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P04174 (DYR_NEIGO) Reviewed, UniProtKB/Swiss-Prot

Last modified December 11, 2013. Version 71. 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

EC=1.5.1.3
Gene names
Name:folA
OrganismNeisseria gonorrhoeae
Taxonomic identifier485 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeNeisseria

Protein attributes

Sequence length162 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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.

Miscellaneous

Strain T47/F62 is trimethoprim resistant by overproduction of DHFR.

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 – 162162Dihydrofolate reductase
PRO_0000186401

Regions

Domain3 – 161159DHFR
Nucleotide binding8 – 92NADP By similarity
Nucleotide binding16 – 216NADP By similarity
Nucleotide binding45 – 484NADP By similarity
Nucleotide binding65 – 684NADP By similarity
Nucleotide binding98 – 1036NADP By similarity
Region7 – 93Substrate binding By similarity

Sites

Binding site291Substrate By similarity
Binding site601Substrate By similarity
Binding site1171Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
P04174 [UniParc].

Last modified March 20, 1987. Version 1.
Checksum: A23BA94E6764E564

FASTA16217,731
        10         20         30         40         50         60 
MLKITIIAAC AENLCIGAGN AMPWHIPEDF AFFKVYTLGK PVIMGRKTWE SLPVKPLPGR 

        70         80         90        100        110        120 
RNIVISRQAD YCAAGAETVA SLEVALALCA GAEEAVIMGG AQIYGQAMPL ATDLRITEVD 

       130        140        150        160 
LSVEGDAFFP EIDRTHWREA ERTERRVSSK GVAYTFVHYL GK 

« Hide

References

[1]"Characterization and amino acid sequence of Neisseria gonorrhoeae dihydrofolate reductase."
Baccanari D.P., Tansik R.L., Paterson S.J., Stone D.
J. Biol. Chem. 259:12291-12298(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE.
Strain: T47/F62.

Cross-references

Sequence databases

PIRRDNHD. A00393.

3D structure databases

ProteinModelPortalP04174.
ModBaseSearch...
MobiDBSearch...

Chemistry

ChEMBLCHEMBL3565.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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]
PIRSFPIRSF000194. DHFR. 1 hit.
PRINTSPR00070. DHFR.
SUPFAMSSF53597. SSF53597. 1 hit.
PROSITEPS00075. DHFR_1. 1 hit.
PS51330. DHFR_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDYR_NEIGO
AccessionPrimary (citable) accession number: P04174
Entry history
Integrated into UniProtKB/Swiss-Prot: March 20, 1987
Last sequence update: March 20, 1987
Last modified: December 11, 2013
This is version 71 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