NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1016/0042-6822(90)90020-R; PubMed=2161148 [NCBI, ExPASy, EBI, Israel, Japan]
Biesinger B., Trimble J.J., Desrosiers R.C., Fleckenstein B.;
"The divergence between two oncogenic Herpesvirus saimiri strains in a genomic region related to the transforming phenotype.";
Virology 176:505-514(1990).

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

EMBL

M55264; AAA72932.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

P00374; 1KMS. [HSSP ENTRY / PDB]

SMR

P22573; 5-184.

ModBase

P22573.

Ontologies

GO:0004146;	Molecular function: dihydrofolate reductase activity (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

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).

ProtoNet

P22573.

Other

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`	`1 213`	`213`	`Viral dihydrofolate reductase.`	`PRO_0000186381`
`DOMAIN`	`4 184`	`181`	`DHFR.`

Sequence information

Length: 213 AA [This is the length of the unprocessed precursor]

Molecular weight: 24577 Da [This is the MW of the unprocessed precursor]

CRC64: 932BBB2EA200033C [This is a checksum on the sequence]

        10         20         30         40         50         60 
MVLLLNCIVA VDQNMGIGKK GHLPWPLLIN DFKYFQRMTT SSVKNKQNLV IMGKNTWFSI 

        70         80         90        100        110        120 
PEKNRPLKDR INLVLSKKLK EIPHGAHFLA RSLNDALKLI EQPELVNKVD RVWIIGGSSV 

       130        140        150        160        170        180 
YKDAMNYSSH LKLFVTRIMQ SFETDTFFPE IDLKNYKLLI EYPGVPSNTQ EEKGIKYKFE 

       190        200        210 
VYEKIVNTFL FKSHAGLTCS VKPKEASYDF ELS

P22573 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