Reviewed, UniProtKB/Swiss-Prot P00378 (DYR_CHICK)

Names and origin

Protein names

Recommended name:
    Dihydrofolate reductase
    EC=1.5.1.3

Gene names

Name:

DHFR

Organism

Gallus gallus (Chicken)

Taxonomic identifier

9031 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Galliformes › Phasianidae › Phasianinae › Gallus

Protein attributes

Sequence length	189 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 Direct protein sequencing
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 – 189

189

Dihydrofolate reductase

PRO_0000186367

Regions

Domain

3 – 184

182

DHFR

Experimental info

Sequence conflict

141

1

E → Q AA sequence Ref.2

Secondary structure

1

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189

Helix Strand Turn

Details...

Beta strand

3 – 10

8

Beta strand

15 – 18

4

Helix

28 – 39

12

Beta strand

47 – 53

7

Helix

54 – 59

6

Helix

62 – 64

3

Beta strand

70 – 75

6

Beta strand

87 – 92

6

Helix

93 – 101

9

Helix

103 – 106

4

Beta strand

109 – 114

6

Helix

118 – 126

9

Beta strand

127 – 140

14

Beta strand

145 – 147

3

Turn

153 – 155

3

Beta strand

156 – 158

3

Beta strand

170 – 172

3

Beta strand

175 – 184

10

Sequences

	Sequence		Length	Mass (Da)
	P00378-1 [UniParc]. Last modified July 21, 1986. Version 1. Checksum: BC5F50C94BCA3EDA	FASTA	189	21,650
	10 20 30 40 50 60 VRSLNSIVAV CQNMGIGKDG NLPWPPLRNE YKYFQRMTST SHVEGKQNAV IMGKKTWFSI 70 80 90 100 110 120 PEKNRPLKDR INIVLSRELK EAPKGAHYLS KSLDDALALL DSPELKSKVD MVWIVGGTAV 130 140 150 160 170 180 YKAAMEKPIN HRLFVTRILH EFESDTFFPE IDYKDFKLLT EYPGVPADIQ EEDGIQYKFE VYQKSVLAQ

References

[1]	"Primary structure of chicken liver dihydrofolate reductase." Kumar A.A., Blankenship D.T., Kaufman B.T., Freisheim J.H. Biochemistry 19:667-678(1980) [PubMed: 6766736] [Abstract] Cited for: PROTEIN SEQUENCE.
[2]	"Activation of chicken liver dihydrofolate reductase by urea and guanidine hydrochloride is accompanied by conformational change at the active site." Fan Y.X., Ju M., Zhou J.M., Tsou C.L. Biochem. J. 315:97-102(1996) [PubMed: 8670138] [Abstract] Cited for: PROTEIN SEQUENCE OF 19-22; 138-141 AND 158-161.
[3]	"Crystal structure of chicken liver dihydrofolate reductase complexed with NADP+ and biopterin." McTigue M.A., Davies J.F. II, Kaufman B.T., Kraut J. Biochemistry 31:7264-7273(1992) [PubMed: 1510919] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

IPI

IPI00822128.

PIR

RDCHD. A00390.

UniGene

Gga.2883

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1DR1	X-ray	2.20	A	1-189	[»]
1DR2	X-ray	2.30	A	1-189	[»]
1DR3	X-ray	2.30	A	1-189	[»]
1DR4	X-ray	2.40	A	1-189	[»]
1DR5	X-ray	2.40	A	1-189	[»]
1DR6	X-ray	2.40	A	1-189	[»]
1DR7	X-ray	2.40	A	1-189	[»]
8DFR	X-ray	1.70	A	1-189	[»]

ModBase

Search...

Genome annotation databases

Ensembl

ENSGALG00000015579. Gallus gallus. [Contig view]

Phylogenomic databases

HOGENOM

P00378.

HOVERGEN

P00378.

Enzyme and pathway databases

BRENDA

1.5.1.3. 4.

Family and domain databases

InterPro

IPR012259. DHFR.
IPR001796. DHFR_reg.
IPR017925. Dihydrofolate_reductase_CS.
[Graphical view]

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...

Entry information

Entry name

DYR_CHICK

Accession

Primary (citable) accession number: P00378

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	June 16, 2009
This is version 72 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)