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P11731 (DYR5_ECOLX) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 73. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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 5

EC=1.5.1.3
Alternative name(s):
Dihydrofolate reductase type V
Gene names
Name:dhfrV
Encoded onPlasmid pLMO20
OrganismEscherichia coli
Taxonomic identifier562 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length157 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

Homodimer.

Miscellaneous

Confers trimethoprim resistance.

Sequence similarities

Belongs to the dihydrofolate reductase family.

Contains 1 DHFR (dihydrofolate reductase) domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 157157Dihydrofolate reductase type 5
PRO_0000186422

Regions

Domain2 – 156155DHFR

Sequences

Sequence LengthMass (Da)Tools
P11731 [UniParc].

Last modified October 1, 1989. Version 1.
Checksum: 04B968163A25EFF4

FASTA15717,531
        10         20         30         40         50         60 
MKVSLMAAKA KNGVIGCGPH IPWSAKGEQL LFKALTYNQW LLVGRKTFES MGALPNRKYA 

        70         80         90        100        110        120 
VVTRSAWTAD NDNVIVFPSI EEAMYGLAEL TDHVIVSGGG EIYRETLPMA STLHISTIDI 

       130        140        150 
EPEGDVFFPN IPNTFEVVFE QHFSSNINYC YQIWQKG 

« Hide

References

[1]"Site-specific recombination promotes linkage between trimethoprim- and sulfonamide resistance genes. Sequence characterization of dhfrV and sulI and a recombination active locus of Tn21."
Sundstroem L., Radstroem P., Swedberg G., Skoeld O.
Mol. Gen. Genet. 213:191-201(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X12868 Genomic DNA. Translation: CAA31356.1.
PIRS04810.
RefSeqYP_008864016.1. NC_022992.1.
YP_008864683.1. NC_022996.1.

3D structure databases

ProteinModelPortalP11731.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID17824297.
17824432.

Enzyme and pathway databases

UniPathwayUPA00077; UER00158.

Family and domain databases

Gene3D3.40.430.10. 1 hit.
InterProIPR012259. DHFR.
IPR024072. DHFR-like_dom.
IPR017925. DHFR_CS.
IPR001796. DHFR_dom.
[Graphical view]
PfamPF00186. DHFR_1. 1 hit.
[Graphical view]
PRINTSPR00070. DHFR.
SUPFAMSSF53597. SSF53597. 1 hit.
PROSITEPS00075. DHFR_1. 1 hit.
PS51330. DHFR_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDYR5_ECOLX
AccessionPrimary (citable) accession number: P11731
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: March 19, 2014
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways