ID A0A0B5EXF7_STRA4 Unreviewed; 608 AA.
AC A0A0B5EXF7;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:AJE83905.1};
GN ORFNames=SLNWT_3529 {ECO:0000313|EMBL:AJE83905.1};
OS Streptomyces albus (strain ATCC 21838 / DSM 41398 / FERM P-419 / JCM 4703 /
OS NBRC 107858).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1081613 {ECO:0000313|EMBL:AJE83905.1, ECO:0000313|Proteomes:UP000031523};
RN [1] {ECO:0000313|EMBL:AJE83905.1, ECO:0000313|Proteomes:UP000031523}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 21838 / DSM 41398 / FERM P-419 / JCM 4703 / NBRC 107858
RC {ECO:0000313|Proteomes:UP000031523};
RA Lu C.;
RT "Enhanced salinomycin production by adjusting the supply of polyketide
RT extender units in Streptomyce albus DSM 41398.";
RL Submitted (JAN-2015) 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}.
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DR EMBL; CP010519; AJE83905.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B5EXF7; -.
DR STRING; 1888.Salbus254_3287; -.
DR KEGG; sals:SLNWT_3529; -.
DR Proteomes; UP000031523; Chromosome.
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; cd01153; ACAD_fadE5; 1.
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 InterPro; IPR034188; FadE5-like.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000031523}.
FT DOMAIN 3..34
FT /note="Acyl-CoA dehydrogenase N-terminal bacteria"
FT /evidence="ECO:0000259|Pfam:PF12418"
FT DOMAIN 162..272
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 286..451
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT DOMAIN 471..604
FT /note="Acetyl-CoA dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12806"
SQ SEQUENCE 608 AA; 66429 MW; EE5BEB0DA24E20F1 CRC64;
MGHYKSNLRD IEFNLFEVLG RDKLYGTGPF AEMDTDTVKS ILSEINRLAE NELAESYADA
DRNPPVFDPA TNTAPVPESF KKSYKAFMDS EYWRLGLPEE IGGTSTPPSV IWAYAELLLG
ANPAIWMYSS GPAFARILFE EGTAQQQEIA KIAVEKTWGA TMVLTEPDAG SDVGAGRTKA
VQQEDGSWHI EGVKRFITSG EHDMEENIIH YVLARPEGAG PGTKGLSLFL VPKFLFDFET
GELGERNGVY ATNVEHKMGL KASNTCEMTF GDQHPAKGWL IGDKHDGIRQ MFRIIEFARM
MVGTKAISTL STGYLNALEY AKERVQGPDL AQFMDKTAPK VTITHHPDVR RSLMTQKAYA
EGMRALVLHT ATVQDAIALG EANGDDVTEL SNLNDLLLPI VKGYGSEKAY EQLAQSLQTF
GGSGYLQEYP IEQYIRDAKI DTLYEGTTAI QGQDYFFRKI VRNQGAALNS LAEDIKKFLA
EASGGEELAE AREQLGKAAV DLESIVGTML TDLAGTEKDV KSIYKVGLNA TRLLLASGDV
VVGYLLLRGA AVAAEKLPSA SSKDKAFYQG KIAAAKFFAA NILSGLALQR QLSESVDLGL
MELDEAAF
//
