[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=Y; DOI=10.1016/0166-6851(94)90076-0; PubMed=7969266 [NCBI, ExPASy, EBI, Israel, Japan] Reche P., Arrebola R., Olmo A., Santi D.V., Gonzalez-Pacanowska D., Ruiz-Perez L.M.; "Cloning and expression of the dihydrofolate reductase-thymidylate synthase gene from Trypanosoma cruzi."; Mol. Biochem. Parasitol. 65:247-258(1994).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=Y; DOI=10.1016/0166-6851(95)02557-X; PubMed=8920005 [NCBI, ExPASy, EBI, Israel, Japan] Reche P., Arrebola R., Santi D.V., Gonzalez-Pacanowska D., Ruiz-Perez L.M.; "Expression and characterization of the Trypanosoma cruzi dihydrofolate reductase domain."; Mol. Biochem. Parasitol. 76:175-185(1996).

Comments

CATALYTIC ACTIVITY: 5,6,7,8-tetrahydrofolate + NADP⁺ = 7,8-dihydrofolate + NADPH.
CATALYTIC ACTIVITY: 5,10-methylenetetrahydrofolate + dUMP = dihydrofolate + dTMP.
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: In the N-terminal section; belongs to the dihydrofolate reductase family.
SIMILARITY: In the C-terminal section; belongs to the thymidylate synthase 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

L22484; AAB49898.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

PDB

2H2Q; X-ray; 2.40 A; A/B=1-521.

[ExPASy / RCSB / EBI]

PDBsum

2H2Q; -.

ModBase

Q27793.

Family and domain databases

InterPro

IPR012262; DHFR-TS.
IPR001796; DHFR_reg.
IPR000398; Thymidylat_synth_C.
Graphical view of domain structure.

Gene3D

G3DSA:3.30.572.10; Thymidylat_synth_C; 1.

PANTHER

PTHR11549:SF2; Thymidylat_synth_C; 1.

Pfam

PF00186; DHFR_1; 1.
PF00303; Thymidylat_synt; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF000389; DHFR-TS; 1.

PRINTS

PR00070; DHFR.
PR00108; THYMDSNTHASE.

ProDom

PD001180; Thymidylat_synth; 1.
[Domain structure / List of seq. sharing at least 1 domain]

TIGRFAMs

TIGR03284; thym_sym; 1.

PROSITE

PS00075; DHFR_1; 1.
PS51330; DHFR_2; 1.
PS00091; THYMIDYLATE_SYNTHASE; 1.
PROSITE graphical view of domain structure (profiles).

Other

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

Keywords

3D-structure; Methyltransferase; Multifunctional enzyme; NADP; Nucleotide biosynthesis; One-carbon metabolism; Oxidoreductase; Transferase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 521`	`521`	`Bifunctional dihydrofolate reductase-thymidylate synthase.`	`PRO_0000186354`
`DOMAIN`	`22 232`	`211`	`DHFR.`
`REGION`	`237 521`	`285`	`Thymidylate synthase.`
`ACT_SITE`	`403 403`		`By similarity.`

Sequence information

Length: 521 AA [This is the length of the unprocessed precursor]

Molecular weight: 58853 Da [This is the MW of the unprocessed precursor]

CRC64: DCB9F8782855810C [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSLFKIRMPE TVAEGTRLAL RAFSLVVAVD EHGGIGDGRS IPWNVPEDMK FFRDLTTKLR 

        70         80         90        100        110        120 
GKNVKPSPAK RNAVVMGRKT WDSIPPKFRP LPGRLNVVLS STLTTQHLLD GLPDEEKRNL 

       130        140        150        160        170        180 
HADSIVAVNG GLEQALRLLA SPNYTPSIET VYCIGGGSVY AEALRPPCVH LLQAIYRTTI 

       190        200        210        220        230        240 
RASESSCSVF FRVPESGTEA AAGIEWQRET ISEELTSANG NETKYYFEKL IPRNREEEQY 

       250        260        270        280        290        300 
LSLVDRIIRE GNVKHDRTGV GTLSIFGAQM RFSLRNNRLP LLTTKRVFWR GVCEELLWFL 

       310        320        330        340        350        360 
RGETYAKKLS DKGVHIWDDN GSRAFLDSRG LTEYEEMDLG PVYGFQWRHF GAAYTHHDAN 

       370        380        390        400        410        420 
YDGQGVDQIK AIVETLKTNP DDRRMLFTAW NPSALPRMAL PPCHLLAQFY VSNGELSCML 

       430        440        450        460        470        480 
YQRSCDMGLG VPFNIASYAL LTILIAKATG LRPGELVHTL GDAHVYSNHV EPCNEQLKRV 

       490        500        510        520 
PRAFPYLVFR REREFLEDYE EGDMEVIDYA PYPPISMKMA V

Q27793 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