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 27-MAR-2024, entry version 125.
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; Pseudomonadota; 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; 99287-STM2186; -.
DR GeneID; 1253708; -.
DR KEGG; stm:STM2186; -.
DR PATRIC; fig|99287.12.peg.2313; -.
DR HOGENOM; CLU_000422_3_3_6; -.
DR OMA; QACVRNN; -.
DR PhylomeDB; Q8ZNL8; -.
DR BioCyc; SENT99287:STM2186-MONOMER; -.
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:0006208; P:pyrimidine nucleobase catabolic process; ISS:UniProtKB.
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; PR00368; FADPNR.
DR PRINTS; PR00469; PNDRDTASEII.
DR SUPFAM; SSF46548; alpha-helical ferredoxin; 1.
DR SUPFAM; SSF51971; Nucleotide-binding domain; 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
//
