NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Tokyo 1998;
DOI=10.1038/35024074; PubMed=10993077 [NCBI, ExPASy, EBI, Israel, Japan]
Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
"Genome sequence of the endocellular bacterial symbiont of aphids Buchnera sp. APS.";
Nature 407:81-86(2000).

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

BA000003; BAB12861.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_239975.1; -.

3D structure databases

HSSP

P00379; 1DHI. [HSSP ENTRY / SWISS-3DIMAGE / PDB]

ModBase

P57243.

Enzyme and pathway databases

BioCyc

BSP107806:BU143-MON; -.

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).

BLOCKS

P57243.

Genome annotation databases

GeneID

1109587; -.

GenomeReviews

BA000003_GR; BU143.

KEGG

buc:BU143; -.

Phylogenomic databases

HOGENOM

P57243; -.

Genome annotation databases

CMR

P57243; BU143.

Other

ProtoNet

P57243.

UniRef

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

Keywords

Complete proteome; NADP; One-carbon metabolism; Oxidoreductase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 161`	`161`	`Dihydrofolate reductase.`	`PRO_0000186383`
`DOMAIN`	`2 161`	`160`	`DHFR.`

Sequence information

Length: 161 AA [This is the length of the unprocessed precursor]

Molecular weight: 19053 Da [This is the MW of the unprocessed precursor]

CRC64: E3E88CA6FDC70079 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MNISLIAAIS KNLVIGYKNK IPWYLPEDLK WFKQKTINKN IIMGRLTWES IKKKPLPMRK 

        70         80         90        100        110        120 
NIVISSNEIK QEGIIWADSI SNAIISAQYN QEIMIIGGAK IYKEMLFYAN KLYLTHIDID 

       130        140        150        160 
IVGDAYFPEY KLYPYWKTLF RKKNTKNKMN PYNYSFEILS R

P57243 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