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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 IncW R3880 Publication
OrganismiEscherichia coli
Taxonomic identifieri562 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 7878Dihydrofolate reductase type 2PRO_0000186436Add
BLAST

Interactioni

Subunit structurei

Homotetramer.By similarity

Structurei

3D structure databases

ProteinModelPortaliP00384.
SMRiP00384. 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.

P00384-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGQSSDEANA PVAGQFALPL SATFGLGDRV RKKSGAAWQG QVVGWYCTKL
60 70
TPEGYAVESE SHPGSVQIYP VAALERVA
Length:78
Mass (Da):8,195
Last modified:July 21, 1986 - v1
Checksum:iEE9B686CBE5BCB93
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V00252 Genomic DNA. Translation: CAA23503.1.
J01773 Genomic DNA. Translation: AAA72145.1.
PIRiA00398. RDECD8.
RefSeqiWP_015060228.1. NG_035487.1.
YP_009077104.1. NG_035487.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V00252 Genomic DNA. Translation: CAA23503.1.
J01773 Genomic DNA. Translation: AAA72145.1.
PIRiA00398. RDECD8.
RefSeqiWP_015060228.1. NG_035487.1.
YP_009077104.1. NG_035487.1.

3D structure databases

ProteinModelPortaliP00384.
SMRiP00384. 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. "Characterization of a R plasmid-associated, trimethoprim-resistant dihydrofolate reductase and determination of the nucleotide sequence of the reductase gene."
    Zolg J.W., Haenggi U.J.
    Nucleic Acids Res. 9:697-710(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "DNA sequence of a plasmid-encoded dihydrofolate reductase."
    Swift G., McCarthy B.J., Heffron F.
    Mol. Gen. Genet. 181:441-447(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Entry informationi

Entry nameiDYR22_ECOLX
AccessioniPrimary (citable) accession number: P00384
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: February 4, 2015
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

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.