Reviewed, UniProtKB/Swiss-Prot O62583 (DYR_ENCCU)

Names and origin

Protein names

Recommended name:
    Dihydrofolate reductase
    EC=1.5.1.3

Gene names

Name:	DHFR-1
Ordered Locus Names:	ECU01_0170
AND
Name:	DHFR-2
Ordered Locus Names:	ECU01_1450
AND
Name:	DHFR-3
Ordered Locus Names:	ECU08_0080

Organism

Encephalitozoon cuniculi (Microsporidian parasite) [Complete proteome]

Taxonomic identifier

6035 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Microsporidia › Unikaryonidae › Encephalitozoon

Protein attributes

Sequence length	205 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Catalytic activity	5,6,7,8-tetrahydrofolate + NADP+ = 7,8-dihydrofolate + NADPH.
Pathway	Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-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.
Sequence similarities	Belongs to the dihydrofolate reductase family. Contains 1 DHFR (dihydrofolate reductase) domain.

Ontologies

Keywords
Biological process	One-carbon metabolism
Ligand	NADP
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	glycine biosynthetic process Inferred from electronic annotation. Source: InterPro nucleotide biosynthetic process Inferred from electronic annotation. Source: InterPro one-carbon metabolic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	NADP or NADPH binding Inferred from electronic annotation. Source: InterPro dihydrofolate reductase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 205	205	Dihydrofolate reductase		PRO_0000186373
Regions
	Domain	1 – 201	201	DHFR

Sequences

	Sequence		Length	Mass (Da)
	O62583-1 [UniParc]. Last modified August 1, 1998. Version 1. Checksum: 45450EAA534487DD	FASTA	205	22,883
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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." Duffieux F., Peyret P., Roe B.A., Vivares C.P. Microb. Comp. Genomics 3:1-11(1998) [PubMed: 11013707] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Sequence and analysis of chromosome I of the amitochondriate intracellular parasite Encephalitozoon cuniculi (Microspora)." Peyret P., Katinka M.D., Duprat S., Duffieux F., Barbe V., Barbazanges M., Weissenbach J., Saurin W., Vivares C.P. Genome Res. 11:198-207(2001) [PubMed: 11157783] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: GB-M1.
[3]	"Genome sequence and gene compaction of the eukaryote parasite Encephalitozoon cuniculi." 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. Nature 414:450-453(2001) [PubMed: 11719806] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: GB-M1.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AJ005644 Genomic DNA. Translation: CAA06647.1. AL391737 Genomic DNA. Translation: CAD24887.1. AL391737 Genomic DNA. Translation: CAD25017.1. AL590448 Genomic DNA. Translation: CAD26313.1.
RefSeq	NP_597137.1. XP_965852.1. XP_965982.1.
3D structure databases
HSSP	HSSP built from PDB template 1J3J based on UniProtKB P13922.
ModBase	Search...
Genome annotation databases
GeneID	859559. 860188. 860189.
GenomeReviews	Gene locus ECU01_0170 in contig AL391737_GR. Gene locus ECU01_1450 in contig AL391737_GR. Gene locus ECU08_0080 in contig AL590448_GR.
KEGG	ecu:ECU01_0170. ecu:ECU01_1450. ecu:ECU08_0080.
Phylogenomic databases
HOGENOM	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.
BRENDA	1.5.1.3. 276319.
Family and domain databases
InterPro	IPR012259. DHFR. IPR001796. DHFR_reg. IPR017925. Dihydrofolate_reductase_CS. [Graphical view]
PANTHER	PTHR11549:SF1. DHFR. 1 hit.
Pfam	PF00186. DHFR_1. 1 hit. [Graphical view]
PRINTS	PR00070. DHFR.
PROSITE	PS00075. DHFR_1. False negative. PS51330. DHFR_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DYR_ENCCU

Accession

Primary (citable) accession number: O62583

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	August 1, 1998
Last modified:	September 22, 2009
This is version 55 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)