ID   A0A2A2DJM2_9PSED        Unreviewed;       424 AA.
AC   A0A2A2DJM2;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=Dihydrothymine dehydrogenase {ECO:0000256|ARBA:ARBA00032722};
DE   AltName: Full=Dihydrouracil dehydrogenase {ECO:0000256|ARBA:ARBA00030119};
GN   ORFNames=BZL43_25165 {ECO:0000313|EMBL:PAU52026.1};
OS   Pseudomonas sp. PICF141.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1949067 {ECO:0000313|EMBL:PAU52026.1, ECO:0000313|Proteomes:UP000217819};
RN   [1] {ECO:0000313|EMBL:PAU52026.1, ECO:0000313|Proteomes:UP000217819}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PICF141 {ECO:0000313|EMBL:PAU52026.1,
RC   ECO:0000313|Proteomes:UP000217819};
RA   Gomez-Lama C., Legarda-Cristobal G., Trivino J.C., Mercado-Blanco J.;
RT   "Genome sequences of Pseudomonas strains PIC25, PIC105 and PICF141
RT   indigenous of the olive (Olea europaea L.) cv. Picual rhizosphere and
RT   effective biological control agents against Verticillium dahliae.";
RL   Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
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:PAU52026.1}.
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DR   EMBL; MUNM01000085; PAU52026.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2A2DJM2; -.
DR   OrthoDB; 9794954at2; -.
DR   Proteomes; UP000217819; 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          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;  45963 MW;  AC12687E4034AAB0 CRC64;
     MADLSIVFAG IKAPNPFWLA SAPPTDKAYN VVRAFEAGWG GVVWKTLGED PAAVNVSSRY
     SAHFGANREV LGFNNIELIT DRSLEINLRE ITQVKKDWPD RALIVSLMVP CVEDSWKNIL
     PLVQATGADG IELNFGCPHG MPERGMGAAV GQVPEYVEQV TRWCKTYCSL PVIVKLTPNI
     TDIRVAARAA YRGGADAVSL INTINSITSV NLERMVANPV VGSQSTHGGY CGSAVKPIAL
     NMVAEIARDP QTQGLPISGI GGIGSWRDAA EFIALGSGSV QVCTAAMLHG FRIVEEMKDG
     LSRWMDSQGY ASVSEFSGRA VGNTTDWKYL DINYQVIAKI DQQACIGCGR CHIACEDTSH
     QAIASLKQAD GTHKYEVIDD ECVGCNLCQI TCPVQDCIEM VPMENGKPFL DWNHDPRNPY
     HTTV
//