ID   A0A3N4RRS7_9ACTN        Unreviewed;       609 AA.
AC   A0A3N4RRS7; A0A8G1UFM2;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Alkylation response protein AidB-like acyl-CoA dehydrogenase {ECO:0000313|EMBL:RPE33435.1};
GN   ORFNames=EDD38_1725 {ECO:0000313|EMBL:RPE33435.1}, EDD39_1206
GN   {ECO:0000313|EMBL:ROR43066.1};
OS   Kitasatospora cineracea.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Kitasatospora.
OX   NCBI_TaxID=88074 {ECO:0000313|EMBL:RPE33435.1, ECO:0000313|Proteomes:UP000266906};
RN   [1] {ECO:0000313|Proteomes:UP000266906, ECO:0000313|Proteomes:UP000267408}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44780 {ECO:0000313|EMBL:ROR43066.1,
RC   ECO:0000313|Proteomes:UP000267408}, and DSM 44781
RC   {ECO:0000313|EMBL:RPE33435.1, ECO:0000313|Proteomes:UP000266906};
RA   Klenk H.-P.;
RT   "Sequencing the genomes of 1000 actinobacteria strains.";
RL   Submitted (NOV-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:RPE33435.1}.
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DR   EMBL; RJVJ01000001; ROR43066.1; -; Genomic_DNA.
DR   EMBL; RKQG01000001; RPE33435.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3N4RRS7; -.
DR   Proteomes; UP000266906; Unassembled WGS sequence.
DR   Proteomes; UP000267408; 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; 2.40.110.20; -; 1.
DR   Gene3D; 1.20.140.10; Butyryl-CoA Dehydrogenase, subunit A, domain 3; 1.
DR   InterPro; IPR025878; Acyl-CoA_dh-like_C_dom.
DR   InterPro; IPR020953; Acyl-CoA_DH_N_bac.
DR   InterPro; IPR006091; Acyl-CoA_Oxase/DH_mid-dom.
DR   InterPro; IPR036250; AcylCo_DH-like_C.
DR   InterPro; IPR009075; AcylCo_DH/oxidase_C.
DR   InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom_sf.
DR   PANTHER; PTHR42803; ACYL-COA DEHYDROGENASE; 1.
DR   PANTHER; PTHR42803:SF1; BROAD-SPECIFICITY LINEAR ACYL-COA DEHYDROGENASE FADE5; 1.
DR   Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR   Pfam; PF12806; Acyl-CoA_dh_C; 1.
DR   Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR   Pfam; PF12418; AcylCoA_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|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU362125}.
FT   DOMAIN          3..34
FT                   /note="Acyl-CoA dehydrogenase N-terminal bacteria"
FT                   /evidence="ECO:0000259|Pfam:PF12418"
FT   DOMAIN          162..270
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          286..452
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
FT   DOMAIN          473..604
FT                   /note="Acetyl-CoA dehydrogenase-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12806"
SQ   SEQUENCE   609 AA;  66663 MW;  2D3240D29C6F8217 CRC64;
     MGHYKSNLRD VEFNLFEVFG RDQVYGTGPF AEMDVDTAKN ILSEIARLAE NDLAASFVDA
     DRNPPVFDPE TNTAPIPETF KKSYQTFMDA EWWRLGIPEG IGGQVTPNSL VWAYAEQVLG
     ANPAIWMYSS GPAFAGVVHD EGTEEQQKVA QRMVEGLWGA TMVLTEPDAG SDVGAGRTKA
     VKQEDGSWHI EGVKRFITSG EHDMSENIIH LVLARPEGGK PGTKGLGLYI VPKFDFDWET
     GELGERNGVY ATNVEHKMGL KASNTCEMTF GAKHPAKGWL LGETVDGIRQ MFKIIEFARM
     MVGTKAIATL STGYLNALEY AKERVQGADL AQFMDKTAPR VTITHHPDVR RSLLTQKAYA
     EGMRALVLYT ASVQDDMLAA RLRGEHDAAA ERLNDLLLPI VKGYGSEKSY EQLAQSLQTF
     GGSGYLQEYP IEQYIRDAKI DTLYEGTTAI QGQDFFFRKI VKDGGQALTA VNEQITKFLA
     TGEGGAELAA ERDLLAKAAG DLEAIVGKLI ADLSAVEADV KNMYKVGQNT TRLLLVSGDV
     VVGWLLLRQA AVALAKLEAG ASEKDVPFYR GKVAAAKHFA RTVLPTTAAQ RQIAENIDNE
     LMELAEEAF
//