NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=Stock 51;
DOI=10.1007/s004380050119; PubMed=8628226 [NCBI, ExPASy, EBI, Israel, Japan]
Schlichtherle I.M., van Houten J.L., Roos D.S.;
"Cloning and molecular analysis of the bifunctional dihydrofolate reductase-thymidylate synthase gene in the ciliated protozoan Paramecium tetraurelia.";
Mol. Gen. Genet. 250:665-673(1996).

[2]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Stock d4-2;
DOI=10.1038/nature05230; PubMed=17086204 [NCBI, ExPASy, EBI, Israel, Japan]
Aury J.-M., Jaillon O., Duret L., Noel B., Jubin C., Porcel B.M., Segurens B., Daubin V., Anthouard V., Aiach N., Arnaiz O., Billaut A., Beisson J., Blanc I., Bouhouche K., Camara F., Duharcourt S., Guigo R., Gogendeau D., Katinka M., Keller A.-M., Kissmehl R., Klotz C., Koll F., Le Mouel A., Lepere G., Malinsky S., Nowacki M., Nowak J.K., Plattner H., Poulain J., Ruiz F., Serrano V., Zagulski M., Dessen P., Betermier M., Weissenbach J., Scarpelli C., Schaechter V., Sperling L., Meyer E., Cohen J., Wincker P.;
"Global trends of whole-genome duplications revealed by the ciliate Paramecium tetraurelia.";
Nature 444:171-178(2006).

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

U03885; AAC47025.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
CT868563; CAK86280.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S65570; S65570.

RefSeq

XP_001453677.1; -.

3D structure databases

HSSP

P04818; 1HW4. [HSSP ENTRY / PDB]

ModBase

Q27828.

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).

BLOCKS

Q27828.

Genome annotation databases

GeneID

5039462; -.

Other

ProtoNet

Q27828.

UniRef

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`	`1 462`	`462`	`Bifunctional dihydrofolate reductase-thymidylate synthase.`	`PRO_0000186346`
`DOMAIN`	`6 165`	`160`	`DHFR.`
`REGION`	`180 462`	`283`	`Thymidylate synthase.`
`ACT_SITE`	`345 345`		`By similarity.`

Sequence information

Length: 462 AA [This is the length of the unprocessed precursor]

Molecular weight: 53201 Da [This is the MW of the unprocessed precursor]

CRC64: C8C9B3A12BBD5C72 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTTNKTFSMV LAMTLNGGIG YQNRLPWKLK EDLQRFKKIT TGGIVIMGRK TFESMNSKPL 

        70         80         90        100        110        120 
PNRVNVVISK NMKSSNEVQV FPRIEDALQF YNTSHQKLYL IGGKRIFEEG LATDKCSDVH 

       130        140        150        160        170        180 
LTRIGVETKC DVYLNKNIFS TFQVNKTSQT KSENGINYDY QHLINKNSHE QSYIDEEHQE 

       190        200        210        220        230        240 
NQYLDMITKI MKEGVSKDDR TGVGTMSIFG QTMRFNLAQS FPLLTTKKVF FRGVVEELLW 

       250        260        270        280        290        300 
FLRGNTNGKL LLDKGVKIWE GNGTREYLDT IGLQHRQEHD LGPVYGFQWR HFGAKYKDCQ 

       310        320        330        340        350        360 
TDYSNQGVDQ VKEIIQLLKN NPDSRRIILS AWNPIDLKQM ALPPCHVMSQ FFVANGKLSC 

       370        380        390        400        410        420 
MMYQRSCDFG LGIPFNIASY ALLTYMLAKE CNLNLGEFVH VLGDTHIYSN HVEALKKQIE 

       430        440        450        460 
RVPYPFPLLK IKGNKSLFDY TYEDFELVGY NAHDKIEMKM AV

Q27828 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