ID   PRET_ECO57              Reviewed;         412 AA.
AC   Q8X645;
DT   16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=NAD-dependent dihydropyrimidine dehydrogenase subunit PreT;
DE            Short=DPD;
DE            EC=1.3.1.1;
DE   AltName: Full=Dihydrothymine dehydrogenase;
DE   AltName: Full=Dihydrouracil dehydrogenase;
GN   Name=preT; Synonyms=yeiT; OrderedLocusNames=Z3401, ECs3038;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA   Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA   Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA   Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA   Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA   Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA   Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA   Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT   genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
CC   -!- FUNCTION: Involved in pyrimidine base degradation. Catalyzes
CC       physiologically the reduction of uracil to 5,6-dihydrouracil (DHU) by
CC       using NADH as a specific cosubstrate. It also catalyzes the reverse
CC       reaction and the reduction of thymine to 5,6-dihydrothymine (DHT) (By
CC       similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5,6-dihydrouracil + NAD(+) = H(+) + NADH + uracil;
CC         Xref=Rhea:RHEA:20189, ChEBI:CHEBI:15378, ChEBI:CHEBI:15901,
CC         ChEBI:CHEBI:17568, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.3.1.1;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5,6-dihydrothymine + NAD(+) = H(+) + NADH + thymine;
CC         Xref=Rhea:RHEA:28791, ChEBI:CHEBI:15378, ChEBI:CHEBI:17821,
CC         ChEBI:CHEBI:27468, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.3.1.1;
CC   -!- SUBUNIT: Heterotetramer of 2 PreA and 2 PreT subunits. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the NADH dehydrogenase family. {ECO:0000305}.
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DR   EMBL; AE005174; AAG57284.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB36461.1; -; Genomic_DNA.
DR   PIR; F91008; F91008.
DR   PIR; H85852; H85852.
DR   RefSeq; NP_311065.1; NC_002695.1.
DR   RefSeq; WP_001136321.1; NZ_SWKA01000005.1.
DR   AlphaFoldDB; Q8X645; -.
DR   SMR; Q8X645; -.
DR   STRING; 155864.EDL933_3307; -.
DR   EnsemblBacteria; AAG57284; AAG57284; Z3401.
DR   EnsemblBacteria; BAB36461; BAB36461; ECs_3038.
DR   GeneID; 916742; -.
DR   KEGG; ece:Z3401; -.
DR   KEGG; ecs:ECs_3038; -.
DR   PATRIC; fig|386585.9.peg.3163; -.
DR   eggNOG; COG0493; Bacteria.
DR   HOGENOM; CLU_000422_3_3_6; -.
DR   OMA; ETKMGVR; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:0004159; F:dihydropyrimidine dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:InterPro.
DR   Gene3D; 1.10.1060.10; -; 1.
DR   Gene3D; 3.50.50.60; -; 2.
DR   InterPro; IPR028261; DPD_II.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR009051; Helical_ferredxn.
DR   Pfam; PF14691; Fer4_20; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
PE   3: Inferred from homology;
KW   NAD; Oxidoreductase; Reference proteome.
FT   CHAIN           1..412
FT                   /note="NAD-dependent dihydropyrimidine dehydrogenase
FT                   subunit PreT"
FT                   /id="PRO_0000169157"
FT   BINDING         286
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   412 AA;  44366 MW;  9D5A1916447DBC92 CRC64;
     MPQQNYLDEL TPAFTPLLAI KEASRCLLCH DAPCSQACPA QTDPGKFIRS IYFRNFKGAA
     ETIRENNALG AVCARVCPTE KLCQSGCTRA GVDAPIDIGR LQRFVTDFEQ QTGMEIYQPG
     TKTLGKVAII GAGPAGLQAS VTLTNQGYDV TIYEKEAHPG GWLRNGIPQF RLPQSVLDAE
     IARIEKMGVT IKCNNEIGKT LTLEQLKAEN RAVLVTVGLS SGSGLPLFEH SDVEIAVDFL
     LRARQAQGDI SIPQSALIIG GGDVAMDVAS TLKVLGCQAV TCVAREELDE FPASEKEFAS
     ARELGVSIID GFTPVAVEGN KVTFKHVRLS GELTMAADKI ILAVGQHARL DDFAKLEPQR
     NTIKTQNYQT RDPQVFAAGD IVEGDKTVVY AVKTGKEAAE AIHHYLEGAC SC