ID F2RKQ7_STRVP Unreviewed; 590 AA.
AC F2RKQ7;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:CCA55296.1};
DE EC=1.3.99.- {ECO:0000313|EMBL:CCA55296.1};
GN OrderedLocusNames=SVEN_2009 {ECO:0000313|EMBL:CCA55296.1};
OS Streptomyces venezuelae (strain ATCC 10712 / CBS 650.69 / DSM 40230 / JCM
OS 4526 / NBRC 13096 / PD 04745).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=953739 {ECO:0000313|EMBL:CCA55296.1, ECO:0000313|Proteomes:UP000006854};
RN [1] {ECO:0000313|EMBL:CCA55296.1, ECO:0000313|Proteomes:UP000006854}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10712 {ECO:0000313|EMBL:CCA55296.1};
RX PubMed=21463507; DOI=10.1186/1471-2164-12-175;
RA Pullan S.T., Bibb M.J., Merrick M.;
RT "Genome-wide analysis of the role of GlnR in Streptomyces venezuelae
RT provides new insights into global nitrogen regulation in actinomycetes.";
RL BMC Genomics 12:175-175(2011).
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; FR845719; CCA55296.1; -; Genomic_DNA.
DR AlphaFoldDB; F2RKQ7; -.
DR STRING; 953739.SVEN_2009; -.
DR KEGG; sve:SVEN_2009; -.
DR PATRIC; fig|953739.5.peg.4165; -.
DR eggNOG; COG1960; Bacteria.
DR HOGENOM; CLU_018204_9_3_11; -.
DR Proteomes; UP000006854; 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 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; 2.
DR Gene3D; 1.20.140.10; Butyryl-CoA Dehydrogenase, subunit A, domain 3; 2.
DR InterPro; IPR006091; Acyl-CoA_Oxase/DH_mid-dom.
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; PTHR43292; ACYL-COA DEHYDROGENASE; 1.
DR PANTHER; PTHR43292:SF4; ACYL-COA DEHYDROGENASE FADE34; 1.
DR Pfam; PF00441; Acyl-CoA_dh_1; 2.
DR Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR Pfam; PF02771; Acyl-CoA_dh_N; 1.
DR SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 2.
DR SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 2.
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|RuleBase:RU362125,
KW ECO:0000313|EMBL:CCA55296.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006854}.
FT DOMAIN 88..218
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT DOMAIN 234..332
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 336..421
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 444..585
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 590 AA; 62821 MW; 723D80C93FF58CD8 CRC64;
MHAVGGWRLD GVAPPVLGGA QADLVLLRAA TADGSVWLAV DVDGLAVRPH ESADPTRPTA
EITARGLHVP AARELALDTA LVHDLAAVLL AADACGTAAR AVETAAEHAR TREQFGRPIG
QFQGVKHLCA DMLVRLEQAR ALTWDAARAR DDEARSLTAA LAAATALDTA YTCAKDCIQI
LGGTGFTWEH HAHLLLRRAV VARQLLGSGD RHRLAALRHA ADGVRRGLRL DLPPEADAYR
REAREAVAPA AGLDPAAARR VLAPTGYAAP HLPEPYGLGA GPLQQLAVQR ELDEAGIGVS
GLGIATWVVP SLLAHGTAAQ QDEHLGPTLR GERLWCQLFS EPGAGSDLAS LRTRAERTED
GRWRINGQKV WTSAAQWAHY GILLARTDPA APKHKGLTYF LVDMRNTPGI DIRPLKEITG
ESLFNEVWFD DAILPADAVV GEVDDGWRVA RNTLGNERVH MADQVAFDTG LEALIERAGQ
QDASVRVRIG GLLAEAHALA CIGLRTTLLQ VSGLEPGAGA SVRKLVQTLH QQKLAELTLE
LLGPEGAVRE GPGERAVHGL LMSRCLTIAG GTTQVQLNVV AERLLGLPRD
//
