacteria strains.";
RL   Submitted (OCT-2018) 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:RKT67519.1}.
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DR   EMBL; RBXR01000001; RKT67519.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A495X1T7; -.
DR   OrthoDB; 6637748at2; -.
DR   Proteomes; UP000272729; 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   CDD; cd00567; ACAD; 1.
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; 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:SF43; ACYL-COA DEHYDROGENASE; 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   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:UP000272729}.
FT   DOMAIN          47..126
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          157..246
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          279..407
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   566 AA;  60654 MW;  190DD3D486136F3B CRC64;
     MTSSVASPPT LRAFFDDLFL GRVRWDLLRP FPTQDPADRA AGDQAVAAAT ALVRAHVDPE
     LLDRTGVLPA GLTDALQDAG FYKLLMGPEL GGLALSPYNA MRVVEAVASW SPAVAWSLAI
     GNGFGSGSYL PIVEDGPLRS LIERHVRAGI VSGSADTEAN GAANHRRHTT AVPHGDEYVV
     NGEKVFIGNG PLARLLDVAC TVEVDGVRQI RYFFVETDSP GFEVVTTQEF LGLKGASIGV
     LRFTDVRVPA ENMLPASADE ARYAPEIARL ATLARTLIIA SPSLAIAKLC LGWQRNFVTR
     RVMDDRPLAS YEEIQRRVAE TAADVFLVES VVAWGLLGQD RADTGPDLTA AKNLTSLACW
     RAVDRTVGLL GGEGIETARS KARRGAPALP VERFVRDARG LRVAGGVDFL LDYWSAEGGL
     EAWYSGAPGS FESTVDDLAL PPRCREHFRF LVDEAARLGD VCARLTGSYG REELMARQRT
     VITLGGIARE LLGMAVVLAR AGSDETALLA DIACASARVR LAGLWAQLDA SDPDFAGVAD
     ELLHGTAFDF LTTDVITDIP SVEDQK
//