Reviewed, UniProtKB/Swiss-Prot P16184 (DYR_PNECA)

Names and origin

Protein names	Recommended name:     Dihydrofolate reductase     EC=1.5.1.3
Organism	Pneumocystis carinii
Taxonomic identifier	4754 [NCBI]
Taxonomic lineage	Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Pneumocystidomycetes › Pneumocystidaceae › Pneumocystis

Protein attributes

Sequence length	206 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (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.
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	3D-structure
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 compound 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 – 206

206

Dihydrofolate reductase

PRO_0000186376

Regions

Domain

6 – 204

199

DHFR

Secondary structure

1

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206

Helix Strand Turn

Details...

Beta strand

7 – 14

8

Beta strand

18 – 21

4

Helix

30 – 41

12

Turn

45 – 50

6

Beta strand

52 – 58

7

Helix

59 – 63

5

Helix

67 – 69

3

Beta strand

75 – 80

6

Beta strand

93 – 97

5

Helix

98 – 108

11

Beta strand

117 – 122

6

Helix

126 – 133

8

Beta strand

138 – 146

9

Beta strand

153 – 155

3

Helix

163 – 165

3

Turn

166 – 168

3

Helix

174 – 181

8

Beta strand

190 – 192

3

Beta strand

195 – 203

9

Sequences

	Sequence		Length	Mass (Da)
	P16184-1 [UniParc]. Last modified April 1, 1990. Version 1. Checksum: 6BA64A7019911508	FASTA	206	23,884
	10 20 30 40 50 60 MNQQKSLTLI VALTTSYGIG RSNSLPWKLK KEISYFKRVT SFVPTFDSFE SMNVVLMGRK 70 80 90 100 110 120 TWESIPLQFR PLKGRINVVI TRNESLDLGN GIHSAKSLDH ALELLYRTYG SESSVQINRI 130 140 150 160 170 180 FVIGGAQLYK AAMDHPKLDR IMATIIYKDI HCDVFFPLKF RDKEWSSVWK KEKHSDLESW 190 200 VGTKVPHGKI NEDGFDYEFE MWTRDL

References

[1]	"Isolation and expression of the Pneumocystis carinii dihydrofolate reductase gene." Edman J.C., Edman U., Cao M., Lundgren B., Kovacs J., Santi D.V. Proc. Natl. Acad. Sci. U.S.A. 86:8625-8629(1989) [PubMed: 2682653] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
[2]	"The structure of Pneumocystis carinii dihydrofolate reductase to 1.9-A resolution." Champness J.N., Achari A., Ballantine S.P., Bryant P.K., Delves C.J., Stammers D.K. Structure 2:915-924(1994) [PubMed: 7866743] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS).
[3]	"Ligand-induced conformational changes in the crystal structures of Pneumocystis carinii dihydrofolate reductase complexes with folate and NADP+." Cody V., Galitsky N., Rak D., Luft J.R., Pangborn W., Queener S.F. Biochemistry 38:4303-4312(1999) [PubMed: 10194348] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

M26495 Genomic DNA. Translation: AAA33787.1.
M26496 mRNA. Translation: AAA33788.1.

PIR

A36177.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1CD2	X-ray	2.20	A	1-206	[»]
1DAJ	X-ray	2.30	A	1-206	[»]
1DYR	X-ray	1.86	A	1-206	[»]
1E26	X-ray	2.00	A	1-206	[»]
1KLK	X-ray	2.30	A	1-206	[»]
1LY3	X-ray	1.90	A	1-206	[»]
1LY4	X-ray	2.10	A	1-206	[»]
1S3Y	X-ray	2.25	A	1-206	[»]
1VJ3	X-ray	2.10	A	2-206	[»]
2CD2	X-ray	1.90	A	1-206	[»]
2FZH	X-ray	2.10	A	1-206	[»]
2FZI	X-ray	1.60	A	1-206	[»]
3CD2	X-ray	2.50	A	1-206	[»]
4CD2	X-ray	2.00	A	1-206	[»]

ModBase

Search...

Enzyme and pathway databases

BRENDA

1.5.1.3. 3409.

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. 1 hit.
PS51330. DHFR_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

BindingDB

P16184.

Entry information

Entry name

DYR_PNECA

Accession

Primary (citable) accession number: P16184

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	April 1, 1990
Last modified:	June 16, 2009
This is version 65 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)