ID Q9RYQ8_DEIRA Unreviewed; 637 AA.
AC Q9RYQ8;
DT 01-MAY-2000, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2000, sequence version 1.
DT 27-MAR-2024, entry version 134.
DE SubName: Full=Acyl-CoA dehydrogenase, putative {ECO:0000313|EMBL:AAF12388.1};
GN OrderedLocusNames=DR_A0250 {ECO:0000313|EMBL:AAF12388.1};
OS Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / CCUG
OS 27074 / LMG 4051 / NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1).
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=243230 {ECO:0000313|EMBL:AAF12388.1, ECO:0000313|Proteomes:UP000002524};
RN [1] {ECO:0000313|EMBL:AAF12388.1, ECO:0000313|Proteomes:UP000002524}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 /
RC NCIMB 9279 / R1 / VKM B-1422 {ECO:0000313|Proteomes:UP000002524};
RX PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA Vamathevan J.J., Lam P., McDonald L., Utterback T., Zalewski C.,
RA Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA Ketchum K.A., Nelson K.E., Salzberg S., Smith H.O., Venter J.C.,
RA Fraser C.M.;
RT "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT R1.";
RL Science 286:1571-1577(1999).
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; AE001825; AAF12388.1; -; Genomic_DNA.
DR PIR; C75578; C75578.
DR RefSeq; NP_285573.1; NC_001264.1.
DR AlphaFoldDB; Q9RYQ8; -.
DR STRING; 243230.DR_A0250; -.
DR PaxDb; 243230-DR_A0250; -.
DR EnsemblBacteria; AAF12388; AAF12388; DR_A0250.
DR KEGG; dra:DR_A0250; -.
DR PATRIC; fig|243230.17.peg.3139; -.
DR eggNOG; COG1960; Bacteria.
DR HOGENOM; CLU_018204_12_2_0; -.
DR InParanoid; Q9RYQ8; -.
DR OrthoDB; 9771038at2; -.
DR Proteomes; UP000002524; Chromosome II.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
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; IPR025878; Acyl-CoA_dh-like_C_dom.
DR InterPro; IPR020953; Acyl-CoA_DH_N_bac.
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; PTHR42803; ACYL-COA DEHYDROGENASE; 1.
DR PANTHER; PTHR42803:SF3; ACYL-COA DEHYDROGENASE-RELATED; 1.
DR Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR Pfam; PF12806; Acyl-CoA_dh_C; 1.
DR Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR Pfam; PF02771; Acyl-CoA_dh_N; 1.
DR Pfam; PF12418; AcylCoA_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 Reference proteome {ECO:0000313|Proteomes:UP000002524}.
FT DOMAIN 44..72
FT /note="Acyl-CoA dehydrogenase N-terminal bacteria"
FT /evidence="ECO:0000259|Pfam:PF12418"
FT DOMAIN 86..194
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 200..276
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 322..489
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT DOMAIN 509..633
FT /note="Acetyl-CoA dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12806"
SQ SEQUENCE 637 AA; 69706 MW; EBCF21B96D1A4E18 CRC64;
MCPIVTPTYK VNVDGHFSAC CVCRCFPSLR PFFLRRLVLM APFLNKRDLQ FQLFEVLDTA
QLPERPRFAE HSREVYQDVL NVAYNVAEKY FANHARAADV NEPHVVDGKV KLVPEAQQAV
EAFRDAGFFS AHHDEELGGL QLPWVVMQAV QANFQAANPG TASYTFLTIG NANLQREFGS
PEQQEKYLLP LLEGRWFGTM ALSEPQAGSG LADITTTATL RDDGTYSITG TKMWISGGEH
ELTENIVHLV LARIKGAPAG VKGISLFLVP RYRINPDGSV GESNHVVLAG LNHKLGHRGT
TNTLLNFGEG GETIGELVGE PGRGLAQMFH MMNEARIGVG MGAVMSGYAG YLASLEYARD
RRQGRHASNR DPQAESVAII EHADVKRMLL RQKVFVEGGL ALGLYAASLV DDLNTGPEEE
KADTALLLDL LTPIVKSWPS KYSQEALSDA IQVMGGAGYT RDTPVEMYYR DNRLNPIHEG
TEGIQGNDLL GRKLTQANGR GLQVLLGKMG ADLKAAEQEG ELSDIRTALQ EAIGQCAAAL
GSLLGRAAEL GPDLFLANAN AALDMVGHTV VGWMWLRQGL AAARALPDAR GDDRDFYEGK
LHAARFFARY ELPKVRTWAE LLASADPTTV EMQENWF
//
