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Database: UniProt
Entry: E8UAU7_DEIML
LinkDB: E8UAU7_DEIML
Original site: E8UAU7_DEIML 
ID   E8UAU7_DEIML            Unreviewed;       393 AA.
AC   E8UAU7;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   27-MAR-2024, entry version 62.
DE   SubName: Full=Butyryl-CoA dehydrogenase {ECO:0000313|EMBL:ADV68186.1};
DE            EC=1.3.8.1 {ECO:0000313|EMBL:ADV68186.1};
DE   Flags: Precursor;
GN   OrderedLocusNames=Deima_2552 {ECO:0000313|EMBL:ADV68186.1};
OS   Deinococcus maricopensis (strain DSM 21211 / LMG 22137 / NRRL B-23946 /
OS   LB-34).
OC   Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=709986 {ECO:0000313|EMBL:ADV68186.1, ECO:0000313|Proteomes:UP000008635};
RN   [1] {ECO:0000313|EMBL:ADV68186.1, ECO:0000313|Proteomes:UP000008635}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21211 / LMG 22137 / NRRL B-23946 / LB-34
RC   {ECO:0000313|Proteomes:UP000008635};
RX   PubMed=21677853; DOI=10.4056/sigs.1633949;
RA   Pukall R., Zeytun A., Lucas S., Lapidus A., Hammon N., Deshpande S.,
RA   Nolan M., Cheng J.F., Pitluck S., Liolios K., Pagani I., Mikhailova N.,
RA   Ivanova N., Mavromatis K., Pati A., Tapia R., Han C., Goodwin L., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA   Brambilla E.M., Rohde M., Goker M., Detter J.C., Woyke T., Bristow J.,
RA   Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Deinococcus maricopensis type strain (LB-
RT   34).";
RL   Stand. Genomic Sci. 4:163-172(2011).
RN   [2] {ECO:0000313|Proteomes:UP000008635}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21211 / LMG 22137 / NRRL B-23946 / LB-34
RC   {ECO:0000313|Proteomes:UP000008635};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Goodwin L., Pitluck S., Kyrpides N.,
RA   Mavromatis K., Pagani I., Ivanova N., Ovchinnikova G., Zeytun A.,
RA   Detter J.C., Han C., Land M., Hauser L., Markowitz V., Cheng J.-F.,
RA   Hugenholtz P., Woyke T., Wu D., Pukall R., Gehrich-Schroeter G.,
RA   Brambilla E., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Deinococcus maricopensis DSM 21211.";
RL   Submitted (JAN-2011) 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; CP002454; ADV68186.1; -; Genomic_DNA.
DR   RefSeq; WP_013557690.1; NC_014958.1.
DR   AlphaFoldDB; E8UAU7; -.
DR   STRING; 709986.Deima_2552; -.
DR   KEGG; dmr:Deima_2552; -.
DR   eggNOG; COG1960; Bacteria.
DR   HOGENOM; CLU_018204_0_2_0; -.
DR   OrthoDB; 9802447at2; -.
DR   Proteomes; UP000008635; 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; cd01158; SCAD_SBCAD; 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; 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; 1.
DR   SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
DR   PROSITE; PS00072; ACYL_COA_DH_1; 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:UP000008635}.
FT   DOMAIN          17..128
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          133..227
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          239..387
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   393 AA;  42360 MW;  5E26C32421F11378 CRC64;
     MSTPTLDTDL GMSFALSDDQ RLILQHVREF AQAEIAPKAA EHDRSGAYPR EQLRGLAQLG
     LLGATVPERW GGAGLDSVTY ALCLEEIAAA DASVAVIVSV QNGLPEQMIL RYGTDAQRER
     YLRPLAEGRH IGAFCLTEST AGSDAASLQL RAERDGDHYV LNGSKAWITS GSQADTYLVM
     ARTGGAGARG VSCFIVENGT PGLSFGRPEE KMGLHAAHTT TVQFEDVRVP AENLVGAEGE
     GLIIALSSLD AGRIGIAMQA LGIARAAFEH AARYALEREQ FGRKLREFEG VSFKIADMAA
     HIEAARLVAL KAAWLKDAGR PYGREASIAK LLASDAAVNV TRDAIQVFGG NGYSREYPVE
     RLYRDAKVTE IYEGTSEIQR LVISRSVFNE FGQ
//
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