ID   PRET_SALTI              Reviewed;         413 AA.
AC   Q8Z5A6;
DT   16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 131.
DE   RecName: Full=NAD-dependent dihydropyrimidine dehydrogenase subunit PreT homolog;
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=STY2416, t0669;
OS   Salmonella typhi.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=90370;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CT18;
RX   PubMed=11677608; DOI=10.1038/35101607;
RA   Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA   Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA   Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA   Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA   Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA   Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA   Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA   Barrell B.G.;
RT   "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT   serovar Typhi CT18.";
RL   Nature 413:848-852(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700931 / Ty2;
RX   PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA   Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA   Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT   "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT   CT18.";
RL   J. Bacteriol. 185:2330-2337(2003).
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}.
CC   -!- CAUTION: Usually PreT interacts with PreA to form the active
CC       dehydrogenase. In S.typhi PreA is a pseudogene which does not possess
CC       the conserved 4Fe-4S ferredoxin-type domains. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AL513382; CAD02566.1; -; Genomic_DNA.
DR   EMBL; AE014613; AAO68367.1; -; Genomic_DNA.
DR   RefSeq; NP_456745.1; NC_003198.1.
DR   RefSeq; WP_001136400.1; NZ_WSUR01000002.1.
DR   AlphaFoldDB; Q8Z5A6; -.
DR   SMR; Q8Z5A6; -.
DR   STRING; 220341.16503426; -.
DR   EnsemblBacteria; AAO68367; AAO68367; t0669.
DR   KEGG; stt:t0669; -.
DR   KEGG; sty:STY2416; -.
DR   PATRIC; fig|220341.7.peg.2442; -.
DR   eggNOG; COG0493; Bacteria.
DR   HOGENOM; CLU_000422_3_3_6; -.
DR   OMA; ETKMGVR; -.
DR   Proteomes; UP000000541; Chromosome.
DR   Proteomes; UP000002670; 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: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.
FT   CHAIN           1..413
FT                   /note="NAD-dependent dihydropyrimidine dehydrogenase
FT                   subunit PreT homolog"
FT                   /id="PRO_0000169158"
FT   BINDING         287
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   413 AA;  44594 MW;  0BC796501BC3028E CRC64;
     MPQQNYLDEL TPGFTPLLAI KEASRCLLCH DAPCSQACPA QTDPGKFIRS IYFRNFKGAA
     ETIRENNALG AVCARVCPTE KLCQRGCTRS GIDKPIDIAR LQRFITDFEQ QTAMQIYQPG
     SKTRGKVAII GAGPAGLQAS VTLTHLGYDV TIYEKQPQPG GWLRHGIPAF RLPQSVLDQE
     IARIVEMGVN IKCNCDVGGS LSLAQLKAEY RAVLMTVGMS CGSDLPLFEQ ASHVEIAVDF
     LQRARQADGD ISVPRSALII GGGDVAMDVA STLKILGCPS VTCVAREELA EFPASEKEFT
     STQALGVSII DGFTPVAVSG NKVTFHHVRH SGELTLEAEN IILAVGQHAR LDNFAEIKAQ
     HNIIDTHNYQ TDDPAIFAAG DIVKGDKTVV YAVKTGKEAA QAIHHYLEEA CSC