ID Q9RYS0_DEIRA Unreviewed; 554 AA.
AC Q9RYS0;
DT 01-MAY-2000, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2000, sequence version 1.
DT 08-NOV-2023, entry version 121.
DE RecName: Full=FAD-dependent oxidoreductase 2 FAD binding domain-containing protein {ECO:0000259|Pfam:PF00890};
GN OrderedLocusNames=DR_A0238 {ECO:0000313|EMBL:AAF12399.1};
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:AAF12399.1, ECO:0000313|Proteomes:UP000002524};
RN [1] {ECO:0000313|EMBL:AAF12399.1, 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).
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DR EMBL; AE001825; AAF12399.1; -; Genomic_DNA.
DR PIR; G75576; G75576.
DR RefSeq; NP_285561.1; NC_001264.1.
DR RefSeq; WP_010889497.1; NZ_JMLF01000014.1.
DR AlphaFoldDB; Q9RYS0; -.
DR STRING; 243230.DR_A0238; -.
DR PaxDb; 243230-DR_A0238; -.
DR EnsemblBacteria; AAF12399; AAF12399; DR_A0238.
DR GeneID; 69519132; -.
DR KEGG; dra:DR_A0238; -.
DR PATRIC; fig|243230.17.peg.3128; -.
DR eggNOG; COG3573; Bacteria.
DR HOGENOM; CLU_022946_0_0_0; -.
DR InParanoid; Q9RYS0; -.
DR OMA; PEDHWPR; -.
DR OrthoDB; 9813348at2; -.
DR Proteomes; UP000002524; Chromosome II.
DR GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR InterPro; IPR003953; FAD-binding_2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR014614; KsdD_DH.
DR PANTHER; PTHR43260; 3-KETOSTEROID-DELTA-1-DEHYDROGENASE; 1.
DR PANTHER; PTHR43260:SF1; KSDD-LIKE STEROID DEHYDROGENASE RV0785; 1.
DR Pfam; PF00890; FAD_binding_2; 1.
DR PIRSF; PIRSF036654; UCP036654; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 4: Predicted;
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000002524}.
FT DOMAIN 10..536
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
SQ SEQUENCE 554 AA; 60537 MW; 2FF988E0A2F2D7E9 CRC64;
METRKAEGEV IVVGAGLAGL VAAAELADAG RRVLILDQEG EQNLGGQAHW SFGGLFFVDS
PEQRRLGIRD SLDLARRDWE TAAGFDRPED HWPRKWAEAY LEFAAGEKRE WLHRQGMRWF
PAVGWAERGG AGAGLPGNSV PRFHITWGTG PGVLEPFVRR VREHQRAGRI EFRFRHRVRG
LTLTAGRVTG VHGDVLEPSD VGRGETSSRV VTGDFELTAQ AVLITSGGIG GNHELVRRYW
PTERLGPAPE VMLSGVPRHV DGLLQQQVVA QGGSLINPDR MWHYTEGVRN WDPVWPQHGI
RILPGPSSLW LDPSGRRLPF PHIPGASSYD TLRHITTHGY PHTWFLLNRA VIKREFGLSG
SEQNPDLTGK DLRLTLRRAS KHVPGPVQAF MDRGEDFVVR DNLRDLVRGM NELTGGELLD
YATVEREVLD RDLQVHNVAG KDAQLAIVRG ARAILSERLT RVAKPAPLLD PAQGPLIAVR
LSVLTRKSLG GLETDLQGRV IGAGGQPLPD LYAAGEVAGF GGGGYHGYRA LEGTFLGGCL
FSGRAAGRAI AGAL
//