[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=10127/5; DOI=10.1016/0378-1119(94)90049-3; PubMed=7916311 [NCBI, ExPASy, EBI, Israel, Japan] Daly S., Mastromei G., Yacoub A., Lorenzetti R.; "Sequence of a dihydrofolate reductase-encoding gene from Candida albicans."; Gene 147:115-118(1994).
[2]	PROTEIN SEQUENCE OF 1-25, AND NUCLEOTIDE SEQUENCE OF 26-36. PubMed=2642898 [NCBI, ExPASy, EBI, Israel, Japan] Baccanari D.P., Tansik R.L., Joyner S.S., Fling M.E., Smith P.L., Freisheim J.H.; "Characterization of Candida albicans dihydrofolate reductase."; J. Biol. Chem. 264:1100-1107(1989).
[3]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS). STRAIN=SYNTEX CA755; DOI=10.1074/jbc.272.48.30289; PubMed=9374515 [NCBI, ExPASy, EBI, Israel, Japan] Whitlow M., Howard A.J., Stewart D., Hardman K.D., Kuyper L.F., Baccanari D.P., Fling M.E., Tansik R.L.; "X-ray crystallographic studies of Candida albicans dihydrofolate reductase. High resolution structures of the holoenzyme and an inhibited ternary complex."; J. Biol. Chem. 272:30289-30298(1997).

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

X78968; CAA55561.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U84588; AAC05610.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A32203; A32203.

3D structure databases

PDB

1AI9; X-ray; 1.85 A; A/B=1-192.	[ExPASy / RCSB / EBI]
1AOE; X-ray; 1.60 A; A/B=1-192.	[ExPASy / RCSB / EBI]
1IA1; X-ray; 1.70 A; A/B=1-192.	[ExPASy / RCSB / EBI]
1IA2; X-ray; 1.82 A; A/B=1-192.	[ExPASy / RCSB / EBI]
1IA3; X-ray; 1.78 A; A/B=1-192.	[ExPASy / RCSB / EBI]
1IA4; X-ray; 1.85 A; A/B=1-192.	[ExPASy / RCSB / EBI]
1M78; X-ray; 1.71 A; A/B=1-192.	[ExPASy / RCSB / EBI]
1M79; X-ray; 1.70 A; A/B=1-192.	[ExPASy / RCSB / EBI]
1M7A; X-ray; 1.76 A; A/B=1-192.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1AI9; -.
1AOE; -.
1IA1; -.
1IA2; -.
1IA3; -.
1IA4; -.
1M78; -.
1M79; -.
1M7A; -.

ModBase

P22906.

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

Other

P22906; -.

P22906; -.

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`	`1 192`	`192`	`Dihydrofolate reductase.`	`PRO_0000186374`
`DOMAIN`	`5 191`	`187`	`DHFR.`
`VARIANT`	`2 2`	`1`	`S -> L (in strain: SYNTEX CA755).`
`VARIANT`	`84 84`	`1`	`K -> E (in strain: SYNTEX CA755).`
`STRAND`	`6 13`	`8`
`TURN`	`14 17`	`4`
`STRAND`	`18 21`	`4`
`HELIX`	`30 41`	`12`
`STRAND`	`49 55`	`7`
`HELIX`	`56 61`	`6`
`HELIX`	`64 66`	`3`
`STRAND`	`72 77`	`6`
`STRAND`	`84 87`	`4`
`STRAND`	`90 95`	`6`
`HELIX`	`96 100`	`5`
`STRAND`	`105 111`	`7`
`HELIX`	`115 121`	`7`
`STRAND`	`127 136`	`10`
`STRAND`	`140 143`	`4`
`HELIX`	`153 155`	`3`
`STRAND`	`156 158`	`3`
`HELIX`	`161 168`	`8`
`STRAND`	`175 179`	`5`
`STRAND`	`182 191`	`10`

Sequence information

Length: 192 AA [This is the length of the unprocessed precursor]

Molecular weight: 22139 Da [This is the MW of the unprocessed precursor]

CRC64: D8E3BEAC1DCADB4C [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSKPNVAIIV AALKPALGIG YKGKMPWRLR KEIRYFKDVT TRTTKPNTRN AVIMGRKTWE 

        70         80         90        100        110        120 
SIPQKFRPLP DRLNIILSRS YENKIIDDNI IHASSIESSL NLVSDVERVF IIGGAEIYNE 

       130        140        150        160        170        180 
LINNSLVSHL LITEIEHPSP ESIEMDTFLK FPLESWTKQP KSELQKFVGD TVLEDDIKEG 

       190 
DFTYNYTLWT RK

P22906 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