PREA_SALTY
ID PREA_SALTY Reviewed; 411 AA.
AC Q8ZNL7;
DT 31-MAY-2011, 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 PreA;
DE Short=DPD;
DE EC=1.3.1.1;
DE AltName: Full=Dihydrothymine dehydrogenase;
DE AltName: Full=Dihydrouracil dehydrogenase;
GN Name=preA; Synonyms=yeiA; OrderedLocusNames=STM2187;
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 -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000305};
CC Note=Binds 2 [4Fe-4S] clusters. {ECO:0000305};
CC -!- SUBUNIT: Heterotetramer of 2 PreA and 2 PreT subunits. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the dihydropyrimidine dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; AE006468; AAL21091.1; -; Genomic_DNA.
DR RefSeq; NP_461132.1; NC_003197.2.
DR RefSeq; WP_000956095.1; NC_003197.2.
DR AlphaFoldDB; Q8ZNL7; -.
DR SMR; Q8ZNL7; -.
DR STRING; 99287.STM2187; -.
DR PaxDb; Q8ZNL7; -.
DR EnsemblBacteria; AAL21091; AAL21091; STM2187.
DR GeneID; 1253709; -.
DR KEGG; stm:STM2187; -.
DR PATRIC; fig|99287.12.peg.2314; -.
DR HOGENOM; CLU_042042_4_2_6; -.
DR OMA; MVPCVEE; -.
DR PhylomeDB; Q8ZNL7; -.
DR BioCyc; SENT99287:STM2187-MON; -.
DR BRENDA; 1.3.1.1; 5542.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0004159; F:dihydropyrimidine dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003954; F:NADH dehydrogenase activity; ISS:UniProtKB.
DR GO; GO:0050661; F:NADP binding; IBA:GO_Central.
DR GO; GO:0002058; F:uracil binding; IBA:GO_Central.
DR GO; GO:0006208; P:pyrimidine nucleobase catabolic process; ISS:UniProtKB.
DR GO; GO:0006210; P:thymine catabolic process; IBA:GO_Central.
DR GO; GO:0006212; P:uracil catabolic process; IBA:GO_Central.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR005720; Dihydroorotate_DH.
DR InterPro; IPR044512; DPYD.
DR PANTHER; PTHR43073; PTHR43073; 2.
DR Pfam; PF01180; DHO_dh; 1.
DR TIGRFAMs; TIGR01037; pyrD_sub1_fam; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
PE 3: Inferred from homology;
KW 4Fe-4S; Iron; Iron-sulfur; Metal-binding; NAD; Oxidoreductase;
KW Reference proteome; Repeat.
FT CHAIN 1..411
FT /note="NAD-dependent dihydropyrimidine dehydrogenase
FT subunit PreA"
FT /id="PRO_0000409467"
FT DOMAIN 335..367
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 369..398
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT ACT_SITE 137
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 76
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 134..136
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 201..202
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 344
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 347
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 350
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 354
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 378
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 381
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 384
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 388
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
SQ SEQUENCE 411 AA; 45079 MW; DC6052B38D305254 CRC64;
MLTKDLSVTF CGVKFPNPFC LSSSPVGNCY EMCAKAYDTG WGGIVFKTIG FFIANEVSPR
FDHLTKEDTG FIGFKNMEQI AEHPLEENLA AIRRLKQDYP DKVLIASIMG ENEQQWQELA
RLVEEAGADM IECNFSCPQM TSHAMGSDVG QSPELVEKYC RAVKRGSSLP MLAKMTPNIG
DMCEVALAAK RGGADGIATI NTVKSITNID LNRKIGMPVV NGKSSISGYS GKAVKPIALR
FIQQLRMHPE LRDFPISGIG GIETWEDAAE FLLLGAATLQ VTTGIMQYGY RIVEDMASGL
SHYLADQGFA SLQEMIGLAN GNIIPAEDLD RSYIVYPRIN QEKCVGCGRC YISCYDGGHQ
AMEWDEHSRT PHCNTEKCVG CLLCGHVCPV ACIDLGEVKF KKGEKEHALT L
