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Protein

Dihydrofolate reductase type 2

Gene
N/A
Organism
Escherichia coli
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

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

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei32 – 321NADPBy similarity
Binding sitei68 – 681Substrate; via amide nitrogenBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi66 – 694NADPBy similarity

GO - Molecular functioni

  1. dihydrofolate reductase activity Source: UniProtKB-EC

GO - Biological processi

  1. one-carbon metabolic process Source: UniProtKB-KW
  2. response to antibiotic Source: UniProtKB-KW
  3. response to drug Source: InterPro
  4. response to methotrexate Source: UniProtKB-KW
  5. tetrahydrofolate biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Antibiotic resistance, Methotrexate resistance, One-carbon metabolism, Trimethoprim resistance

Keywords - Ligandi

NADP

Enzyme and pathway databases

UniPathwayiUPA00077; UER00158.

Names & Taxonomyi

Protein namesi
Recommended name:
Dihydrofolate reductase type 2 (EC:1.5.1.3)
Alternative name(s):
Dihydrofolate reductase type II
Encoded oniPlasmid IncP-beta R7510 Publication
OrganismiEscherichia coli
Taxonomic identifieri562 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 7878Dihydrofolate reductase type 2PRO_0000186437Add
BLAST

Interactioni

Subunit structurei

Homotetramer.By similarity

Structurei

3D structure databases

ProteinModelPortaliP05794.
SMRiP05794. Positions 19-77.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domaini

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

Family and domain databases

InterProiIPR009159. Dhfr_type_II.
IPR008990. Elect_transpt_acc-like_dom.
[Graphical view]
PfamiPF06442. DHFR_2. 1 hit.
[Graphical view]
PIRSFiPIRSF000199. Dhfr_type_II. 1 hit.
SUPFAMiSSF50090. SSF50090. 1 hit.

Sequencei

Sequence statusi: Complete.

P05794-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDQHNNGVST LVAGQFALPS HATFGLGDRV RKKSGAAWQG QVVGWYCTKL
60 70
TPEGYAVESE SHPGSVQIYP VAALERVA
Length:78
Mass (Da):8,328
Last modified:November 1, 1988 - v1
Checksum:i3D67C2EB67220697
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04128 Genomic DNA. Translation: CAA27740.1.
X72585 Genomic DNA. Translation: CAA51181.1.
U67194 Genomic DNA. Translation: AAC64461.1.
PIRiA23598. RDECD5.
S32183.
RefSeqiYP_009073794.1. NG_034347.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04128 Genomic DNA. Translation: CAA27740.1.
X72585 Genomic DNA. Translation: CAA51181.1.
U67194 Genomic DNA. Translation: AAC64461.1.
PIRiA23598. RDECD5.
S32183.
RefSeqiYP_009073794.1. NG_034347.1.

3D structure databases

ProteinModelPortaliP05794.
SMRiP05794. Positions 19-77.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00077; UER00158.

Family and domain databases

InterProiIPR009159. Dhfr_type_II.
IPR008990. Elect_transpt_acc-like_dom.
[Graphical view]
PfamiPF06442. DHFR_2. 1 hit.
[Graphical view]
PIRSFiPIRSF000199. Dhfr_type_II. 1 hit.
SUPFAMiSSF50090. SSF50090. 1 hit.
ProtoNetiSearch...

Publicationsi

  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].

Entry informationi

Entry nameiDYR23_ECOLX
AccessioniPrimary (citable) accession number: P05794
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: November 1, 1988
Last modified: January 7, 2015
This is version 78 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

Plasmid

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.