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Database: UniProt
Entry: A0A367F545_9ACTN
LinkDB: A0A367F545_9ACTN
Original site: A0A367F545_9ACTN 
ID   A0A367F545_9ACTN        Unreviewed;       369 AA.
AC   A0A367F545;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:RCG24855.1};
GN   ORFNames=DTL70_11070 {ECO:0000313|EMBL:RCG24855.1};
OS   Streptomyces diacarni.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=2800381 {ECO:0000313|EMBL:RCG24855.1, ECO:0000313|Proteomes:UP000252914};
RN   [1] {ECO:0000313|EMBL:RCG24855.1, ECO:0000313|Proteomes:UP000252914}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LHW51701 {ECO:0000313|EMBL:RCG24855.1,
RC   ECO:0000313|Proteomes:UP000252914};
RA   Li L.;
RT   "Streptomyces reniochalinae sp. nov. and Streptomyces diacarnus sp. nov.
RT   from marine sponges.";
RL   Submitted (JUN-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:RCG24855.1}.
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DR   EMBL; QOIN01000039; RCG24855.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A367F545; -.
DR   OrthoDB; 4319499at2; -.
DR   Proteomes; UP000252914; 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   CDD; cd00567; ACAD; 1.
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   Reference proteome {ECO:0000313|Proteomes:UP000252914}.
FT   DOMAIN          7..116
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          216..343
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   369 AA;  37981 MW;  DB8272F16BECEC9F CRC64;
     MDFSLGEELE AVRELARKIF TDRATPERLR TVETSATRVD QQLWDDLAAA GLLGVVLPEE
     AGGAGLGPAG LCLLLEEQGR CVAPVPLWSA LVAAMAVSAH GSARQRAARL PSAVDGSARI
     ALALEEFGPA GPDAPLTTAT HGADGWRISG TKAAVPSPGG AGHVLLTAAT GAGPRLFLVA
     ADAAGLTWEE AETTSHDLSA HLGLDGAAAE ALGDPGSGAV RGTLDLASVA LAAVQLGVAQ
     GALRHAAGHL AQREQFGRPL ATFQAVRHQL ADCYIDIEAM RMTLWQAVTA LEDGEGATRA
     ALVAKWWATE GGANVVHRVQ HVHGGIGVDI DYPVHRHFLW GRQLATTLGG AGADLFRLGE
     ELAHGGAAS
//
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