ID   W1WXE8_ECOLX            Unreviewed;       411 AA.
AC   W1WXE8;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=Dihydrothymine dehydrogenase {ECO:0000256|ARBA:ARBA00032722};
DE   AltName: Full=Dihydrouracil dehydrogenase {ECO:0000256|ARBA:ARBA00030119};
GN   ORFNames=Q609_ECAC01617G0019 {ECO:0000313|EMBL:ETJ22601.1};
OS   Escherichia coli DORA_A_5_14_21.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=1403943 {ECO:0000313|EMBL:ETJ22601.1, ECO:0000313|Proteomes:UP000018853};
RN   [1] {ECO:0000313|EMBL:ETJ22601.1, ECO:0000313|Proteomes:UP000018853}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DORA_A_5_14_21 {ECO:0000313|Proteomes:UP000018853};
RA   Brown C.T., Sharon I., Thomas B.C., Castelle C.J., Morowitz M.J.,
RA   Banfield J.F.;
RT   "A Varibaculum cambriense genome reconstructed from a premature infant gut
RT   community with otherwise low bacterial novelty that shifts toward anaerobic
RT   metabolism during the third week of life.";
RL   Submitted (DEC-2013) 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:ETJ22601.1}.
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DR   EMBL; AZLZ01001617; ETJ22601.1; -; Genomic_DNA.
DR   AlphaFoldDB; W1WXE8; -.
DR   PATRIC; fig|1403943.3.peg.3156; -.
DR   Proteomes; UP000018853; 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          335..367
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          369..398
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   411 AA;  45058 MW;  C79E8C7FBC7AA274 CRC64;
     MLTKDLSITF CGVKFPNPFC LSSSPVGNCY EMCAKAYDTG WGGVVFKTIG FFIANEVSPR
     FDHLVKEDTG FIGFKNMEQI AEHPLEENLA ALRRLKEDYP DKVLIASIMG ENEQQWEELA
     RLVQEAGADM IECNFSCPQM TSHAMGSDVG QSPELVEKYC RAVKRGSTLP MLAKMTPNIG
     DMCEVALAAK RGGADGIAAI NTVKSITNID LNQKIGMPIV NGKSSISGYS GKAVKPIALR
     FIQQMRTHPE LRNFPISGIG GIETWEDAAE FLLLGAATLQ VTTGIMQYGY RIVEDMASGL
     SHYLADQGFD SLQEMVGLAN HNIVPAEDLD RSYIVYPHIN LDKCVGCGRC YISCYDGGHQ
     AMEWSEKTRT PHCNTEKCVG CLLCGHVCPV GCIDLGEVKF KKGEKEHPVT L
//