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
//