PRET_ECOLI
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 03-AUG-2022, entry version 161.
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; Proteobacteria; 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; P76440; -.
DR PRIDE; P76440; -.
DR EnsemblBacteria; AAC75207; AAC75207; b2146.
DR EnsemblBacteria; BAE76623; BAE76623; BAE76623.
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; ETKMGVR; -.
DR PhylomeDB; P76440; -.
DR BioCyc; EcoCyc:G7145-MON; -.
DR BioCyc; MetaCyc:G7145-MON; -.
DR SABIO-RK; P76440; -.
DR PRO; PR:P76440; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
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; -; 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 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
