ID S9RMY2_9RHOB Unreviewed; 447 AA.
AC S9RMY2;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE SubName: Full=Pyridine nucleotide-disulfide oxidoreductase associated with reductive pyrimidine catabolism {ECO:0000313|EMBL:EPX79460.1};
GN ORFNames=thalar_02285 {ECO:0000313|EMBL:EPX79460.1};
OS Litoreibacter arenae DSM 19593.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Litoreibacter.
OX NCBI_TaxID=1123360 {ECO:0000313|EMBL:EPX79460.1, ECO:0000313|Proteomes:UP000015351};
RN [1] {ECO:0000313|Proteomes:UP000015351}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19593 {ECO:0000313|Proteomes:UP000015351};
RX PubMed=24501650; DOI=10.4056/sigs.4258318;
RA Riedel T., Fiebig A., Petersen J., Gronow S., Kyrpides N.C., Goker M.,
RA Klenk H.P.;
RT "Genome sequence of the Litoreibacter arenae type strain (DSM 19593(T)), a
RT member of the Roseobacter clade isolated from sea sand.";
RL Stand. Genomic Sci. 9:117-127(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:EPX79460.1}.
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; AONI01000010; EPX79460.1; -; Genomic_DNA.
DR RefSeq; WP_021100840.1; NZ_KE557306.1.
DR AlphaFoldDB; S9RMY2; -.
DR STRING; 1123360.thalar_02285; -.
DR PATRIC; fig|1123360.3.peg.2263; -.
DR eggNOG; COG0493; Bacteria.
DR HOGENOM; CLU_000422_3_3_5; -.
DR OrthoDB; 9803192at2; -.
DR Proteomes; UP000015351; Unassembled WGS sequence.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR Gene3D; 1.10.1060.10; Alpha-helical ferredoxin; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR InterPro; IPR028261; DPD_II.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR009051; Helical_ferredxn.
DR PANTHER; PTHR43073; DIHYDROPYRIMIDINE DEHYDROGENASE [NADP(+)]; 1.
DR PANTHER; PTHR43073:SF2; DIHYDROPYRIMIDINE DEHYDROGENASE [NADP(+)]; 1.
DR Pfam; PF14691; Fer4_20; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR PRINTS; PR00419; ADXRDTASE.
DR SUPFAM; SSF46548; alpha-helical ferredoxin; 1.
DR SUPFAM; SSF51971; Nucleotide-binding domain; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000015351}.
FT DOMAIN 23..132
FT /note="Dihydroprymidine dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF14691"
FT DOMAIN 145..432
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
SQ SEQUENCE 447 AA; 46784 MW; 83A90D1BC32D3F3D CRC64;
MPEATPLTPG ITSGRLSAET LSEHFDDLHE PYAPHEAAVA ADRCYFCHDA PCITACPTDI
DIPLFIRQIQ TGTPEAAAKT ILTQNILGGM CARVCPTETL CEEACVREAA EGKPVEIGRL
QRYATDTLME KGVHPFTRAR STGKSVAVVG AGPAGLACAH RLAMHGHDVV LFDARAKAGG
LNEFGIAAYK STDNFAAREV DWLLGIGGIT LHLDQRLGDG LSLSELRDEY DAVFLGIGLA
GVNALRASGE DKDGVSDAVS FIAELRQASD LTKLPVGRDI VVIGGGMTAV DAAVQSKLLG
AQNVTIAYRR GLDQMGASKF EQDLAASKGV RIIANAQPLA VHGNGAVSEV EFEYTISDGG
ELTGTGETFR LKADQVFKAI GQTLDGAPDA LKLDGRKIAV DEKGRTSEAK VWAGGDCASG
GDDLTVTAVA EGRDAAEDIH ATLTGGK
//