Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

NAD-dependent dihydropyrimidine dehydrogenase subunit PreA

Gene

preA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Involved in pyrimidine base degradation. Catalyzes physiologically the reduction of uracil to 5,6-dihydrouracil (DHU) by using NADH as a specific cosubstrate. It also catalyzes the reverse reaction and the reduction of thymine to 5,6-dihydrothymine (DHT).2 Publications

Catalytic activityi

5,6-dihydrouracil + NAD+ = uracil + NADH.1 Publication
5,6-dihydrothymine + NAD+ = thymine + NADH.1 Publication

Cofactori

[4Fe-4S] clusterCuratedNote: Binds 2 [4Fe-4S] clusters.Curated

Kineticsi

  1. KM=38 µM for uracil (at pH 6 and 30 degrees Celsius)1 Publication
  2. KM=87 µM for thymidine (at pH 6 and 30 degrees Celsius)1 Publication
  3. KM=130 µM for DHT (at pH 11 and 30 degrees Celsius)1 Publication
  4. KM=160 µM for DHU (at pH 11 and 30 degrees Celsius)1 Publication
  1. Vmax=0.18 µmol/min/mg enzyme toward DHT (at pH 11 and 30 degrees Celsius)1 Publication
  2. Vmax=0.26 µmol/min/mg enzyme toward thymidine (at pH 6 and 30 degrees Celsius)1 Publication
  3. Vmax=0.43 µmol/min/mg enzyme toward uracil (at pH 6 and 30 degrees Celsius)1 Publication
  4. Vmax=0.44 µmol/min/mg enzyme toward DHU (at pH 11 and 30 degrees Celsius)1 Publication
  5. Vmax=0.67 µmol/min/mg enzyme toward fluorouracil (at pH 6 and 30 degrees Celsius)1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei76SubstrateBy similarity1
Active sitei137NucleophileBy similarity1
Metal bindingi344Iron-sulfur 1 (4Fe-4S)Sequence analysis1
Metal bindingi347Iron-sulfur 1 (4Fe-4S)Sequence analysis1
Metal bindingi350Iron-sulfur 1 (4Fe-4S)Sequence analysis1
Metal bindingi354Iron-sulfur 2 (4Fe-4S)Sequence analysis1
Metal bindingi378Iron-sulfur 2 (4Fe-4S)Sequence analysis1
Metal bindingi381Iron-sulfur 2 (4Fe-4S)Sequence analysis1
Metal bindingi384Iron-sulfur 2 (4Fe-4S)Sequence analysis1
Metal bindingi388Iron-sulfur 1 (4Fe-4S)Sequence analysis1

GO - Molecular functioni

  • 4 iron, 4 sulfur cluster binding Source: UniProtKB-KW
  • dihydrouracil dehydrogenase (NAD+) activity Source: UniProtKB-EC
  • iron-sulfur cluster binding Source: EcoCyc
  • metal ion binding Source: UniProtKB-KW
  • NADH dehydrogenase activity Source: UniProtKB

GO - Biological processi

  • pyrimidine nucleobase catabolic process Source: UniProtKB

Keywordsi

Molecular functionOxidoreductase
Ligand4Fe-4S, Iron, Iron-sulfur, Metal-binding, NAD

Enzyme and pathway databases

BioCyciEcoCyc:EG11289-MONOMER
MetaCyc:EG11289-MONOMER

Names & Taxonomyi

Protein namesi
Recommended name:
NAD-dependent dihydropyrimidine dehydrogenase subunit PreA (EC:1.3.1.1)
Short name:
DPD
Alternative name(s):
Dihydrothymine dehydrogenase
Dihydrouracil dehydrogenase
Gene namesi
Name:preA
Synonyms:yeiA
Ordered Locus Names:b2147, JW2134
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11289 preA

Subcellular locationi

GO - Cellular componenti

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001691481 – 411NAD-dependent dihydropyrimidine dehydrogenase subunit PreAAdd BLAST411

