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Reviewed, UniProtKB/Swiss-Prot P00384 (DYR22_ECOLX)

Last modified November 25, 2008. Version 53. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Dihydrofolate reductase type 2
    EC=1.5.1.3
Alternative name(s):
    Dihydrofolate reductase type II
Encoded onPlasmid IncW R388
OrganismEscherichia coli
Taxonomic identifier562 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length78 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existencePredicted.

General annotation (Comments)

Catalytic activity

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

Pathway

Cofactor biosynthesis; tetrahydrofolate biosynthesis; tetrahydrofolate from dihydrofolate: step 1/1.

Miscellaneous

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

The reaction catalyzed by this enzyme represents an essential step for de novo glycine and purine synthesis, DNA precursor synthesis, and for the conversion of dUMP to dTMP.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 7878Dihydrofolate reductase type 2
PRO_0000186436

Sequences

Sequence LengthMass (Da)Tools
P00384-1 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: EE9B686CBE5BCB93

FASTA788,195
        10         20         30         40         50         60 
MGQSSDEANA PVAGQFALPL SATFGLGDRV RKKSGAAWQG QVVGWYCTKL TPEGYAVESE 

        70 
SHPGSVQIYP VAALERVA 

« Hide

References

[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: 6261228] [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: 7022127] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

V00252 Genomic DNA. Translation: CAA23503.1.
J01773 Genomic DNA. Translation: AAA72145.1.
PIRRDECD8. A00398.

3D structure databases

HSSPHSSP built from PDB template 1VIE based on UniProtKB P00383.
SMRP00384. Positions 19-77.
ModBaseSearch...

Family and domain databases

InterProIPR009159. Dhfr_type_II.
[Graphical view]
PfamPF06442. DHFR_2. 1 hit.
[Graphical view]
PIRSFPIRSF000199. Dhfr_type_II. 1 hit.
ProtoNetSearch...

Entry information

Entry nameDYR22_ECOLX
AccessionPrimary (citable) accession number: P00384
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: November 25, 2008
This is version 53 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents