ID A0A3N6HHB8_9ACTN Unreviewed; 428 AA.
AC A0A3N6HHB8;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:RPK60735.1};
DE EC=1.3.99.- {ECO:0000313|EMBL:RPK60735.1};
GN Name=acdA7 {ECO:0000313|EMBL:RPK60735.1};
GN ORFNames=EES43_16820 {ECO:0000313|EMBL:RPK60735.1};
OS Streptomyces sp. ADI96-02.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1522760 {ECO:0000313|EMBL:RPK60735.1, ECO:0000313|Proteomes:UP000273170};
RN [1] {ECO:0000313|EMBL:RPK60735.1, ECO:0000313|Proteomes:UP000273170}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ADI96-02 {ECO:0000313|EMBL:RPK60735.1,
RC ECO:0000313|Proteomes:UP000273170};
RA Guerrero-Garzon J.F., Zehl M., Urban E., Schneider O., Ruckert C.,
RA Busche T., Kalinowski J., Zotchev S.B.;
RT "Streptomyces spp. from the marine sponge Antho dichothoma: analyses of
RT secondary metabolite biosynthesis gene clusters and some of their
RT products.";
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 -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009347}.
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:RPK60735.1}.
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DR EMBL; RPGW01000096; RPK60735.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N6HHB8; -.
DR OrthoDB; 8677713at2; -.
DR Proteomes; UP000273170; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
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; 1.
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:SF20; ACYL-COA DEHYDROGENASE FADE28; 1.
DR Pfam; PF00441; Acyl-CoA_dh_1; 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};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022827};
KW Oxidoreductase {ECO:0000313|EMBL:RPK60735.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000273170}.
FT DOMAIN 6..118
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 259..382
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 428 AA; 43691 MW; 32CE56016319EA19 CRC64;
MDAAFTEEQE AIRRTLRDLL AEHAGPGAVR AAVRTPEGYD PALWRRLARD LGLPGLALPE
EYGGAGCTAT ELALACEETG RALLPSPLLA TAVLAAPLIA ALGTPGQRAG LLPRIADGSL
TAALALPGPS PAAALGLTGD NRDGAWAGGG RSGGVQAHRA ADGGGWRLYG EADRVPDGHS
AGLLLVAAHA GGYPRSRTLL FLVRPEAAAG LVRTRLTAMD ETRPLARVEL RDTEAELLGA
DDAQDVLGAL AGTGRTAAAV LAAEAVGTAA GALERTVAYV KQREQFGRAI GSFQAVKHRL
ADLYVRVEAA RSAAYYAAWD PSAGPLALAQ ALEAARIATG EAVQLHGGTG FTWEHEAHLY
FKRAAGDELL LGPVHRLRDR AARLAGLFGA ADGEAGDDGT GDGGTGGTDG GAADARAAGA
RAAYRAVV
//
