ID A0A161LIG3_9ACTN Unreviewed; 755 AA.
AC A0A161LIG3;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:GAT65247.1};
GN ORFNames=PS9374_00879 {ECO:0000313|EMBL:GAT65247.1};
OS Planomonospora sphaerica.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Streptosporangiaceae; Planomonospora.
OX NCBI_TaxID=161355 {ECO:0000313|EMBL:GAT65247.1, ECO:0000313|Proteomes:UP000077701};
RN [1] {ECO:0000313|EMBL:GAT65247.1, ECO:0000313|Proteomes:UP000077701}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 9374 {ECO:0000313|EMBL:GAT65247.1,
RC ECO:0000313|Proteomes:UP000077701};
RA Dohra H., Suzuki T., Inoue Y., Kodani S.;
RT "Draft Genome Sequence of Planomonospora sphaerica JCM9374, a Rare
RT Actinomycete.";
RL Genome Announc. 4:e00779-16(2016).
RN [2] {ECO:0000313|Proteomes:UP000077701}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 9374 {ECO:0000313|Proteomes:UP000077701};
RA Suzuki T., Dohra H., Kodani S.;
RT "Planomonospora sphaerica JCM9374 whole genome shotgun sequence.";
RL Submitted (APR-2016) 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:GAT65247.1}.
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DR EMBL; BDCX01000002; GAT65247.1; -; Genomic_DNA.
DR RefSeq; WP_068894625.1; NZ_BDCX01000002.1.
DR AlphaFoldDB; A0A161LIG3; -.
DR STRING; 161355.PS9374_00879; -.
DR OrthoDB; 3778631at2; -.
DR Proteomes; UP000077701; 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; 2.
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; 2.
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};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Reference proteome {ECO:0000313|Proteomes:UP000077701}.
FT DOMAIN 6..115
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 214..362
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT DOMAIN 398..485
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 489..583
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 595..745
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 755 AA; 78790 MW; 1F9062C503D98BCB CRC64;
MAIGLSEEHE ALHESVRGWA ERNIPSEVVR AAIAAESEAR PAFWSGLADQ GLLGLHIPEE
HGGSGYGLLE TAVAVEALGE RVAPGPYVPT VLASAAILAA EGKAGAELLP GLADGTLTGA
VALRGSISGG RGADGALTVG GTAEFVLGGA LADVLVLPVH TDRGEVWVAV DASAATVTPV
GSLDLTRGVA RVELDGVAVP ADRVLDGLKG SAVLNLAAIL LGAEAAGVAS WCVASAAEYA
KVRVQFGRPI GQFQGVKHKA SRMLVALEQA RATVWDAARA TTDTERRADA AGGAGAAEGE
GAGAGDESAY AAAIAGVTAP DAAVQCAKDA VQIFGGIGYT YEHDVHLYYR RALTLRALLG
PSSEWAESVA ELALNGVSRE MEIELPEDAA ALRESIRAEI AAIARLEGRE QKRALADGGF
VMPHLPRPWG RGASPLEQVL IFQELKAARV KLPQMIIGAW VVPSIAAYGT REQQERFLPK
TLAGEMIWCQ LFSEPGAGSD LAALQMKAER VEGGWRLNGQ KIWTSVAHFA EWGICIARNS
SEGSKHEGIT YFLVDMKAPG VTVRPLTEMT GENLFNEVFL DDVFVPDDLV VGEVGEGWKV
ARNTLSNERV SLSSGSGGTG ASVPDLLGLA GRLGRELNPA ERQELARVVC EGHSINALSL
RVTMKQLAGA EPGADASVRK LLSTSHAQHV SECAVGLLGA SAVLAADVKL GDPGFWNRAV
LATRAMTIYG GTTEVQLNII AERMLGLPRD PEPGK
//