[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. DOI=10.1016/0378-1119(84)90266-X; PubMed=6735180 [NCBI, ExPASy, EBI, Israel, Japan] Brisson N., Hohn T.; "Nucleotide sequence of the dihydrofolate-reductase gene borne by the plasmid R67 and conferring methotrexate resistance."; Gene 28:271-275(1984).
[2]	PROTEIN SEQUENCE. PubMed=387758 [NCBI, ExPASy, EBI, Israel, Japan] Stone D., Smith S.L.; "The amino acid sequence of the trimethoprim-resistant dihydrofolate reductase specified in Escherichia coli by R-plasmid R67."; J. Biol. Chem. 254:10857-10861(1979).
[3]	X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 17-78. DOI=10.1038/nsb1195-1018; PubMed=7583655 [NCBI, ExPASy, EBI, Israel, Japan] Narayana N., Matthews D.A., Howell E.E., Nguyen-Huu X.; "A plasmid-encoded dihydrofolate reductase from trimethoprim-resistant bacteria has a novel D2-symmetric active site."; Nat. Struct. Biol. 2:1018-1025(1995).

Comments

CATALYTIC ACTIVITY: 5,6,7,8-tetrahydrofolate + NADP⁺ = 7,8-dihydrofolate + NADPH.
PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis; tetrahydrofolate from dihydrofolate: step 1/1 .
MISCELLANEOUS: Type II plasmid-specified enzyme is practically insensitive to trimethoprim and methotrexate.
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.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

K02118; AAA26083.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A91512; RDECD6.

3D structure databases

PDB

1VIE; X-ray; 1.70 A; A=17-78.	[ExPASy / RCSB / EBI]
1VIF; X-ray; 1.80 A; A=17-78.	[ExPASy / RCSB / EBI]
2GQV; X-ray; 1.10 A; A=17-78.	[ExPASy / RCSB / EBI]
2P4T; X-ray; 1.15 A; A=17-78.	[ExPASy / RCSB / EBI]
2RH2; X-ray; 0.96 A; A=17-78.	[ExPASy / RCSB / EBI]
2RK1; X-ray; 1.26 A; A=17-78.	[ExPASy / RCSB / EBI]
2RK2; X-ray; 1.90 A; A=17-78.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1VIE; -.
1VIF; -.
2GQV; -.
2P4T; -.
2RH2; -.
2RK1; -.
2RK2; -.

ModBase

P00383.

Ontologies

GO:0006730;	Biological process: one-carbon compound metabolic process (inferred from electronic annotation from UniProtKB-KW).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0046677;	Biological process: response to antibiotic (inferred from electronic annotation from UniProtKB-KW).
GO:0031427;	Biological process: response to methotrexate (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR009159; Dhfr_type_II.
Graphical view of domain structure.

Pfam

PF06442; DHFR_2; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF000199; Dhfr_type_II; 1.

Other

P00383; -.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Antibiotic resistance; Direct protein sequencing; Methotrexate resistance; NADP; One-carbon metabolism; Oxidoreductase; Plasmid; Trimethoprim resistance.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 78`	`78`	`Dihydrofolate reductase type 2.`	`PRO_0000186435`
`STRAND`	`29 36`	`8`
`STRAND`	`39 46`	`8`
`STRAND`	`52 62`	`11`
`STRAND`	`66 70`	`5`
`HELIX`	`71 73`	`3`
`STRAND`	`74 76`	`3`

Sequence information

Length: 78 AA [This is the length of the unprocessed precursor]

Molecular weight: 8446 Da [This is the MW of the unprocessed precursor]

CRC64: 0BDB0B9146529417 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MERSSNEVSN PVAGNFVFPS NATFGMGDRV RKKSGAAWQG QIVGWYCTNL TPEGYAVESE 

        70 
AHPGSVQIYP VAALERIN

P00383 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools