ID A0A0A1DRY3_NOCSI Unreviewed; 364 AA.
AC A0A0A1DRY3;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 2.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Butyryl-CoA dehydrogenase {ECO:0000313|EMBL:AIY19323.2};
DE EC=1.3.8.1 {ECO:0000313|EMBL:AIY19323.2};
GN ORFNames=KR76_25720 {ECO:0000313|EMBL:AIY19323.2};
OS Nocardioides simplex (Arthrobacter simplex).
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Pimelobacter.
OX NCBI_TaxID=2045 {ECO:0000313|EMBL:AIY19323.2, ECO:0000313|Proteomes:UP000030300};
RN [1] {ECO:0000313|EMBL:AIY19323.2, ECO:0000313|Proteomes:UP000030300}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM Ac-2033D {ECO:0000313|EMBL:AIY19323.2,
RC ECO:0000313|Proteomes:UP000030300};
RX PubMed=25573942;
RA Shtratnikova V.Y., Schelkunov M.I., Pekov Y.A., Fokina V.V.,
RA Logacheva M.D., Sokolov S.L., Bragin E.Y., Ashapkin V.V., Donova M.V.;
RT "Complete Genome Sequence of Steroid-Transforming Nocardioides simplex VKM
RT Ac-2033D.";
RL Genome Announc. 3:0-0(2015).
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; CP009896; AIY19323.2; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A1DRY3; -.
DR STRING; 2045.KR76_25720; -.
DR KEGG; psim:KR76_25720; -.
DR eggNOG; COG1960; Bacteria.
DR HOGENOM; CLU_018204_3_0_11; -.
DR Proteomes; UP000030300; Chromosome.
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 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; 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:SF40; -; 1.
DR PANTHER; PTHR43884; ACYL-COA DEHYDROGENASE; 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 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:AIY19323.2};
KW Reference proteome {ECO:0000313|Proteomes:UP000030300}.
FT DOMAIN 2..69
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 77..184
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 196..343
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 364 AA; 39153 MW; A34B009B340F654D CRC64;
MDAGFVKALI PDAQGGQKMS SVDFSIAAEE LTSVDVNVPT ALLATGLGLQ AIIHFGTDEQ
KERWLRPFTG TDALLAAFGF TEAGGGANFD SKDPSVGVRT HARLEGDEWV INGTKHYTTN
GTGWEGKGPD LITLVCRTDM TKPPHESLAV IVVPGNTPGL EVSGLIDTVG HRATISPKLT
FTDVRVPAGN ILGKPGDGME ICRMAFNWTA SLIGAACVGR MRAAFEFALN WAKTERRNGP
VPVIEYQNAG YMLVDIKTRI EAARYLTWKA CHHYDVTGGA DEELGHMAKV FCSELSVQAV
YDTMRLVGVD GYGDQTPIAA IMNDVLCFPV YDGGNMGVRR RQLHELIARD TYDGMASAEG
RVAG
//
