[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PubMed=11013707 [NCBI, ExPASy, EBI, Israel, Japan] Duffieux F., Peyret P., Roe B.A., Vivares C.P.; "First report on the systematic sequencing of the small genome of Encephalitozoon cuniculi (Protozoa, Microspora): gene organization of a 4.3 kbp region on chromosome I."; Microb. Comp. Genomics 3:1-11(1998).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=GB-M1; DOI=10.1101/gr.164301; PubMed=11157783 [NCBI, ExPASy, EBI, Israel, Japan] Peyret P., Katinka M.D., Duprat S., Duffieux F., Barbe V., Barbazanges M., Weissenbach J., Saurin W., Vivares C.P.; "Sequence and analysis of chromosome I of the amitochondriate intracellular parasite Encephalitozoon cuniculi (Microspora)."; Genome Res. 11:198-207(2001).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=GB-M1; DOI=10.1038/35106579; PubMed=11719806 [NCBI, ExPASy, EBI, Israel, Japan] Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F., Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P., Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J., Vivares C.P.; "Genome sequence and gene compaction of the eukaryote parasite Encephalitozoon cuniculi."; Nature 414:450-453(2001).

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

AJ005644; CAA06647.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AL391737; CAD24887.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AL391737; CAD25017.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AL590448; CAD26313.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_597137.1; -.
XP_965852.1; -.
XP_965982.1; -.

3D structure databases

HSSP

P13922; 1J3J. [HSSP ENTRY / PDB]

ModBase

O62583.

Enzyme and pathway databases

BioCyc

ECUN-XXX-01:ECUN-XXX-01-000015-MON; -.
ECUN-XXX-01:ECUN-XXX-01-000145-MON; -.
ECUN-XXX-01:ECUN-XXX-01-001587-MON; -.

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

Genome annotation databases

GeneID

859559; -.
860188; -.
860189; -.

GenomeReviews

AL391737_GR; ECU01_0170.
AL391737_GR; ECU01_1450.
AL590448_GR; ECU08_0080.

KEGG

ecu:ECU01_0170; -.
ecu:ECU01_1450; -.
ecu:ECU08_0080; -.

Phylogenomic databases

HOGENOM

O62583; -.

Other

ProtoNet

O62583.

UniRef

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

Keywords

Complete proteome; NADP; One-carbon metabolism; Oxidoreductase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 205`	`205`	`Dihydrofolate reductase.`	`PRO_0000186373`
`DOMAIN`	`1 201`	`201`	`DHFR.`

Sequence information

Length: 205 AA [This is the length of the unprocessed precursor]

Molecular weight: 22883 Da [This is the MW of the unprocessed precursor]

CRC64: 45450EAA534487DD [This is a checksum on the sequence]

        10         20         30         40         50         60 
MLALVVALAS HRGIGNANAL PWPRPLAADM AWFRTLSQSI PLISPDRIAL APSASNAVVM 

        70         80         90        100        110        120 
GRRTWDSIPS RFRPLANRIN VVLSRGPARS TENTFFIQTF EALDSLPLPP SSMTFVIGGR 

       130        140        150        160        170        180 
DVYSLALESG RPHLIFATEV FESPECDVFF PHIDWASYEK RDITRDVSRL IDRTLASAFY 

       190        200 
SPETATFTEN GTSFKMFLYT KPETR

O62583 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