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Database: UniProt
Entry: A0A0N1GN10_9ACTN
LinkDB: A0A0N1GN10_9ACTN
Original site: A0A0N1GN10_9ACTN 
ID   A0A0N1GN10_9ACTN        Unreviewed;       404 AA.
AC   A0A0N1GN10;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Butyryl-CoA dehydrogenase {ECO:0000313|EMBL:KPI28013.1};
DE            EC=1.3.8.1 {ECO:0000313|EMBL:KPI28013.1};
GN   ORFNames=OV320_6061 {ECO:0000313|EMBL:KPI28013.1};
OS   Actinobacteria bacterium OV320.
OC   Bacteria; Actinomycetota; Actinomycetes.
OX   NCBI_TaxID=1592329 {ECO:0000313|EMBL:KPI28013.1, ECO:0000313|Proteomes:UP000037870};
RN   [1] {ECO:0000313|EMBL:KPI28013.1, ECO:0000313|Proteomes:UP000037870}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OV320 {ECO:0000313|EMBL:KPI28013.1,
RC   ECO:0000313|Proteomes:UP000037870};
RA   Brown S.D., Utturkar S.M., Klingeman D.M., Pelletier D.;
RT   "Draft genome sequences for four actinobacteria strains OK006 OK074 OV450
RT   and OV320.";
RL   Submitted (AUG-2015) 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}.
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:KPI28013.1}.
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DR   EMBL; LJCX01000027; KPI28013.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0N1GN10; -.
DR   PATRIC; fig|1592329.3.peg.5365; -.
DR   Proteomes; UP000037870; Unassembled WGS sequence.
DR   GO; GO:0004085; F:butyryl-CoA dehydrogenase activity; IEA:UniProtKB-EC.
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; 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.
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:KPI28013.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037870}.
FT   DOMAIN          11..122
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          126..233
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          248..397
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   404 AA;  44438 MW;  E3B2DEC1A2D01D86 CRC64;
     MARLAQTAGL TDIQQEILST VRDFVDKEII PVATGLEHRD EYPQQIVDGL KELGLFGLMI
     PEEYGGLGES LLTYALCVEE IARGWMSVSG IINTHFIVAY MLKQHGTQEQ KDHYLPRMAA
     GDIRGAFSMS EPALGSDVSA ITSKAVKDGD EYVLNGQKMW LTNGGTSSLV AVLVRSDEGH
     SPEEAAAKPH KSMTTFLIEK EPGFGEVRPG LTIPGKIDKM GYKGVDTTEM IMDGLRLPAD
     RVLGGVTGRG FYQMMDGVEV GRVNVAARGC GVAQRAFELG VSYAQQRHTF GKPIAQHQAI
     QFKLAEMATK VEAAHAMMVN AARKKDSGER NDLEAGMAKY LASEYCKEVV EDAFRIHGGY
     GFSKEYEIER LYREAPMLLI GEGTAEIQKM IIGRRLLEEY RFQG
//
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