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P00382

- DYR1_ECOLX

UniProt

P00382 - DYR1_ECOLX

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Protein

Dihydrofolate reductase type 1

Gene

dhfrI

Organism
Escherichia coli
Status
Reviewed - 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

Pathwayi

GO - Molecular functioni

  1. dihydrofolate reductase activity Source: UniProtKB-EC
  2. NADP binding Source: InterPro

GO - Biological processi

  1. glycine biosynthetic process Source: InterPro
  2. nucleotide biosynthetic process Source: InterPro
  3. one-carbon metabolic process Source: UniProtKB-KW
  4. response to antibiotic Source: UniProtKB-KW
  5. response to methotrexate Source: UniProtKB-KW
  6. tetrahydrofolate biosynthetic process Source: UniProtKB-UniPathway
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

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 [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:
EMBL
GenBank
DDBJ
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.
YP_004422906.1. NC_015472.1.
YP_190212.1. NC_006671.1.

Genome annotation databases

GeneIDi10549022.
1238688.
3244885.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X00926 Genomic DNA. Translation: CAA25445.1 .
X17477 Genomic DNA. Translation: CAA35509.1 .
X17478 Genomic DNA. Translation: CAA35512.1 .
PIRi S03651. RDECD7.
RefSeqi NP_065309.1. NC_002525.1.
YP_004422906.1. NC_015472.1.
YP_190212.1. NC_006671.1.

3D structure databases

ProteinModelPortali P00382.
ModBasei Search...
MobiDBi Search...

Chemistry

ChEMBLi CHEMBL2627.

Proteomic databases

PRIDEi P00382.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 10549022.
1238688.
3244885.

Enzyme and pathway databases

UniPathwayi UPA00077 ; UER00158 .

Family and domain databases

Gene3Di 3.40.430.10. 1 hit.
InterProi IPR012259. DHFR.
IPR024072. DHFR-like_dom.
IPR017925. DHFR_CS.
IPR001796. DHFR_dom.
[Graphical view ]
Pfami PF00186. DHFR_1. 1 hit.
[Graphical view ]
PRINTSi PR00070. DHFR.
SUPFAMi SSF53597. SSF53597. 1 hit.
PROSITEi PS00075. DHFR_1. 1 hit.
PS51330. DHFR_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: October 1, 2014
This is version 86 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