ID   PRET_SALTY              Reviewed;         413 AA.
AC   Q8ZNL8;
DT   16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 117.
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=STM2186;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(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; AE006468; AAL21090.1; -; Genomic_DNA.
DR   RefSeq; NP_461131.1; NC_003197.2.
DR   RefSeq; WP_001136409.1; NC_003197.2.
DR   AlphaFoldDB; Q8ZNL8; -.
DR   SMR; Q8ZNL8; -.
DR   STRING; 99287.STM2186; -.
DR   PaxDb; Q8ZNL8; -.
DR   EnsemblBacteria; AAL21090; AAL21090; STM2186.
DR   GeneID; 1253708; -.
DR   KEGG; stm:STM2186; -.
DR   PATRIC; fig|99287.12.peg.2313; -.
DR   HOGENOM; CLU_000422_3_3_6; -.
DR   OMA; ETKMGVR; -.
DR   PhylomeDB; Q8ZNL8; -.
DR   BioCyc; SENT99287:STM2186-MON; -.
DR   Proteomes; UP000001014; 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   GO; GO:0003954; F:NADH dehydrogenase activity; ISS:UniProtKB.
DR   GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR   GO; GO:0006208; P:pyrimidine nucleobase catabolic process; ISS:UniProtKB.
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..413
FT                   /note="NAD-dependent dihydropyrimidine dehydrogenase
FT                   subunit PreT"
FT                   /id="PRO_0000169159"
FT   BINDING         287
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   413 AA;  44537 MW;  5CF22B2B18A8C13E CRC64;
     MPQQNYLDEL TPGFTPLLAI KEASRCLLCH DAPCSQACPA QTDPGKFIRS IYFRNFKGAA
     ETIRENNALG AVCARVCPTE KLCQRGCTRS GIDKPIDIAR LQRFITDFEQ QTAMQIYQPG
     SKTRGKVAII GAGPAGLQAS VTLTHLGYDV TIYEKQPQPG GWLRHGIPAF RLPQSVLDQE
     IARIVEMGVN IKCNCEVGGS LSLAQLKAEY RAVLMTVGMS CGSGLPLFEQ ASHVEIAVDF
     LQRARQADGD ISVPRSALII GGGDVAMDVA STLKILGCPS VTCVAREELA EFPASEKEFT
     STQALGVSII DGFTPVAVSG NKVTFHHVRH SGELTLEAEN IILAVGQHAR LDTFAEIKAQ
     HNIIDTHNYQ TDDPAIFAAG DIVKGDKTVV YAVKTGKEAA QAIHHYLEEA CSC