NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 3-22; 32-38; 143-149; 153-159 AND 170-175, AND ENZYME REGULATION.
TISSUE=Larva;
PubMed=10632709 [NCBI, ExPASy, EBI, Israel, Japan]
Walker V.K., Tyshenko M.G., Kuiper M.J., Dargar R.V., Yuhas D.A., Cruickshank P.A., Chaguturu R.;
"Tobacco budworm dihydrofolate reductase is a promising target for insecticide discovery.";
Eur. J. Biochem. 267:394-403(2000).

Comments

CATALYTIC ACTIVITY: 5,6,7,8-tetrahydrofolate + NADP⁺ = 7,8-dihydrofolate + NADPH.
ENZYME REGULATION: Activated by dithiothreitol and p-chloromercuribenzoate. Inhibited by trimethoprim, methotrexate, sodium tetrathionate and hydroxymercuribenzoate.
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

AF104106; AAF04459.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

P00374; 1KMV. [HSSP ENTRY / PDB]

ModBase

Q9U8B8.

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

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

Keywords

Direct protein sequencing; NADP; One-carbon metabolism; Oxidoreductase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 185`	`185`	`Dihydrofolate reductase.`	`PRO_0000186371`
`DOMAIN`	`5 184`	`180`	`DHFR.`
`CONFLICT`	`5 5`		`K -> L (in Ref. 1; AA sequence).`
`CONFLICT`	`7 7`		`N -> D (in Ref. 1; AA sequence).`
`CONFLICT`	`11 13`		`AAC -> IFD (in Ref. 1; AA sequence).`
`CONFLICT`	`15 15`		`N -> D (in Ref. 1; AA sequence).`
`CONFLICT`	`21 21`		`N -> D (in Ref. 1; AA sequence).`
`CONFLICT`	`158 158`		`H -> Q (in Ref. 1; AA sequence).`

Sequence information

Length: 185 AA [This is the length of the unprocessed precursor]

Molecular weight: 21089 Da [This is the MW of the unprocessed precursor]

CRC64: 9B8C0E50ED175812 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSQVKLNLIA AACDNMGIGV NGALPWRLKK EMAYFTTMTS KVSEPTKVNA VIMGRRTWDC 

        70         80         90        100        110        120 
IPDKYRPLQD RVNIVLTHNV DSVKENVPEG VMVFPGLDEA IKYIEGREDI ESTWVIGGSS 

       130        140        150        160        170        180 
IYRAAMTHPN CGKIYLTEIQ KSFDCDTFFP NIDKQQFHLV DEEQIPGEKQ VEGNISYYFR 


VYKKL

Q9U8B8 in FASTA format

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View entry in raw text format (no links)
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	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