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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//