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Reviewed, UniProtKB/Swiss-Prot Q04515 (DYR10_ECOLX)

Last modified June 16, 2009. Version 56. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Dihydrofolate reductase type A10
    EC=1.5.1.3
Alternative name(s):
    Dihydrofolate reductase type X
      Short name=DHFRX
Gene names
Name: dfrA10
Synonyms: dfr10
Encoded onPlasmid pDGO100
OrganismEscherichia coli
Taxonomic identifier562 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length187 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Function

Confers trimethoprim resistance.

Catalytic activity

5,6,7,8-tetrahydrofolate + NADP+ = 7,8-dihydrofolate + NADPH.

Pathway

Cofactor biosynthesis; tetrahydrofolate biosynthesis; tetrahydrofolate from dihydrofolate: step 1/1.

Subunit structure

Homodimer By similarity.

Miscellaneous

The reaction catalyzed by this enzyme represents an essential step for de novo glycine and purine synthesis, DNA precursor synthesis, and for the conversion of dUMP to dTMP.

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 – 187187Dihydrofolate reductase type A10
PRO_0000186428

Regions

Domain2 – 174173DHFR

Sequences

Sequence LengthMass (Da)Tools
Q04515-1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: D3E8D81B7AC6E571

FASTA18721,220
        10         20         30         40         50         60 
MNISLIFANE LITRAFGNQG KLPWQFIKED MQFFQKTTEN SVVVMGLNTW RSLPKMKKLG 

        70         80         90        100        110        120 
RDFIVISSTI TEHEVLNNNI QIFKSFESFL EAFRDTTKPI NVIGGVGLLS EAIEHASTVY 

       130        140        150        160        170        180 
MSSIHMVKPV HADVYVPVEL MNKLYSDFKY PENILWVGDP IDSVYSLSID KFVRPASLVG 


VPNDINT 

« Hide

References

[1]"A new trimethoprim resistance gene, dhfrX, in the In7 integron of plasmid pDGO100."
Parsons Y., Hall R.M., Stokes H.W.
Antimicrob. Agents Chemother. 35:2436-2439(1991) [PubMed: 1804022] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: VA292.
[2]"The partial 3'-conserved segment duplications in the integrons In6 from pSa and In7 from pDGO100 have a common origin."
Stokes H.W., Tomaras C., Parsons Y., Hall R.M.
Plasmid 30:39-50(1993) [PubMed: 8378445] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"In34, a complex In5 family class 1 integron containing orf513 and dfrA10."
Partridge S.R., Hall R.M.
Antimicrob. Agents Chemother. 47:342-349(2003) [PubMed: 12499211] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

L06418 Genomic DNA. Translation: AAA92749.1.
PIRA49790.

3D structure databases

HSSPHSSP built from PDB template 1DYR based on UniProtKB P16184.
ModBaseSearch...

Enzyme and pathway databases

BRENDA1.5.1.3. 246.

Family and domain databases

InterProIPR012259. DHFR.
IPR001796. DHFR_reg.
IPR017925. Dihydrofolate_reductase_CS.
[Graphical view]
PANTHERPTHR11549:SF1. DHFR. 1 hit.
PfamPF00186. DHFR_1. 1 hit.
[Graphical view]
PRINTSPR00070. DHFR.
PROSITEPS00075. DHFR_1. 1 hit.
PS51330. DHFR_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDYR10_ECOLX
AccessionPrimary (citable) accession number: Q04515
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: June 16, 2009
This is version 56 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents