[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. DOI=10.1016/0166-6851(94)90087-6; PubMed=7969277 [NCBI, ExPASy, EBI, Israel, Japan] Cheng Q., Saul A.; "The dihydrofolate reductase domain of rodent malarias: point mutations and pyrimethamine resistance."; Mol. Biochem. Parasitol. 65:361-363(1994).

Comments

CATALYTIC ACTIVITY: 5,6,7,8-tetrahydrofolate + NADP⁺ = 7,8-dihydrofolate + NADPH.
CATALYTIC ACTIVITY: 5,10-methylenetetrahydrofolate + dUMP = dihydrofolate + dTMP.
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: In the N-terminal section; belongs to the dihydrofolate reductase family.
SIMILARITY: In the C-terminal section; belongs to the thymidylate synthase 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

L28121; AAA29582.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

P13922; 1J3I. [HSSP ENTRY / PDB]

ModBase

P46103.

Family and domain databases

InterPro

IPR012259; DHFR.
IPR001796; DHFR_reg.
IPR000398; Thymidylat_synth_C.
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.
PS00091; THYMIDYLATE_SYNTHASE; FALSE_NEG.
PROSITE graphical view of domain structure (profiles).

Other

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

Keywords

Methyltransferase; Multifunctional enzyme; NADP; Nucleotide biosynthesis; One-carbon metabolism; Oxidoreductase; Transferase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`<1 >182`	`>182`	`Bifunctional dihydrofolate reductase-thymidylate synthase.`	`PRO_0000186350`
`DOMAIN`	`<1 >182`	`>182`	`DHFR.`
`NON_TER`	`1 1`
`NON_TER`	`182 182`

Sequence information

Length: 182 AA [This is the length of the partial sequence of the unprocessed precursor]

Molecular weight: 20925 Da [This is the MW of the partial sequence of the unprocessed precursor]

CRC64: 33CCD27441763198 [This is a checksum on the sequence]

        10         20         30         40         50         60 
AICACCKVLN SNEKASCFSN KTFKGLGNAG GLPWKCNSVD MKHFVSVTSY VNENNYIRLK 

        70         80         90        100        110        120 
WKRDKYIKEN NVKVNTDGIP SIDKLQNIVV MGKTSWESIP SKFKPLENRI NIILSRTLKK 

       130        140        150        160        170        180 
ENLAKEYSNV IIIKSVDELF PILKCIKYYK CFIIGGASVY KEFLDRNLIK KIYFTRINNA 


YT

P46103 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	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