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Database: UniProt
Entry: B1VQW3_STRGG
LinkDB: B1VQW3_STRGG
Original site: B1VQW3_STRGG 
ID   B1VQW3_STRGG            Unreviewed;       608 AA.
AC   B1VQW3;
DT   20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT   20-MAY-2008, sequence version 1.
DT   27-MAR-2024, entry version 81.
DE   SubName: Full=Putative acyl-CoA dehydrogenase {ECO:0000313|EMBL:BAG20614.1};
GN   OrderedLocusNames=SGR_3785 {ECO:0000313|EMBL:BAG20614.1};
OS   Streptomyces griseus subsp. griseus (strain JCM 4626 / NBRC 13350).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=455632 {ECO:0000313|EMBL:BAG20614.1, ECO:0000313|Proteomes:UP000001685};
RN   [1] {ECO:0000313|EMBL:BAG20614.1, ECO:0000313|Proteomes:UP000001685}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 4626 / NBRC 13350 {ECO:0000313|Proteomes:UP000001685};
RX   PubMed=18375553; DOI=10.1128/JB.00204-08;
RA   Ohnishi Y., Ishikawa J., Hara H., Suzuki H., Ikenoya M., Ikeda H.,
RA   Yamashita A., Hattori M., Horinouchi S.;
RT   "Genome sequence of the streptomycin-producing microorganism Streptomyces
RT   griseus IFO 13350.";
RL   J. Bacteriol. 190:4050-4060(2008).
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; AP009493; BAG20614.1; -; Genomic_DNA.
DR   RefSeq; WP_012380141.1; NC_010572.1.
DR   AlphaFoldDB; B1VQW3; -.
DR   GeneID; 6209000; -.
DR   KEGG; sgr:SGR_3785; -.
DR   PATRIC; fig|455632.4.peg.3854; -.
DR   eggNOG; COG1960; Bacteria.
DR   HOGENOM; CLU_018204_12_1_11; -.
DR   Proteomes; UP000001685; 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}.
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..452
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
FT   DOMAIN          472..604
FT                   /note="Acetyl-CoA dehydrogenase-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12806"
SQ   SEQUENCE   608 AA;  66344 MW;  2DE7E0C51B3952A1 CRC64;
     MGHYKSNLRD IEFNLFEVLG RDKVYGTGPF GEMDVDTAKS ILDEIARLAE NELADSYADA
     DRNPPVFDPE TKTAPVPASF KKSYQAFMDS EYWRLGLPEE IGGTTSPRSL IWGYAELLLG
     ANPAVWMYSS GPAFAGILFE EGNDEQKKIA EIAVEKQWGS TMVLTEPDAG SDVGAGRTKA
     VRQEDGSWHI EGVKRFITSG EHDMSENIIH YVLARPEGAG PGTKGLSLFM VPKFHFDWTT
     GELGERNGVY ATNVEHKMGL KASNTCEMTF GDQHPAKGWL IGDKHDGIRQ MFRIIEFARM
     MVGTKAIAAL SAGYLNALEY AKERVQGPDL ANFMDKTAPK VTITHHPDVR RSLMTQKAYA
     EGMRSLVLYT ASVQDAIQEQ EAAGEDAKAL NGLNDLLLPI VKGYGSEKSY EQLAQSLQTF
     GGSGYLQEYP VEQYIRDAKI DTLYEGTTAI QGQDFFFRKI VRDQGASLNT LSEEIKKFLA
     GAHGNEELAP ALDSLAKAAV DLEAIVGTMI TDLTATGEDV KNIYKVGLNT TRLLMASGDV
     VVGYLLLKGA AVAAEKLPTA SAKDVPFYRG KIAAAKFFAA NVLPGVSTER ALAESVDNSL
     MELDEAAF
//
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