ID R7WNZ8_9NOCA Unreviewed; 550 AA.
AC R7WNZ8;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Putative FAD-binding dehydrogenase {ECO:0000313|EMBL:EOM77037.1};
GN ORFNames=Rrhod_1657 {ECO:0000313|EMBL:EOM77037.1};
OS Rhodococcus rhodnii LMG 5362.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=1273125 {ECO:0000313|EMBL:EOM77037.1, ECO:0000313|Proteomes:UP000013525};
RN [1] {ECO:0000313|EMBL:EOM77037.1, ECO:0000313|Proteomes:UP000013525}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 5362 {ECO:0000313|EMBL:EOM77037.1,
RC ECO:0000313|Proteomes:UP000013525};
RX PubMed=23788540;
RA Pachebat J.A., van Keulen G., Whitten M.M., Girdwood S., Del Sol R.,
RA Dyson P.J., Facey P.D.;
RT "Draft Genome Sequence of Rhodococcus rhodnii Strain LMG5362, a Symbiont of
RT Rhodnius prolixus (Hemiptera, Reduviidae, Triatominae), the Principle
RT Vector of Trypanosoma cruzi.";
RL Genome Announc. 1:e00329-13(2013).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EOM77037.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; APMY01000054; EOM77037.1; -; Genomic_DNA.
DR RefSeq; WP_010837720.1; NZ_APMY01000054.1.
DR AlphaFoldDB; R7WNZ8; -.
DR PATRIC; fig|1273125.3.peg.1599; -.
DR eggNOG; COG3573; Bacteria.
DR OrthoDB; 9813348at2; -.
DR Proteomes; UP000013525; Unassembled WGS sequence.
DR GO; GO:0033765; F:steroid dehydrogenase activity, acting on the CH-CH group of donors; IEA:UniProt.
DR GO; GO:0008152; P:metabolic process; IEA:UniProt.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR Gene3D; 3.90.700.10; Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain; 1.
DR InterPro; IPR003953; FAD-binding_2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR014614; KsdD_DH.
DR InterPro; IPR027477; Succ_DH/fumarate_Rdtase_cat_sf.
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:UP000013525}.
FT DOMAIN 5..532
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
SQ SEQUENCE 550 AA; 59576 MW; 58DB9F393204DED7 CRC64;
MTDADAIVVG AGLAGLVATY ELTKAGKKVL VVDQENEANL GGQAFWSLGG LFLVDSPEQR
RLGIKDSFDL AMADWLGTAG FDREREDHWP RRWAQAYVDF ASGEKRSYLH ELGLRLMPNV
GWAERGDGTA EGHGNSVPRF HITWGTGPGV VDVFRGPVLE AQARGLVRFA HRHRVDEIVV
TDGVATGVRG GVLAPSAEPR GVASSREVVG EFEFSAPAVV VTSGGIGGNH ELVRQNWPAR
LGEPPEQMLT GVPAHVDGRM LEITENAGGA IVNRDRMWHY TEGITNWDPI WPGHGIRIIP
GPSSMWFDAT GKRLPVPIFP GFDTMRTLSH IMTTGHRHTW FVLSQKIIEK EFALSGSEQN
PDLTGRDLAL LSQRLKKGAP GPVEAFKQHG ADFVVRDNLR DLVEGMNALT ETPLVDHDDL
ERQIVARDRQ VYNKYAKDFQ VMAIHNARGV FTEKLSRVAA PHAILDPANG PLIAVRLHLL
TRKTLGGLET DLESRVMRPD GSAFPGLYAA GEVAGFGGGG VHGYAALEGT FLGGCIFSGR
AAGRAAARSV
//
