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Database: UniProt
Entry: A0A0A7KDN6_9DEIO
LinkDB: A0A0A7KDN6_9DEIO
Original site: A0A0A7KDN6_9DEIO 
ID   A0A0A7KDN6_9DEIO        Unreviewed;       386 AA.
AC   A0A0A7KDN6;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:AIZ44246.1};
GN   ORFNames=QR90_02660 {ECO:0000313|EMBL:AIZ44246.1};
OS   Deinococcus radiopugnans.
OC   Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=57497 {ECO:0000313|EMBL:AIZ44246.1, ECO:0000313|Proteomes:UP000030634};
RN   [1] {ECO:0000313|Proteomes:UP000030634}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DY59 {ECO:0000313|Proteomes:UP000030634};
RA   Jung H.-Y., Kim M.K., Srinivasan S., Lim S.;
RT   "Hymenobacter sp. DG25B genome submission.";
RL   Submitted (NOV-2014) 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; CP010028; AIZ44246.1; -; Genomic_DNA.
DR   RefSeq; WP_039682030.1; NZ_CP010028.1.
DR   AlphaFoldDB; A0A0A7KDN6; -.
DR   STRING; 1182571.QR90_02660; -.
DR   KEGG; dsw:QR90_02660; -.
DR   HOGENOM; CLU_018204_3_5_0; -.
DR   Proteomes; UP000030634; Chromosome.
DR   GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IEA:InterPro.
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:UP000030634}.
FT   DOMAIN          11..122
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          126..220
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          232..380
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   386 AA;  41172 MW;  7188188E09585DA7 CRC64;
     MTSGMGFALN DDSRMILQHV RDFCRAEIAP LAADYDRSGE FPHPQLRGLA EMGLLGATVP
     EAWGGAALDS VTYALCLEEI SAADASVGVI VSVQNGLPEQ MILRYGTDAQ RETYLKPLAS
     GERIGAFCLT EASAGSDAAS LRLRAVREGD DWVLDGAKAW ITSGGQAATY LVMARTGGSG
     ARGVSCFIVE KGMDGLGFGK PEEKMGLHAA HTTTVTFDGV RVPHANMVGE EGQGLIVALA
     SLDAGRIGIA MQAIGIARAA LEHASKYANE REQFGKKLRE FEGVSFKIAR MAARIESARL
     VALKAAWLKD QGQPYGKEAS MAKLLASEAA VDCARDAIQI FGGNGYSRDY PVERLFRDAK
     VTEIYEGTSE IQQLVISRAV FAELEG
//
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