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Database: UniProt
Entry: Q9RWW4_DEIRA
LinkDB: Q9RWW4_DEIRA
Original site: Q9RWW4_DEIRA 
ID   Q9RWW4_DEIRA            Unreviewed;       414 AA.
AC   Q9RWW4;
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=Glutaryl-CoA dehydrogenase, putative {ECO:0000313|EMBL:AAF10130.1};
GN   OrderedLocusNames=DR_0551 {ECO:0000313|EMBL:AAF10130.1};
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:AAF10130.1, ECO:0000313|Proteomes:UP000002524};
RN   [1] {ECO:0000313|EMBL:AAF10130.1, 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; AE000513; AAF10130.1; -; Genomic_DNA.
DR   PIR; A75505; A75505.
DR   RefSeq; NP_294274.1; NC_001263.1.
DR   AlphaFoldDB; Q9RWW4; -.
DR   STRING; 243230.DR_0551; -.
DR   PaxDb; 243230-DR_0551; -.
DR   EnsemblBacteria; AAF10130; AAF10130; DR_0551.
DR   KEGG; dra:DR_0551; -.
DR   PATRIC; fig|243230.17.peg.726; -.
DR   eggNOG; COG1960; Bacteria.
DR   HOGENOM; CLU_018204_8_2_0; -.
DR   InParanoid; Q9RWW4; -.
DR   OrthoDB; 9802447at2; -.
DR   Proteomes; UP000002524; Chromosome I.
DR   GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IEA:InterPro.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006635; P:fatty acid beta-oxidation; 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; IPR045008; ACX4-like.
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; PTHR43188; ACYL-COENZYME A OXIDASE; 1.
DR   PANTHER; PTHR43188:SF1; ACYL-COENZYME A OXIDASE 4, PEROXISOMAL; 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.
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|RuleBase:RU362125};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002524}.
FT   DOMAIN          39..150
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          155..248
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          260..407
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   414 AA;  45705 MW;  C0874F5E5668E28C CRC64;
     MNDKQLKQLS RALGVGGSGR QRVLPAADGD YYDYLDTLTD SQVEVAGRVH DFMRAEVMPI
     MNEYWSRDEF PRDLIGKMRE LNLLRSIWNE DGTRKPDATL IEGVVILEAC RVDVSTAVFF
     GVHGGLATAS IALGSDEEQK KRWLPDMLDM KKIGAFGLTE PEGGSQVSEG MRTTCRRDGD
     GWVLNGEKKW IGNSTFSDFT VIWARDEETN EVRGFVVEAG TPGYDVEKIQ GKIALRMVEN
     GHITLKDCRV ADANRLQAVQ GWETVSQVLK LTRAGVAWQG VGCAMGAYEL ALAYTQTRKQ
     FGKRIGEFQL IQSHLTHMLA DVTAMLGMVM RLSHIADEGR MDDAHAALAK VHTAARCREV
     VARAREVFGG NGILLEHGVA KHFCDTEAIY SYEGTNEINT LVVGRAITGL SAFV
//
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