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P05794

- DYR23_ECOLX

UniProt

P05794 - DYR23_ECOLX

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Protein

Dihydrofolate reductase type 2

Gene
N/A
Organism
Escherichia coli
Status
Reviewed - 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.

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei32 – 321NADP By similarity
Binding sitei68 – 681Substrate; via amide nitrogen By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi66 – 694NADP By 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.

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

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

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X04128 Genomic DNA. Translation: CAA27740.1.
X72585 Genomic DNA. Translation: CAA51181.1.
U67194 Genomic DNA. Translation: AAC64461.1.
PIRiA23598. RDECD5.
S32183.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X04128 Genomic DNA. Translation: CAA27740.1 .
X72585 Genomic DNA. Translation: CAA51181.1 .
U67194 Genomic DNA. Translation: AAC64461.1 .
PIRi A23598. RDECD5.
S32183.

3D structure databases

ProteinModelPortali P05794.
SMRi P05794. Positions 19-77.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00077 ; UER00158 .

Family and domain databases

InterProi IPR009159. Dhfr_type_II.
IPR008990. Elect_transpt_acc-like_dom.
[Graphical view ]
Pfami PF06442. DHFR_2. 1 hit.
[Graphical view ]
PIRSFi PIRSF000199. Dhfr_type_II. 1 hit.
SUPFAMi SSF50090. SSF50090. 1 hit.
ProtoNeti Search...

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: October 16, 2013
This is version 76 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

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