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Protein

Dihydrofolate reductase type 1

Gene

dhfrI

Organism
Escherichia coli
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis (By similarity).By similarity

Catalytic activityi

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

Pathway:itetrahydrofolate biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate.
Proteins known to be involved in this subpathway in this organism are:
  1. Dihydrofolate reductase type 8 (dhfrVIII), Dihydrofolate reductase type 9 (dhfrIX), Dihydrofolate reductase (folA), Dihydrofolate reductase (dfrA26), Dihydrofolate reductase (dfrA12), Dihydrofolate reductase (dfrA12), Dihydrofolate reductase type A10 (dfrA10), Dihydrofolate reductase (dfrA21), Dihydrofolate reductase type A13 (dfrA13), Dihydrofolate reductase (ECs0051), Dihydrofolate reductase (folA), Dihydrofolate reductase type 2, Dihydrofolate reductase type 2, Dihydrofolate reductase type 2, Dihydrofolate reductase type 7 (dhfrVII), Dihydrofolate reductase type 1 (dhfrI), Dihydrofolate reductase (dfr22), Dihydrofolate reductase type 5 (dhfrV), Dihydrofolate reductase (dfrA12), Dihydrofolate reductase type 15 (dhfrXV), Dihydrofolate reductase (folA), Dihydrofolate reductase (dfrA12), Dihydrofolate reductase (dfrA12), Dihydrofolate reductase (dfrA12), Dihydrofolate reductase (dfr22), Dihydrofolate reductase (dfrA12)
This subpathway is part of the pathway tetrahydrofolate biosynthesis, which is itself part of Cofactor biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate, the pathway tetrahydrofolate biosynthesis and in Cofactor biosynthesis.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Antibiotic resistance, Methotrexate resistance, One-carbon metabolism, Trimethoprim resistance

Keywords - Ligandi

NADP

Enzyme and pathway databases

UniPathwayiUPA00077; UER00158.

Names & Taxonomyi

Protein namesi
Recommended name:
Dihydrofolate reductase type 1 (EC:1.5.1.3)
Alternative name(s):
Dihydrofolate reductase type I
Trimethoprim resistance protein
Gene namesi
Name:dhfrI
Encoded oniPlasmid IncI1 R4832 Publications
Plasmid pLMO1501 Publication
Plasmid pLMO2291 Publication
OrganismiEscherichia coli
Taxonomic identifieri562 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 157157Dihydrofolate reductase type 1PRO_0000186420Add
BLAST

Proteomic databases

PRIDEiP00382.

Interactioni

Subunit structurei

Homodimer.

Structurei

3D structure databases

ProteinModelPortaliP00382.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 156155DHFRPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the dihydrofolate reductase family.Curated
Contains 1 DHFR (dihydrofolate reductase) domain.PROSITE-ProRule annotation

Phylogenomic databases

KOiK18589.

Family and domain databases

Gene3Di3.40.430.10. 1 hit.
InterProiIPR012259. DHFR.
IPR024072. DHFR-like_dom.
IPR017925. DHFR_CS.
IPR001796. DHFR_dom.
[Graphical view]
PfamiPF00186. DHFR_1. 1 hit.
[Graphical view]
PRINTSiPR00070. DHFR.
SUPFAMiSSF53597. SSF53597. 1 hit.
PROSITEiPS00075. DHFR_1. 1 hit.
PS51330. DHFR_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P00382-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKLSLMVAIS KNGVIGNGPD IPWSAKGEQL LFKAITYNQW LLVGRKTFES
60 70 80 90 100
MGALPNRKYA VVTRSSFTSD NENVLIFPSI KDALTNLKKI TDHVIVSGGG
110 120 130 140 150
EIYKSLIDQV DTLHISTIDI EPEGDVYFPE IPSNFRPVFT QDFASNINYS

YQIWQKG
Length:157
Mass (Da):17,575
Last modified:July 21, 1986 - v1
Checksum:i487F818A40E4991B
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti75 – 751L → V in plasmid pLMO229.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X00926 Genomic DNA. Translation: CAA25445.1.
X17477 Genomic DNA. Translation: CAA35509.1.
X17478 Genomic DNA. Translation: CAA35512.1.
PIRiS03651. RDECD7.
RefSeqiNP_065309.1. NC_002525.1.
WP_000777554.1. NZ_JSPZ01000013.1.
YP_004422906.1. NC_015472.1.
YP_190212.1. NC_006671.1.

Genome annotation databases

GeneIDi10549022.
1238688.
3244885.
KEGGipg:10549022.
pg:1238688.
pg:3244885.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X00926 Genomic DNA. Translation: CAA25445.1.
X17477 Genomic DNA. Translation: CAA35509.1.
X17478 Genomic DNA. Translation: CAA35512.1.
PIRiS03651. RDECD7.
RefSeqiNP_065309.1. NC_002525.1.
WP_000777554.1. NZ_JSPZ01000013.1.
YP_004422906.1. NC_015472.1.
YP_190212.1. NC_006671.1.

3D structure databases

ProteinModelPortaliP00382.
ModBaseiSearch...
MobiDBiSearch...

Chemistry

BindingDBiP00382.
ChEMBLiCHEMBL2627.

Proteomic databases

PRIDEiP00382.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi10549022.
1238688.
3244885.
KEGGipg:10549022.
pg:1238688.
pg:3244885.

Phylogenomic databases

KOiK18589.

Enzyme and pathway databases

UniPathwayiUPA00077; UER00158.

Miscellaneous databases

PROiP00382.

Family and domain databases

Gene3Di3.40.430.10. 1 hit.
InterProiIPR012259. DHFR.
IPR024072. DHFR-like_dom.
IPR017925. DHFR_CS.
IPR001796. DHFR_dom.
[Graphical view]
PfamiPF00186. DHFR_1. 1 hit.
[Graphical view]
PRINTSiPR00070. DHFR.
SUPFAMiSSF53597. SSF53597. 1 hit.
PROSITEiPS00075. DHFR_1. 1 hit.
PS51330. DHFR_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The nucleotide sequence of the trimethoprim-resistant dihydrofolate reductase gene harbored by Tn7."
    Fling M.E., Richards C.
    Nucleic Acids Res. 11:5147-5158(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Transposon: Tn7.
  2. "Expression of the plasmid-encoded type I dihydrofolate reductase gene in cultured mammalian cells: a novel selectable marker."
    Simonsen C.S., Walter M., Levinson A.D.
    Nucleic Acids Res. 16:2235-2246(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Plasmid: IncI1 R483
  3. "The dhfrI trimethoprim resistance gene of Tn7 can be found at specific sites in other genetic surroundings."
    Sundstroem L., Skoeld O.
    Antimicrob. Agents Chemother. 34:642-650(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Plasmid: pLMO150 pLMO229
  4. "R plasmid dihydrofolate reductase with a dimeric subunit structure."
    Novak P., Stone D., Burchall J.J.
    J. Biol. Chem. 258:10956-10959(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-34.
    Plasmid: IncI1 R483

Entry informationi

Entry nameiDYR1_ECOLX
AccessioniPrimary (citable) accession number: P00382
Secondary accession number(s): P13923
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: July 22, 2015
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing, Plasmid, Transposable element

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.