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P12833 (DYR3_SALTM) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 81. 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 3

EC=1.5.1.3
Alternative name(s):
Dihydrofolate reductase type III
Gene names
Name:dhfrIII
Encoded onPlasmid pAZ1
OrganismSalmonella typhimurium
Taxonomic identifier90371 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

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.

Subunit structure

Monomer.

Miscellaneous

The plasmid pAZ1 determines trimethoprim and sulphonamide 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 – 162162Dihydrofolate reductase type 3
PRO_0000186421

Regions

Domain2 – 160159DHFR

Experimental info

Sequence conflict81A → S AA sequence Ref.2

Sequences

Sequence LengthMass (Da)Tools
P12833 [UniParc].

Last modified October 1, 1989. Version 1.
Checksum: 199343AE8675FDED

FASTA16218,033
        10         20         30         40         50         60 
MLISLIAALA HNNLIGKDNL IPWHLPADLR HFKAVTLGKP VVMGRRTFES IGRPLPGRRN 

        70         80         90        100        110        120 
VVVSRNPQWQ AEGVEVAPSL DAALALLTDC EEAMIIGGGQ LYAEALPRAD RLYLTYIDAQ 

       130        140        150        160 
LNGDTHFPDY LSLGWQELER STHPADDKNS YACEFVTLSR QR 

« Hide

References

[1]"Characterization of plasmid pAZ1 and the type III dihydrofolate reductase gene."
Fling M.E., Kopf J., Richards C.
Plasmid 19:30-38(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Characterization of an R-plasmid dihydrofolate reductase with a monomeric structure."
Joyner S.S., Fling M.E., Stone D., Baccanari D.P.
J. Biol. Chem. 259:5851-5856(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-21.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J03306 Genomic DNA. Translation: AAA25550.1.
PIRB22241.
RDEBDT. JT0266.

3D structure databases

ProteinModelPortalP12833.
SMRP12833. Positions 2-161.
ModBaseSearch...
MobiDBSearch...

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 nameDYR3_SALTM
AccessionPrimary (citable) accession number: P12833
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: October 16, 2013
This is version 81 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