NAD-dependent dihydropyrimidine dehydrogenase sunbunit PreT

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P76440 (PRET_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 107. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
NAD-dependent dihydropyrimidine dehydrogenase sunbunit PreT
Short name=DPD
EC=1.3.1.1

Alternative name(s):
Dihydrothymine dehydrogenase
Dihydrouracil dehydrogenase

Gene names

Name:	preT
Synonyms:	yeiT
Ordered Locus Names:	b2146, JW2133

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	412 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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). Ref.3 Ref.4
Catalytic activity	5,6-dihydrouracil + NAD⁺ = uracil + NADH. 5,6-dihydrothymine + NAD⁺ = thymine + NADH.
Subunit structure	Heterotetramer of 2 PreA and 2 PreT subunits. Ref.4
Induction	Transcriptionally regulated by IscS. Ref.3
Sequence similarities	Belongs to the NADH dehydrogenase family.
Biophysicochemical properties	Kinetic parameters: K_M=38 µM for uracil (at pH 6 and 30 degrees Celsius) Ref.4 K_M=87 µM for thymidine (at pH 6 and 30 degrees Celsius) K_M=130 µM for DHT (at pH 11 and 30 degrees Celsius) K_M=160 µM for DHU (at pH 11 and 30 degrees Celsius) V_max=0.18 µmol/min/mg enzyme toward DHT (at pH 11 and 30 degrees Celsius) V_max=0.26 µmol/min/mg enzyme toward thymidine (at pH 6 and 30 degrees Celsius) V_max=0.43 µmol/min/mg enzyme toward uracil (at pH 6 and 30 degrees Celsius) V_max=0.44 µmol/min/mg enzyme toward DHU (at pH 11 and 30 degrees Celsius)

Ontologies

Keywords
Ligand	NAD
Molecular function	Oxidoreductase
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	pyrimidine nucleobase catabolic process Inferred from direct assay Ref.4. Source: UniProtKB
Molecular_function	NADH dehydrogenase activity Inferred from direct assay Ref.4. Source: UniProtKB dihydrouracil dehydrogenase (NAD+) activity Inferred from electronic annotation. Source: EC flavin adenine dinucleotide binding Inferred from electronic annotation. Source: InterPro iron-sulfur cluster binding Inferred from direct assay Ref.3. Source: EcoCyc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 412

412

NAD-dependent dihydropyrimidine dehydrogenase sunbunit PreT

PRO_0000169156

Sites

Binding site

286

NAD Probable

Sequences

Sequence

Length

Mass (Da)

Tools

P76440 [UniParc].

Last modified February 1, 1997. Version 1.
Checksum: 6907F20BFAF7AF4E
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FASTA

412

44,329

        10         20         30         40         50         60 
MPQQNYLDEL TPAFTSLLAI KEASRCLLCH DAPCSQACPA QTDPGKFIRS IYFRNFKGAA 

        70         80         90        100        110        120 
ETIRENNALG AVCARVCPTE KLCQSGCTRA GVDAPIDIGR LQRFVTDFEQ QTGMEIYQPG 

       130        140        150        160        170        180 
TKTLGKVAII GAGPAGLQAS VTLTNQGYDV TIYEKEAHPG GWLRNGIPQF RLPQSVLDAE 

       190        200        210        220        230        240 
IARIEKMGVT IKCNNEVGNT LTLEQLKAEN RAVLVTVGLS SGSGLPLFEH SDVEIAVDFL 

       250        260        270        280        290        300 
QRARQAQGDI SIPQSALIIG GGDVAMDVAS TLKVLGCQAV TCVAREELDE FPASEKEFTS 

       310        320        330        340        350        360 
ARELGVSIID GFTPVAVEGN KVTFKHVRLS GELTMAADKI ILAVGQHARL DAFAELEPQR 

       370        380        390        400        410 
NTIKTQNYQT RDPQVFAAGD IVEGDKTVVY AVKTGKEAAE AIHHYLEGAC SC

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[2]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]	"The iscS gene deficiency affects the expression of pyrimidine metabolism genes." Mihara H., Hidese R., Yamane M., Kurihara T., Esaki N. Biochem. Biophys. Res. Commun. 372:407-411(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-15, FUNCTION IN PYRIMIDINE METABOLISM, INDUCTION, NAD.
[4]	"Escherichia coli dihydropyrimidine dehydrogenase is a novel NAD-dependent heterotetramer essential for the production of 5,6-dihydrouracil." Hidese R., Mihara H., Kurihara T., Esaki N. J. Bacteriol. 193:989-993(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION AS A DIHYDROPYRIMIDINE DEHYDROGENASE, BIOPHYSICOCHEMICAL PROPERTIES, NAD BINDING, SUBUNIT. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U00096 Genomic DNA. Translation: AAC75207.1. AP009048 Genomic DNA. Translation: BAE76623.1.
PIR	A64983.
RefSeq	NP_416651.1. NC_000913.2. YP_490385.1. NC_007779.1.
3D structure databases
ProteinModelPortal	P76440.
SMR	P76440. Positions 19-408.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-28055N.
IntAct	P76440. 5 interactions.
STRING	511145.b2146.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAC75207; AAC75207; b2146. BAE76623; BAE76623; BAE76623.
GeneID	12930175. 949049.
KEGG	ecj:Y75_p2108. eco:b2146.
PATRIC	32119635. VBIEscCol129921_2228.
Organism-specific databases
EchoBASE	EB3827.
EcoGene	EG14074. preT.
Phylogenomic databases
eggNOG	COG0493.
HOGENOM	HOG000031439.
OMA	SLKMTRE.
ProtClustDB	PRK11749.
Enzyme and pathway databases
BioCyc	EcoCyc:G7145-MONOMER. ECOL316407:JW2133-MONOMER. MetaCyc:G7145-MONOMER.
Gene expression databases
Genevestigator	P76440.
Family and domain databases
Gene3D	1.10.1060.10. 1 hit. 3.40.50.720. 1 hit.
InterPro	IPR012285. Fum_reductase_C. IPR009051. Helical_ferredxn. IPR016040. NAD(P)-bd_dom. IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD. IPR001327. Pyr_OxRdtase_NAD-bd_dom. [Graphical view]
Pfam	PF00070. Pyr_redox. 1 hit. PF07992. Pyr_redox_2. 1 hit. [Graphical view]
SUPFAM	SSF46548. Helical_ferredxn. 1 hit.
ProtoNet	Search...

Entry information

Entry name

PRET_ECOLI

Accession

Primary (citable) accession number: P76440
Secondary accession number(s): Q2MAT3

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 16, 2002
Last sequence update:	February 1, 1997
Last modified:	May 1, 2013
This is version 107 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents