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P31073 (DYR_CITFR) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 66. 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
OrganismCitrobacter freundii
Taxonomic identifier546 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeCitrobacterCitrobacter freundii complex

Protein attributes

Sequence length159 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.

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 – 159159Dihydrofolate reductase
PRO_0000186386

Regions

Domain1 – 158158DHFR
Nucleotide binding13 – 197NADP By similarity
Nucleotide binding45 – 462NADP By similarity
Nucleotide binding63 – 642NADP By similarity
Nucleotide binding95 – 1028NADP By similarity

Sites

Binding site51Substrate; via carbonyl oxygen By similarity
Binding site71NADP; via amide nitrogen and carbonyl oxygen By similarity
Binding site271Substrate By similarity
Binding site521Substrate By similarity
Binding site571Substrate By similarity
Binding site761NADP; via carbonyl oxygen By similarity
Binding site1131Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
P31073 [UniParc].

Last modified July 1, 1993. Version 1.
Checksum: 3CE7D7688577DCEE

FASTA15918,028
        10         20         30         40         50         60 
MISLIAALAV DRVIGMENAM PWNLPADLAW FKRNTLNKPV VMGRHTWESI GRPLPGRKNI 

        70         80         90        100        110        120 
VISSKPGTDD RVQWVKSVDE AIAACGDEPE IMVIGGGRVY EQFLPKAQKL YLTHIDAEVE 

       130        140        150 
GDTHFPDYEP DDWESVFSEF HDADAQNSHS YCFEILERR 

« Hide

References

[1]"Temporal and topological clustering of diverged residues among enterobacterial dihydrofolate reductases."
Garvin L.D., Hardies S.C.
Mol. Biol. Evol. 8:654-668(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M26023 Genomic DNA. Translation: AAA23093.1.
PIRB39799.

3D structure databases

ProteinModelPortalP31073.
SMRP31073. Positions 1-159.
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 nameDYR_CITFR
AccessionPrimary (citable) accession number: P31073
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: October 16, 2013
This is version 66 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