ID   A0A438MMP0_9ACTN        Unreviewed;       623 AA.
AC   A0A438MMP0;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   SubName: Full=Alkylation response protein AidB-like acyl-CoA dehydrogenase {ECO:0000313|EMBL:RVX47062.1};
GN   ORFNames=EDD27_9983 {ECO:0000313|EMBL:RVX47062.1};
OS   Nonomuraea polychroma.
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Streptosporangiaceae; Nonomuraea.
OX   NCBI_TaxID=46176 {ECO:0000313|EMBL:RVX47062.1, ECO:0000313|Proteomes:UP000284824};
RN   [1] {ECO:0000313|EMBL:RVX47062.1, ECO:0000313|Proteomes:UP000284824}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 43925 {ECO:0000313|EMBL:RVX47062.1,
RC   ECO:0000313|Proteomes:UP000284824};
RA   Klenk H.-P.;
RT   "Sequencing the genomes of 1000 actinobacteria strains.";
RL   Submitted (JAN-2019) 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:RVX47062.1}.
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DR   EMBL; SAUN01000001; RVX47062.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A438MMP0; -.
DR   OrthoDB; 5241155at2; -.
DR   Proteomes; UP000284824; 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   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; 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; 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   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:UP000284824}.
FT   DOMAIN          56..163
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          166..256
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          268..426
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   623 AA;  68700 MW;  D8BE14B81050E7D2 CRC64;
     MTEHAKYAES RAVGEQAREK EWRLPSFGRQ LFLGDFRLDL VYPAPTLPDE ATKRGEEFVR
     AVRRYLDAHV DPALIERTGQ IPDEVVKGLA GLGAFGITIG EEYGGLGLPY LYYCRALMLV
     GSYCPALATL LSAHQSIGVP QPLKLFGTEE QKREFLPRCA AGEISAFLLT EPDVGSDPAR
     LSTTAVRDGD DYVLDGVKLW TTNGVVADLL VVMARTGKKI SAFVVEADSP GITVKRRNGF
     MGLRGIENGV TEFSQVRVPA KNLIGREGDG LRIALTTLNT GRLSLPATCA GNAKWALKIA
     REWGNARVQW GHKIGTHEAV ATKIAFIAAT AYALEAVMEL TSRLADDKRN DIRIEAALGK
     LYATEMSYQA LDELVQIRGG RGYETAESLA ARGERGVPAE QMLRDSRINR IFEGSSEIMR
     LMITREAVDA HLSAAGELIN PDASRHERTQ ALKRASRFYA KWLPTLVAGT GNLPTAYADF
     GPLAAHLRFV ERTSRKLARS TFYGMSRWQG RLEHKQSFLG RIVDIGAELF AMTAACVKAE
     EDAKDLGRRP YELADTFCHQ ARRRVDALFD RLWDNSDAHD ARLAGYVLEG RYGFVEEGIL
     DPSIEGPWIG TPEGGENVRR KIL
//