ID A0A1D8G0S4_9ACTN Unreviewed; 385 AA.
AC A0A1D8G0S4;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Acryloyl-CoA reductase (NADH) {ECO:0000313|EMBL:AOT58996.1};
DE EC=1.3.1.95 {ECO:0000313|EMBL:AOT58996.1};
GN Name=acrC_2 {ECO:0000313|EMBL:AOT58996.1};
GN ORFNames=A4G23_01821 {ECO:0000313|EMBL:AOT58996.1};
OS Streptomyces rubrolavendulae.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=285473 {ECO:0000313|EMBL:AOT58996.1, ECO:0000313|Proteomes:UP000095349};
RN [1] {ECO:0000313|EMBL:AOT58996.1, ECO:0000313|Proteomes:UP000095349}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MJM4426 {ECO:0000313|EMBL:AOT58996.1,
RC ECO:0000313|Proteomes:UP000095349};
RA Kim J.-G.;
RT "Streptomyces rubrolavendulae MJM4426 Genome sequencing and assembly.";
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
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; CP017316; AOT58996.1; -; Genomic_DNA.
DR RefSeq; WP_069976485.1; NZ_CP017316.1.
DR AlphaFoldDB; A0A1D8G0S4; -.
DR STRING; 285473.A4G23_01821; -.
DR KEGG; srn:A4G23_01821; -.
DR PATRIC; fig|285473.5.peg.1895; -.
DR OrthoDB; 8876745at2; -.
DR Proteomes; UP000095349; Chromosome.
DR GO; GO:0043958; F:acryloyl-CoA reductase (NADH) activity; IEA:UniProtKB-EC.
DR GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IEA:InterPro.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
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; IPR006089; Acyl-CoA_DH_CS.
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; PTHR43884; ACYL-COA DEHYDROGENASE; 1.
DR PANTHER; PTHR43884:SF12; COMPLEX I ASSEMBLY FACTOR ACAD9, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR Pfam; PF02771; Acyl-CoA_dh_N; 1.
DR PIRSF; PIRSF016578; HsaA; 2.
DR SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
DR PROSITE; PS00073; ACYL_COA_DH_2; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000095349}.
FT DOMAIN 7..119
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 123..223
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 235..383
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 385 AA; 42174 MW; 1C0EF1B64542ED31 CRC64;
MRRTVFNEDH EAFRDTIRAF IEAEVVPVYD EWFAAGQAPR DFYYKLGELG IFGINVPEEF
GGAGLDTHKF EAVLYEETAR AGVQFGGSGV HVLLALPYIK MLASDEQKRR YLPKFVTGEE
MWALAMTEPG TGSDVAGMKT TAKLSEDGTH YVLNGAKTFI TGGVHADRVI VCARTSAPSA
EDRRFGISLF AVDTKSEGYS IGRKLDKLGL RTSDTAELAF VDVKVPVEDL LGEEGKGFSY
LGHNLASERW GIAFGAYAQA KAAIRFAQQY VQERTVFGKP VAHFQNTKFE LAACQAEVDA
AEAVADRALE ALDAGELTPA EAASAKLFCT EVAHRVIDRC LQLHGGYGYM NEYPIARLYA
DNRVNRIYGG TSEIMKSIIA KSMGL
//
