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Database: UniProt
Entry: V8R862_9PSED
LinkDB: V8R862_9PSED
Original site: V8R862_9PSED 
ID   V8R862_9PSED            Unreviewed;       424 AA.
AC   V8R862;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=Dihydrothymine dehydrogenase {ECO:0000256|ARBA:ARBA00032722};
DE   AltName: Full=Dihydrouracil dehydrogenase {ECO:0000256|ARBA:ARBA00030119};
GN   ORFNames=PMO01_15520 {ECO:0000313|EMBL:ETF07474.1};
OS   Pseudomonas moraviensis R28-S.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1395516 {ECO:0000313|EMBL:ETF07474.1};
RN   [1] {ECO:0000313|EMBL:ETF07474.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R28-S {ECO:0000313|EMBL:ETF07474.1};
RX   PubMed=24558233;
RA   Hunter S.S., Yano H., Loftie-Eaton W., Hughes J., De Gelder L.,
RA   Stragier P., De Vos P., Settles M.L., Top E.M.;
RT   "Draft Genome Sequence of Pseudomonas moraviensis R28-S.";
RL   Genome Announc. 2:e00035-14(2014).
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:ETF07474.1}.
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DR   EMBL; AYMZ01000006; ETF07474.1; -; Genomic_DNA.
DR   RefSeq; WP_016775132.1; NZ_CM002330.1.
DR   AlphaFoldDB; V8R862; -.
DR   PATRIC; fig|1395516.4.peg.3152; -.
DR   eggNOG; COG0167; Bacteria.
DR   eggNOG; COG1149; Bacteria.
DR   HOGENOM; CLU_042042_4_2_6; -.
DR   Proteomes; UP000024771; Chromosome.
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:ETF07474.1}.
FT   DOMAIN          336..365
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          373..403
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   424 AA;  45868 MW;  4337FCFDDBE230A2 CRC64;
     MADLSIVFAG IKAPNPFWLA SAPPTDKAYN VVRAFEAGWG GVVWKTLGED PAAVNVSSRY
     SAHYGANREV LGINNIELIT DRSLEINLRE ITQVKKDWPD RALIVSLMVP CVEESWKHIL
     PLVEATGADG IELNFGCPHG MPERGMGAAV GQVPEYVEQV TRWCKTYCSL PVIVKLTPNI
     TDIRVAARAA HRGGADAVSL INTINSITSV DLEHMVALPT VGSKSTHGGY CGSAVKPIAL
     NMVAEIARDP QTQGLPICGI GGIGSWRDAA EFMALGSGAV QVCTAAMLHG FRIVEEMKDG
     LSRWMDSQGY ANIAEFSGRA VGNTTDWKYL DINYQVIAKI DQEACIGCGR CHIACEDTSH
     QAIGSLKQAD GTHKYEVIDE ECVGCNLCQI TCPVADCIEM VPMDTGKPFL DWNHDPRNPY
     HVAV
//
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