[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PubMed=2509470 [NCBI, ExPASy, EBI, Israel, Japan] Zusman T., Rosenshine I., Boehm G., Jaenicke R., Leskiw B., Mevarech M.; "Dihydrofolate reductase of the extremely halophilic archaebacterium Halobacterium volcanii. The enzyme and its coding gene."; J. Biol. Chem. 264:18878-18883(1989).
[2]	X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS). DOI=10.1016/S0969-2126(98)00009-4; PubMed=9493269 [NCBI, ExPASy, EBI, Israel, Japan] Pieper U., Kapadia G., Mevarech M., Herzberg O.; "Structural features of halophilicity derived from the crystal structure of dihydrofolate reductase from the Dead Sea halophilic archaeon, Haloferax volcanii."; Structure 6:75-88(1998).

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

J05088; AAA72219.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A34429; A34429.

3D structure databases

PDB

1VDR; X-ray; 2.55 A; A/B=1-162.	[ExPASy / RCSB / EBI]
2ITH; NMR; -; A=1-162.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1VDR; -.
2ITH; -.

ModBase

P15093.

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

P15093; -.

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

Keywords

3D-structure; NADP; One-carbon metabolism; Oxidoreductase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 162`	`162`	`Dihydrofolate reductase.`	`PRO_0000186433`
`DOMAIN`	`2 162`	`161`	`DHFR.`
`STRAND`	`3 11`	`9`
`STRAND`	`13 17`	`5`
`HELIX`	`27 36`	`10`
`STRAND`	`38 40`	`3`
`STRAND`	`42 45`	`4`
`HELIX`	`46 51`	`6`
`TURN`	`52 54`	`3`
`STRAND`	`58 64`	`7`
`STRAND`	`73 75`	`3`
`STRAND`	`78 81`	`4`
`HELIX`	`82 91`	`10`
`STRAND`	`97 101`	`5`
`HELIX`	`103 109`	`7`
`HELIX`	`110 112`	`3`
`STRAND`	`114 124`	`11`
`STRAND`	`128 130`	`3`
`TURN`	`136 138`	`3`
`STRAND`	`139 146`	`8`
`STRAND`	`151 157`	`7`

Sequence information

Length: 162 AA [This is the length of the unprocessed precursor]

Molecular weight: 17980 Da [This is the MW of the unprocessed precursor]

CRC64: 31B047661F14281F [This is a checksum on the sequence]

        10         20         30         40         50         60 
MELVSVAALA ENRVIGRDGE LPWPSIPADK KQYRSRIADD PVVLGRTTFE SMRDDLPGSA 

        70         80         90        100        110        120 
QIVMSRSERS FSVDTAHRAA SVEEAVDIAA SLDAETAYVI GGAAIYALFQ PHLDRMVLSR 

       130        140        150        160 
VPGEYEGDTY YPEWDAAEWE LDAETDHEGF TLQEWVRSAS SR

P15093 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