NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTAGENESIS.
STRAIN=ATCC 14990 / DSM 20044 / CIP 81.55;
PubMed=7768789 [NCBI, ExPASy, EBI, Israel, Japan]
Dale G.E., Broger C., Hartman P.G., Langen H., Page M.G.P., Then R.L., Stueber D.;
"Characterization of the gene for the chromosomal dihydrofolate reductase (DHFR) of Staphylococcus epidermidis ATCC 14990: the origin of the trimethoprim-resistant S1 DHFR from Staphylococcus aureus?";
J. Bacteriol. 177:2965-2970(1995).

Comments

FUNCTION: Not resistant to trimethoprim.
CATALYTIC ACTIVITY: 5,6,7,8-tetrahydrofolate + NADP⁺ = 7,8-dihydrofolate + NADPH.
PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis; tetrahydrofolate from dihydrofolate: step 1/1 .
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.
SIMILARITY: Belongs to the dihydrofolate reductase family.
SIMILARITY: Contains 1 DHFR (dihydrofolate reductase) domain.

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

Z48233; CAA88269.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A57271; A57271.

3D structure databases

HSSP

P00379; 1DHI. [HSSP ENTRY / SWISS-3DIMAGE / PDB]

ModBase

P0C0P0.

Ontologies

GO:0004146;	Molecular function: dihydrofolate reductase activity (inferred from electronic annotation from InterPro).
GO:0050661;	Molecular function: NADP binding (inferred from electronic annotation from InterPro).
GO:0006545;	Biological process: glycine biosynthetic process (inferred from electronic annotation from InterPro).
GO:0009165;	Biological process: nucleotide biosynthetic process (inferred from electronic annotation from InterPro).
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).
QuickGo view.

Family and domain databases

InterPro

IPR012259; DHFR.
IPR001796; DHFR_reg.
Graphical view of domain structure.

PANTHER

PTHR11549:SF1; DHFR; 1.

Pfam

PF00186; DHFR_1; 1.
Pfam graphical view of domain structure.

PRINTS

PR00070; DHFR.

PROSITE

PS00075; DHFR_1; 1.
PS51330; DHFR_2; 1.
PROSITE graphical view of domain structure (profiles).

Other

ProtoNet

P0C0P0.

UniRef

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

Keywords

NADP; One-carbon metabolism; Oxidoreductase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 161`	`161`	`Dihydrofolate reductase.`	`PRO_0000186413`
`DOMAIN`	`2 157`	`156`	`DHFR.`
`MUTAGEN`	`32 32`		`V->I: 3-fold increase of KM for dihydrofolate.`
`MUTAGEN`	`44 44`		`G->A: 5-fold increase of KM for NADPH.`
`MUTAGEN`	`99 99`		`F->Y: Trimethoprim resistance.`

Sequence information

Length: 161 AA [This is the length of the unprocessed precursor]

Molecular weight: 18417 Da [This is the MW of the unprocessed precursor]

CRC64: CB3167940A387EE0 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTLSIIVAHD KQRVIGYQNQ LPWHLPNDLK HVKQLTTGNT LVMGRKTFNS IGKPLPNRRN 

        70         80         90        100        110        120 
VVLTNQASFH HEGVDVINSL DEIKELSGHV FIFGGQTLFE AMIDQVDDMY ITVIDGKFQG 

       130        140        150        160 
DTFFPPYTFE NWEVESSVEG QLDEKNTIPH TFLHLVRRKG K

P0C0P0 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