ID   PRET_ECOLI              Reviewed;         412 AA.
AC   P76440; Q2MAT3;
DT   16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   27-MAR-2024, entry version 169.
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=b2146, JW2133;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [3]
RP   PROTEIN SEQUENCE OF 1-15, FUNCTION IN PYRIMIDINE METABOLISM, INDUCTION, AND
RP   NAD.
RX   PubMed=18482579; DOI=10.1016/j.bbrc.2008.05.019;
RA   Mihara H., Hidese R., Yamane M., Kurihara T., Esaki N.;
RT   "The iscS gene deficiency affects the expression of pyrimidine metabolism
RT   genes.";
RL   Biochem. Biophys. Res. Commun. 372:407-411(2008).
RN   [4]
RP   FUNCTION AS A DIHYDROPYRIMIDINE DEHYDROGENASE, BIOPHYSICOCHEMICAL
RP   PROPERTIES, NAD BINDING, AND SUBUNIT.
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=21169495; DOI=10.1128/jb.01178-10;
RA   Hidese R., Mihara H., Kurihara T., Esaki N.;
RT   "Escherichia coli dihydropyrimidine dehydrogenase is a novel NAD-dependent
RT   heterotetramer essential for the production of 5,6-dihydrouracil.";
RL   J. Bacteriol. 193:989-993(2011).
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).
CC       {ECO:0000269|PubMed:18482579, ECO:0000269|PubMed:21169495}.
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   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=38 uM for uracil (at pH 6 and 30 degrees Celsius)
CC         {ECO:0000269|PubMed:21169495};
CC         KM=87 uM for thymidine (at pH 6 and 30 degrees Celsius)
CC         {ECO:0000269|PubMed:21169495};
CC         KM=130 uM for DHT (at pH 11 and 30 degrees Celsius)
CC         {ECO:0000269|PubMed:21169495};
CC         KM=160 uM for DHU (at pH 11 and 30 degrees Celsius)
CC         {ECO:0000269|PubMed:21169495};
CC         Vmax=0.18 umol/min/mg enzyme toward DHT (at pH 11 and 30 degrees
CC         Celsius) {ECO:0000269|PubMed:21169495};
CC         Vmax=0.26 umol/min/mg enzyme toward thymidine (at pH 6 and 30 degrees
CC         Celsius) {ECO:0000269|PubMed:21169495};
CC         Vmax=0.43 umol/min/mg enzyme toward uracil (at pH 6 and 30 degrees
CC         Celsius) {ECO:0000269|PubMed:21169495};
CC         Vmax=0.44 umol/min/mg enzyme toward DHU (at pH 11 and 30 degrees
CC         Celsius) {ECO:0000269|PubMed:21169495};
CC   -!- SUBUNIT: Heterotetramer of 2 PreA and 2 PreT subunits.
CC       {ECO:0000269|PubMed:21169495}.
CC   -!- INDUCTION: Transcriptionally regulated by IscS.
CC       {ECO:0000269|PubMed:18482579}.
CC   -!- SIMILARITY: Belongs to the NADH dehydrogenase family. {ECO:0000305}.
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DR   EMBL; U00096; AAC75207.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE76623.1; -; Genomic_DNA.
DR   PIR; A64983; A64983.
DR   RefSeq; NP_416651.1; NC_000913.3.
DR   RefSeq; WP_001136389.1; NZ_LN832404.1.
DR   AlphaFoldDB; P76440; -.
DR   SMR; P76440; -.
DR   BioGRID; 4259169; 9.
DR   ComplexPortal; CPX-5561; NAD-dependent dihydropyrimidine dehydrogenase complex.
DR   DIP; DIP-28055N; -.
DR   IntAct; P76440; 5.
DR   STRING; 511145.b2146; -.
DR   jPOST; P76440; -.
DR   PaxDb; 511145-b2146; -.
DR   EnsemblBacteria; AAC75207; AAC75207; b2146.
DR   GeneID; 949049; -.
DR   KEGG; ecj:JW2133; -.
DR   KEGG; eco:b2146; -.
DR   PATRIC; fig|1411691.4.peg.96; -.
DR   EchoBASE; EB3827; -.
DR   eggNOG; COG0493; Bacteria.
DR   HOGENOM; CLU_000422_3_3_6; -.
DR   InParanoid; P76440; -.
DR   OMA; QACVRNN; -.
DR   OrthoDB; 9803192at2; -.
DR   PhylomeDB; P76440; -.
DR   BioCyc; EcoCyc:G7145-MONOMER; -.
DR   BioCyc; MetaCyc:G7145-MONOMER; -.
DR   SABIO-RK; P76440; -.
DR   PRO; PR:P76440; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0140690; C:dihydropyrimidine dehydrogenase (NAD+) complex; IDA:EcoCyc.
DR   GO; GO:1990204; C:oxidoreductase complex; IDA:ComplexPortal.
DR   GO; GO:0004159; F:dihydropyrimidine dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IDA:EcoCyc.
DR   GO; GO:0003954; F:NADH dehydrogenase activity; IDA:UniProtKB.
DR   GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR   GO; GO:0006208; P:pyrimidine nucleobase catabolic process; IDA:UniProtKB.
DR   GO; GO:0006210; P:thymine catabolic process; IDA:ComplexPortal.
DR   GO; GO:0006212; P:uracil catabolic process; IDA:ComplexPortal.
DR   Gene3D; 1.10.1060.10; Alpha-helical ferredoxin; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 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   PANTHER; PTHR43073; DIHYDROPYRIMIDINE DEHYDROGENASE [NADP(+)]; 1.
DR   PANTHER; PTHR43073:SF2; DIHYDROPYRIMIDINE DEHYDROGENASE [NADP(+)]; 1.
DR   Pfam; PF14691; Fer4_20; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   PRINTS; PR00419; ADXRDTASE.
DR   SUPFAM; SSF46548; alpha-helical ferredoxin; 1.
DR   SUPFAM; SSF51971; Nucleotide-binding domain; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; NAD; Oxidoreductase; Reference proteome.
FT   CHAIN           1..412
FT                   /note="NAD-dependent dihydropyrimidine dehydrogenase
FT                   subunit PreT"
FT                   /id="PRO_0000169156"
FT   BINDING         286
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   412 AA;  44329 MW;  6907F20BFAF7AF4E CRC64;
     MPQQNYLDEL TPAFTSLLAI KEASRCLLCH DAPCSQACPA QTDPGKFIRS IYFRNFKGAA
     ETIRENNALG AVCARVCPTE KLCQSGCTRA GVDAPIDIGR LQRFVTDFEQ QTGMEIYQPG
     TKTLGKVAII GAGPAGLQAS VTLTNQGYDV TIYEKEAHPG GWLRNGIPQF RLPQSVLDAE
     IARIEKMGVT IKCNNEVGNT LTLEQLKAEN RAVLVTVGLS SGSGLPLFEH SDVEIAVDFL
     QRARQAQGDI SIPQSALIIG GGDVAMDVAS TLKVLGCQAV TCVAREELDE FPASEKEFTS
     ARELGVSIID GFTPVAVEGN KVTFKHVRLS GELTMAADKI ILAVGQHARL DAFAELEPQR
     NTIKTQNYQT RDPQVFAAGD IVEGDKTVVY AVKTGKEAAE AIHHYLEGAC SC
//