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P05794 (DYR23_ECOLX) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Dihydrofolate reductase type 2

EC=1.5.1.3
Alternative name(s):
Dihydrofolate reductase type II
Encoded onPlasmid IncP-beta R751
OrganismEscherichia coli
Taxonomic identifier562 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length78 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis By similarity.

Catalytic activity

5,6,7,8-tetrahydrofolate + NADP+ = 7,8-dihydrofolate + NADPH.

Pathway

Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1.

Subunit structure

Homotetramer By similarity.

Domain

The active site is situated at the inner surface of a pore formed by the four subunits By similarity.

Miscellaneous

Type II plasmid-specified enzyme is practically insensitive to trimethoprim and methotrexate.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 7878Dihydrofolate reductase type 2
PRO_0000186437

Regions

Nucleotide binding66 – 694NADP By similarity

Sites

Binding site321NADP By similarity
Binding site681Substrate; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
P05794 [UniParc].

Last modified November 1, 1988. Version 1.
Checksum: 3D67C2EB67220697

FASTA788,328
        10         20         30         40         50         60 
MDQHNNGVST LVAGQFALPS HATFGLGDRV RKKSGAAWQG QVVGWYCTKL TPEGYAVESE 

        70 
SHPGSVQIYP VAALERVA 

« Hide

References

[1]"Nucleotide sequence analysis of the trimethoprim resistant dihydrofolate reductase encoded by R plasmid R751."
Flensburg J., Steen R.
Nucleic Acids Res. 14:5933-5933(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]Radstroem P., Sundstroem L., Swedberg G., Flensburg J., Skoeld O.
Submitted (MAR-1993) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]Thomas C.M.
Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X04128 Genomic DNA. Translation: CAA27740.1.
X72585 Genomic DNA. Translation: CAA51181.1.
U67194 Genomic DNA. Translation: AAC64461.1.
PIRRDECD5. A23598.
S32183.

3D structure databases

ProteinModelPortalP05794.
SMRP05794. Positions 19-77.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00077; UER00158.

Family and domain databases

InterProIPR009159. Dhfr_type_II.
IPR008990. Elect_transpt_acc-like_dom.
[Graphical view]
PfamPF06442. DHFR_2. 1 hit.
[Graphical view]
PIRSFPIRSF000199. Dhfr_type_II. 1 hit.
SUPFAMSSF50090. SSF50090. 1 hit.
ProtoNetSearch...

Entry information

Entry nameDYR23_ECOLX
AccessionPrimary (citable) accession number: P05794
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: November 1, 1988
Last modified: October 16, 2013
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways