ID   A0A1I5XA15_9RHOB        Unreviewed;       434 AA.
AC   A0A1I5XA15;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=Dihydrothymine dehydrogenase {ECO:0000256|ARBA:ARBA00032722};
DE   AltName: Full=Dihydrouracil dehydrogenase {ECO:0000256|ARBA:ARBA00030119};
GN   ORFNames=SAMN05421853_103252 {ECO:0000313|EMBL:SFQ28815.1};
OS   Roseivivax halotolerans.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Roseivivax.
OX   NCBI_TaxID=93684 {ECO:0000313|EMBL:SFQ28815.1, ECO:0000313|Proteomes:UP000243106};
RN   [1] {ECO:0000313|Proteomes:UP000243106}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 10271 {ECO:0000313|Proteomes:UP000243106};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the dihydropyrimidine dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00010804}.
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DR   EMBL; FOXV01000003; SFQ28815.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I5XA15; -.
DR   STRING; 93684.SAMN05421853_103252; -.
DR   Proteomes; UP000243106; 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   Reference proteome {ECO:0000313|Proteomes:UP000243106}.
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   434 AA;  46997 MW;  FC186AE6F81748EF CRC64;
     MADLTTDFVG IKSPNPFWLA SAPPTDKEYN VRRAFEAGWG GVVWKTLGAE GPPVVNVNGP
     RYGAIYGADR RLLGLNNIEL ITDRPLEVNL EEMARVKADY PDRALIASIM VPCEEAAWKA
     ILPRVAETGA DGIELNFGCP HGMSERGMGS AVGQVPEYIE MVTRWCKEYY DRPVIVKLTP
     NITDIRKPAE AARNGGADAV SLINTINSIT SVDLDQMCPQ PTIDGKGSHG GYCGPAVKPI
     ALSMVSEIAR AEATRGMPIS GIGGVTTWRD AAEFMALGCG NVQVCTAAMT YGFRIVEEMT
     RGLSAWMDEK GYTSTAEIVG RAVPNVTDWQ YLNLNYVTKA RIDQDACIQC GRCYAACEDT
     SHQAIAMKPG RVFEVVDEEC VACNLCVDVC PVEDCITMVE LEPGATDPRT GRVVESEYAN
     WTTHPNNPAA QAAE
//