[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=RH; PubMed=8454599 [NCBI, ExPASy, EBI, Israel, Japan] Roos D.S.; "Primary structure of the dihydrofolate reductase-thymidylate synthase gene from Toxoplasma gondii."; J. Biol. Chem. 268:6269-6280(1993).

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

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Cross-references

Sequence databases

EMBL

L08489; AAB00163.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A46005; A46005.

3D structure databases

HSSP

P04818; 1HW3. [HSSP ENTRY / PDB]

ModBase

Q07422.

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

Q07422; -.

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

Keywords

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

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 610`	`610`	`Bifunctional dihydrofolate reductase-thymidylate synthase.`	`PRO_0000186352`
`DOMAIN`	`4 250`	`247`	`DHFR.`
`REGION`	`322 610`	`289`	`Thymidylate synthase.`
`ACT_SITE`	`489 489`		`By similarity.`

Sequence information

Length: 610 AA [This is the length of the unprocessed precursor]

Molecular weight: 68752 Da [This is the MW of the unprocessed precursor]

CRC64: CFAF564416D04A29 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MQKPVCLVVA MTPKRGIGIN NGLPWPHLTT DFKHFSRVTK TTPEEASRLN GWLPRKFAKT 

        70         80         90        100        110        120 
GDSGLPSPSV GKRFNAVVMG RKTWESMPRK FRPLVDRLNI VVSSSLKEED IAAEKPQAEG 

       130        140        150        160        170        180 
QQRVRVCASL PAALSLLEEE YKDSVDQIFV VGGAGLYEAA LSLGVASHLY ITRVAREFPC 

       190        200        210        220        230        240 
DVFFPAFPGD DILSNKSTAA QAAAPAESVF VPFCPELGRE KDNEATYRPI FISKTFSDNG 

       250        260        270        280        290        300 
VPYDFVVLEK RRKTDDAATA EPSNAMSSLT STRETTPVHG LQAPSSAAAI APVLAWMDEE 

       310        320        330        340        350        360 
DRKKREQKEL IRAVPHVHFR GHEEFQYLDL IADIINNGRT MDDRTGVGVI SKFGCTMRYS 

       370        380        390        400        410        420 
LDQAFPLLTT KRVFWKGVLE ELLWFIRGDT NANHLSEKGV KIWDKNVTRE FLDSRNLPHR 

       430        440        450        460        470        480 
EVGDIGPGYG FQWRHFGAAY KDMHTDYTGQ GVDQLKNVIQ MLRTNPTDRR MLMTAWNPAA 

       490        500        510        520        530        540 
LDEMALPPCH LLCQFYVNDQ KELSCIMYQR SCDVGLGVPF NIASYSLLTL MVAHVCNLKP 

       550        560        570        580        590        600 
KEFIHFMGNT HVYTNHVEAL KEQLRREPRP FPIVNILNKE RIKEIDDFTA EDFEVVGYVP 

       610 
HGRIQMEMAV

Q07422 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
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