ID S9QP79_9RHOB Unreviewed; 433 AA.
AC S9QP79;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Dihydrothymine dehydrogenase {ECO:0000256|ARBA:ARBA00032722};
DE AltName: Full=Dihydrouracil dehydrogenase {ECO:0000256|ARBA:ARBA00030119};
GN ORFNames=ruthe_02876 {ECO:0000313|EMBL:EPX83251.1};
OS Rubellimicrobium thermophilum DSM 16684.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Rubellimicrobium.
OX NCBI_TaxID=1123069 {ECO:0000313|EMBL:EPX83251.1, ECO:0000313|Proteomes:UP000015346};
RN [1] {ECO:0000313|EMBL:EPX83251.1, ECO:0000313|Proteomes:UP000015346}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16684 {ECO:0000313|EMBL:EPX83251.1,
RC ECO:0000313|Proteomes:UP000015346};
RX PubMed=24501632; DOI=10.4056/sigs.4247911;
RA Fiebig A., Riedel T., Gronow S., Petersen J., Klenk H.P., Goker M.;
RT "Genome sequence of the reddish-pigmented Rubellimicrobium thermophilum
RT type strain (DSM 16684(T)), a member of the Roseobacter clade.";
RL Stand. Genomic Sci. 8:480-490(2013).
CC -!- SIMILARITY: Belongs to the dihydropyrimidine dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00010804}.
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:EPX83251.1}.
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DR EMBL; AOLV01000033; EPX83251.1; -; Genomic_DNA.
DR RefSeq; WP_021098940.1; NZ_KE557324.1.
DR AlphaFoldDB; S9QP79; -.
DR STRING; 1123069.ruthe_02876; -.
DR PATRIC; fig|1123069.3.peg.2847; -.
DR HOGENOM; CLU_042042_4_2_5; -.
DR OrthoDB; 9794954at2; -.
DR Proteomes; UP000015346; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
DR CDD; cd02940; DHPD_FMN; 1.
DR Gene3D; 3.30.70.20; -; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR005720; Dihydroorotate_DH_cat.
DR PANTHER; PTHR43073; DIHYDROPYRIMIDINE DEHYDROGENASE [NADP(+)]; 1.
DR PANTHER; PTHR43073:SF2; DIHYDROPYRIMIDINE DEHYDROGENASE [NADP(+)]; 1.
DR Pfam; PF01180; DHO_dh; 1.
DR Pfam; PF14697; Fer4_21; 1.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
PE 3: Inferred from homology;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:EPX83251.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000015346}.
FT DOMAIN 338..370
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 371..401
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 433 AA; 46835 MW; F4C440C0856FEA9F CRC64;
MASLATDFIG IRSPNPFWLA SAPPTDKEYN VRRAFQAGWG GVVWKTLGAE GPPVVNVNGP
RYGVIHGPDR RVMGLNNIEL ITDRPLEVNL REIKAVKRDF PDRALVVSLM VPCDEESWKA
ILARVEETDC DGVELNFGCP HGMSERGMGS AVGQVPEYIE MVTRWVKQHS RMPCIVKLTP
NITDIRKPAE AAKRGGADAV SLINTINSIT SVNLDTFSPE PSIDGKGAHG GYCGPAVKPI
ALNMVAEIAR NPATRDLPIS GIGGITTWRD AAEFLALGAG SVQVCTAAMT YGFGIIREMT
AGLSAWMDEK GFTAVDQIVG RAVPNVTDWQ YLNLNYVTKA RINQDLCIKC GRCYAACEDT
SHQAIAMGPG RVFTVKDEEC VACNLCVDVC PVENCITMVE LPKGSVDPRT GIVVGDYANW
TTHPNNPMAR AAE
//
