[1]	PROTEIN SEQUENCE. DOI=10.1021/bi00545a010; PubMed=6766736 [NCBI, ExPASy, EBI, Israel, Japan] Kumar A.A., Blankenship D.T., Kaufman B.T., Freisheim J.H.; "Primary structure of chicken liver dihydrofolate reductase."; Biochemistry 19:667-678(1980).
[2]	PROTEIN SEQUENCE OF 19-22; 138-141 AND 158-161. PubMed=8670138 [NCBI, ExPASy, EBI, Israel, Japan] Fan Y.X., Ju M., Zhou J.M., Tsou C.L.; "Activation of chicken liver dihydrofolate reductase by urea and guanidine hydrochloride is accompanied by conformational change at the active site."; Biochem. J. 315:97-102(1996).
[3]	X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS). DOI=10.1021/bi00147a009; PubMed=1510919 [NCBI, ExPASy, EBI, Israel, Japan] McTigue M.A., Davies J.F. II, Kaufman B.T., Kraut J.; "Crystal structure of chicken liver dihydrofolate reductase complexed with NADP+ and biopterin."; Biochemistry 31:7264-7273(1992).

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

PIR

A00390; RDCHD.

UniGene

Gga.2883

3D structure databases

PDB

1DR1; X-ray; 2.20 A; A=1-189.	[ExPASy / RCSB / EBI]
1DR2; X-ray; 2.30 A; A=1-189.	[ExPASy / RCSB / EBI]
1DR3; X-ray; 2.30 A; A=1-189.	[ExPASy / RCSB / EBI]
1DR4; X-ray; 2.40 A; A=1-189.	[ExPASy / RCSB / EBI]
1DR5; X-ray; 2.40 A; A=1-189.	[ExPASy / RCSB / EBI]
1DR6; X-ray; 2.40 A; A=1-189.	[ExPASy / RCSB / EBI]
1DR7; X-ray; 2.40 A; A=1-189.	[ExPASy / RCSB / EBI]
8DFR; X-ray; 1.70 A; A=1-189.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1DR1; -.
1DR2; -.
1DR3; -.
1DR4; -.
1DR5; -.
1DR6; -.
1DR7; -.
8DFR; -.

ModBase

P00378.

Ontologies

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).

Genome annotation databases

Ensembl

ENSGALG00000015579; Gallus gallus. [Contig view]

Phylogenomic databases

HOGENOM

P00378; -.

HOVERGEN

P00378; -.

Other

LinkHub

P00378; -.

UniRef

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

Keywords

3D-structure; Direct protein sequencing; NADP; One-carbon metabolism; Oxidoreductase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 189`	`189`	`Dihydrofolate reductase.`	`PRO_0000186367`
`DOMAIN`	`3 184`	`182`	`DHFR.`
`CONFLICT`	`141 141`		`E -> Q (in Ref. 2; AA sequence).`
`STRAND`	`3 10`	`8`
`STRAND`	`15 18`	`4`
`HELIX`	`28 39`	`12`
`STRAND`	`47 53`	`7`
`HELIX`	`54 59`	`6`
`HELIX`	`62 64`	`3`
`STRAND`	`70 75`	`6`
`STRAND`	`87 92`	`6`
`HELIX`	`93 101`	`9`
`HELIX`	`103 106`	`4`
`STRAND`	`109 114`	`6`
`HELIX`	`118 126`	`9`
`STRAND`	`127 140`	`14`
`STRAND`	`145 147`	`3`
`TURN`	`153 155`	`3`
`STRAND`	`156 158`	`3`
`STRAND`	`170 172`	`3`
`STRAND`	`175 184`	`10`

Sequence information

Length: 189 AA [This is the length of the unprocessed precursor]

Molecular weight: 21650 Da [This is the MW of the unprocessed precursor]

CRC64: BC5F50C94BCA3EDA [This is a checksum on the sequence]

        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

P00378 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