Proteomic databases

PaxDbiP25889
PRIDEiP25889

Expressioni

Inductioni

Transcriptionally regulated by IscS.1 Publication

Interactioni

Subunit structurei

Heterotetramer of 2 PreA and 2 PreT subunits.1 Publication

Protein-protein interaction databases

BioGridi4259170, 34 interactors
DIPiDIP-11915N
IntActiP25889, 2 interactors
STRINGi316385.ECDH10B_2304

Structurei

3D structure databases

ProteinModelPortaliP25889
SMRiP25889
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini335 – 3674Fe-4S ferredoxin-type 1PROSITE-ProRule annotationAdd BLAST33
Domaini369 – 3984Fe-4S ferredoxin-type 2PROSITE-ProRule annotationAdd BLAST30

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni134 – 136Substrate bindingBy similarity3
Regioni201 – 202Substrate bindingBy similarity2

Sequence similaritiesi

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG4107SJI Bacteria
COG0167 LUCA
COG1146 LUCA
HOGENOMiHOG000225106
InParanoidiP25889
KOiK17723
OMAiMVPCVEE
PhylomeDBiP25889

Family and domain databases

Gene3Di3.20.20.70, 1 hit
InterProiView protein in InterPro
IPR017896 4Fe4S_Fe-S-bd
IPR017900 4Fe4S_Fe_S_CS
IPR013785 Aldolase_TIM
IPR005720 Dihydroorotate_DH
PfamiView protein in Pfam
PF01180 DHO_dh, 1 hit
TIGRFAMsiTIGR01037 pyrD_sub1_fam, 1 hit
PROSITEiView protein in PROSITE
PS00198 4FE4S_FER_1, 1 hit
PS51379 4FE4S_FER_2, 2 hits

Sequencei

Sequence statusi: Complete.

P25889-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLTKDLSITF CGVKFPNPFC LSSSPVGNCY EMCAKAYDTG WGGVVFKTIG
60 70 80 90 100
FFIANEVSPR FDHLVKEDTG FIGFKNMEQI AEHPLEENLA ALRRLKEDYP
110 120 130 140 150
DKVLIASIMG ENEQQWEELA RLVQEAGADM IECNFSCPQM TSHAMGSDVG
160 170 180 190 200
QSPELVEKYC RAVKRGSTLP MLAKMTPNIG DMCEVALAAK RGGADGIAAI
210 220 230 240 250
NTVKSITNID LNQKIGMPIV NGKSSISGYS GKAVKPIALR FIQQMRTHPE
260 270 280 290 300
LRDFPISGIG GIETWEDAAE FLLLGAATLQ VTTGIMQYGY RIVEDMASGL
310 320 330 340 350
SHYLADQGFD SLQEMVGLAN NNIVPAEDLD RSYIVYPRIN LDKCVGCGRC
360 370 380 390 400
YISCYDGGHQ AMEWSEKTRT PHCNTEKCVG CLLCGHVCPV GCIELGEVKF
410
KKGEKEHPVT L
Length:411
Mass (Da):45,069
Last modified:July 15, 1998 - v3
Checksum:iF44F5F7BA8FAD23C
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti389 – 411PVGCI…HPVTL → RWVVLSSGK in M59444 (PubMed:1719366).CuratedAdd BLAST23

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA Translation: AAC75208.2
AP009048 Genomic DNA Translation: BAE76624.1
M59444 Genomic DNA No translation available.
RefSeqiNP_416652.4, NC_000913.3
WP_000956071.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaiAAC75208; AAC75208; b2147
BAE76624; BAE76624; BAE76624
GeneIDi949037
KEGGiecj:JW2134
eco:b2147
PATRICifig|1411691.4.peg.95

Similar proteinsi

Entry informationi

Entry nameiPREA_ECOLI
AccessioniPrimary (citable) accession number: P25889
Secondary accession number(s): P76441, Q2MAT2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: July 15, 1998
Last modified: March 28, 2018
This is version 145 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Cookie policy

We would like to use anonymized google analytics cookies to gather statistics on how uniprot.org is used in aggregate. Learn more

UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health