[1]	PROTEIN SEQUENCE. TISSUE=Liver; PubMed=500653 [NCBI, ExPASy, EBI, Israel, Japan] Smith S.L., Patrick P., Stone D., Phillips A.W., Burchall J.J.; "Porcine liver dihydrofolate reductase. Purification, properties, and amino acid sequence."; J. Biol. Chem. 254:11475-11484(1979).

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: 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

PIR

A00389; RDPGD.

3D structure databases

HSSP

P00374; 1KMS. [HSSP ENTRY / PDB]

SMR

P00377; 1-186.

ModBase

P00377.

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).
QuickGo view.

Family and domain databases

InterPro

IPR001796; DHFR_reg.
Graphical view of domain structure.

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).

Phylogenomic databases

HOVERGEN

P00377; -.

Other

UniRef

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

Keywords

Direct protein sequencing; NADP; One-carbon metabolism; Oxidoreductase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 186`	`186`	`Dihydrofolate reductase.`	`PRO_0000186365`
`DOMAIN`	`3 184`	`182`	`DHFR.`
`MOD_RES`	`162 162`		`Cysteine derivative; partial.`

Sequence information

Length: 186 AA [This is the length of the unprocessed precursor]

Molecular weight: 21455 Da [This is the MW of the unprocessed precursor]

CRC64: D05DB526FE5C12CE [This is a checksum on the sequence]

        10         20         30         40         50         60 
VRPLNCIVAV SQNMGIGKNG DLPWPPLRNE YKYFQRMTTT SSVEGKQNLV IMGRKTWFSI 

        70         80         90        100        110        120 
PEKNRPLKDR INIVLSRELK EPPQGAHFLA KSLDDALKLT EQPELKDKVD MVWIVGGSSV 

       130        140        150        160        170        180 
YKEAMNKPGH IRLFVTRIMK EFESDTFFPE IDLEKYKLLS ECSGVPSDVQ EEKGIKYKFE 


VYEKNN

P00377 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