ID   A0A1M7AMN2_9RHOB        Unreviewed;       434 AA.
AC   A0A1M7AMN2;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=Dihydrothymine dehydrogenase {ECO:0000256|ARBA:ARBA00032722};
DE   AltName: Full=Dihydrouracil dehydrogenase {ECO:0000256|ARBA:ARBA00030119};
GN   ORFNames=SAMN05444414_11444 {ECO:0000313|EMBL:SHL44010.1};
OS   Roseovarius marisflavi.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Roseovarius.
OX   NCBI_TaxID=1054996 {ECO:0000313|EMBL:SHL44010.1, ECO:0000313|Proteomes:UP000184191};
RN   [1] {ECO:0000313|EMBL:SHL44010.1, ECO:0000313|Proteomes:UP000184191}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 29327 {ECO:0000313|EMBL:SHL44010.1,
RC   ECO:0000313|Proteomes:UP000184191};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-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; FRBN01000014; SHL44010.1; -; Genomic_DNA.
DR   RefSeq; WP_073198522.1; NZ_FRBN01000014.1.
DR   AlphaFoldDB; A0A1M7AMN2; -.
DR   STRING; 1054996.SAMN05444414_11444; -.
DR   OrthoDB; 9794954at2; -.
DR   Proteomes; UP000184191; 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}.
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;  46919 MW;  6AFE91B70FDDAD29 CRC64;
     MANLETTFIG IKSPNPFWLA SAPPTDKEYN VRRAFEAGWG GVVWKTLGEA GPPVVNVNGP
     RYGAIWGADR RLLGLNNIEL ITDRPLEVNL EEMKRVKRDW PDRALIASLM VPVNEDAWKD
     ILHRVEDTGC DGVELNFGCP HGMSERGMGS AVGQVPEYVG QVAHWCKKHS DLPVIVKLTP
     NITDIRKPAQ AAKEGGADAV SLINTINSIT SVDLDLFAPE PTIDGQGAHG GYCGPAVKPI
     ALNMVAEIAR DPATAGLPIS GIGGVTTWRD AAEFMALGAG NVQVCTAAMT YGFKVVQEMI
     SGLSQYMDEK GFTSTEQLIG RAVPNVVNWQ DLNLNYVAKA KINQQDCIKC GRCYAACEDT
     SHQAISMSED RVFEVKDDEC VACNLCVNVC PIEGCITMER MPTGAVDPRT GKVVQEDYAN
     WTTHPNNPGS CAAE
//