PREA_ECO57
ID PREA_ECO57 Reviewed; 413 AA.
AC Q8X643; Q7AC92;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 130.
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=Z3402, ECs3039;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(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; AE005174; AAG57285.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB36462.1; -; Genomic_DNA.
DR PIR; A85853; A85853.
DR PIR; B64983; B64983.
DR PIR; G91008; G91008.
DR RefSeq; NP_311066.2; NC_002695.1.
DR AlphaFoldDB; Q8X643; -.
DR SMR; Q8X643; -.
DR STRING; 155864.EDL933_3308; -.
DR EnsemblBacteria; AAG57285; AAG57285; Z3402.
DR EnsemblBacteria; BAB36462; BAB36462; ECs_3039.
DR GeneID; 916743; -.
DR KEGG; ece:Z3402; -.
DR KEGG; ecs:ECs_3039; -.
DR PATRIC; fig|386585.9.peg.3164; -.
DR eggNOG; COG0167; Bacteria.
DR eggNOG; COG1146; Bacteria.
DR HOGENOM; CLU_042042_4_2_6; -.
DR OMA; MVPCVEE; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003954; F:NADH dehydrogenase activity; ISS:UniProtKB.
DR GO; GO:0006208; P:pyrimidine nucleobase catabolic process; ISS:UniProtKB.
DR GO; GO:0006210; P:thymine catabolic process; IEA:InterPro.
DR GO; GO:0006212; P:uracil catabolic process; IEA:InterPro.
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..413
FT /note="NAD-dependent dihydropyrimidine dehydrogenase
FT subunit PreA"
FT /id="PRO_0000409466"
FT DOMAIN 337..369
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 371..400
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT ACT_SITE 139
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 78
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 136..138
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 203..204
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 346
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 349
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 352
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 356
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 380
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 383
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 386
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 390
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
SQ SEQUENCE 413 AA; 45313 MW; 108F48E599CC1146 CRC64;
MLMLTKDLSI TFCGVKFPNP FCLSSSPVGN CYEMCAKAYD TGWGGVVFKT IGFFIANEVS
PRFDHLVKED TGFIGFKNME QIAEHPLEEN LAALRRLKED YPDKVLIASI MGENEQQWEE
LARLVQEAGA DMIECNFSCP QMTSHAMGSD VGQSPELVEK YCRAVKRGST LPMLAKMTPN
IGDMCEVALA AKRGGADGIA AINTVKSITN IDLNQKIGMP IVNGKSSISG YSGKAVKPIA
LRFIQQMRTH PELRDFPISG IGGIETWEDA AEFLLLGAAT LQVTTGIMQY GYRIVEDMAS
GLSHYLADQG FDSLQEMVGL ANNNIVPAED LDRSYIVYPR INLDKCVGCG RCYISCYDGG
HQAMEWSEKT RTPHCNTEKC VGCLLCGHVC PVGCIELGEV KFKKGEKEHP VTL
