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Q59397 (DYR9_ECOLX) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 63. 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 9

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

Protein attributes

Sequence length177 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 By similarity.

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 – 177177Dihydrofolate reductase type 9
PRO_0000186427

Regions

Domain3 – 167165DHFR

Sequences

Sequence LengthMass (Da)Tools
Q59397 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: F478DBA8E745ABD0

FASTA17719,879
        10         20         30         40         50         60 
MASLNMIVAV NKTGGIGFEN QIPWHEPEDL KHFKAVTMNS VLIMGRKTFA SLPKVLPGRL 

        70         80         90        100        110        120 
HVVVSKTVPP TQNTDQVVYV STYQIAVRTA SLLVDKPEYS QIFVIGGKSA YENLAAYVDK 

       130        140        150        160        170 
LYLTRVQLNT QQDTELDLSL FKSWKLVSEV PTITENKTKL IFQIWINPNP ISEEPTC 

« Hide

References

[1]"Appearance of a new trimethoprim resistance gene, dhfrIX, in Escherichia coli from swine."
Jansson C., Skoeld O.
Antimicrob. Agents Chemother. 35:1891-1899(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 3926.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X57730 Genomic DNA. Translation: CAA40897.1.
PIRA49788.

3D structure databases

ProteinModelPortalQ59397.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEQ59397.

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

Entry information

Entry nameDYR9_ECOLX
AccessionPrimary (citable) accession number: Q59397
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: October 16, 2013
This is version 63 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