NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=Isolate Ari/Pakistan, Isolate BUR-151, and Isolate BUR-98;
DOI=10.1016/S0378-1119(98)00118-8; PubMed=9573357 [NCBI, ExPASy, EBI, Israel, Japan]
Eldin de Pecoulas P., Basco L.K., Tahar R., Ouatas T., Mazabraud A.;
"Analysis of the Plasmodium vivax dihydrofolate reductase-thymidylate synthase gene sequence.";
Gene 211:177-185(1998).

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 .
DOMAIN: The repeat region is missing in the pyrimethamine-resistant isolates BUR-98 and BUR-151.
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

X98123; CAA66805.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

JC6568; JC6568.

3D structure databases

PDB

2BL9; X-ray; 1.90 A; A=1-238.	[ExPASy / RCSB / EBI]
2BLA; X-ray; 2.50 A; A=1-238.	[ExPASy / RCSB / EBI]
2BLB; X-ray; 3.00 A; A=1-238.	[ExPASy / RCSB / EBI]
2BLC; X-ray; 2.25 A; A=1-238.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

2BL9; -.
2BLA; -.
2BLB; -.
2BLC; -.

SMR

O02604; 338-623.

ModBase

O02604.

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; Repeat; Transferase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 623`	`623`	`Bifunctional dihydrofolate reductase-thymidylate synthase.`	`PRO_0000186351`
`DOMAIN`	`9 237`	`229`	`DHFR.`
`REPEAT`	`88 91`	`4`	`1.`
`REPEAT`	`94 97`	`4`	`2.`
`REPEAT`	`100 103`	`4`	`3.`
`REGION`	`88 103`	`16`	`3 X 4 AA repeats of G-G-D-N.`
`REGION`	`337 623`	`287`	`Thymidylate synthase.`
`ACT_SITE`	`505 505`		`By similarity.`
`VARIANT`	`58 58`	`1`	`S -> R (in the pyrimethamine-resistant isolates BUR-98 and BUR-151).`
`VARIANT`	`117 117`	`1`	`S -> N (in the pyrimethamine-resistant isolates BUR-98 and BUR-151).`
`HELIX`	`4 7`	`4`
`STRAND`	`10 19`	`10`
`STRAND`	`23 26`	`4`
`STRAND`	`38 41`	`4`
`STRAND`	`46 48`	`3`
`HELIX`	`51 62`	`12`
`HELIX`	`66 68`	`3`
`HELIX`	`69 83`	`15`
`STRAND`	`109 114`	`6`
`HELIX`	`115 119`	`5`
`HELIX`	`123 125`	`3`
`STRAND`	`131 136`	`6`
`TURN`	`142 144`	`3`
`STRAND`	`150 153`	`4`
`HELIX`	`155 163`	`9`
`STRAND`	`170 174`	`5`
`HELIX`	`176 184`	`9`
`STRAND`	`189 200`	`12`
`STRAND`	`203 205`	`3`
`HELIX`	`211 213`	`3`
`STRAND`	`214 219`	`6`
`STRAND`	`223 225`	`3`
`STRAND`	`228 237`	`10`

Sequence information

Length: 623 AA [This is the length of the unprocessed precursor]

Molecular weight: 71057 Da [This is the MW of the unprocessed precursor]

CRC64: 3E6E958F04FB5828 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MEDLSDVFDI YAICACCKVA PTSEGTKNEP FSPRTFRGLG NKGTLPWKCN SVDMKYFSSV 

        70         80         90        100        110        120 
TTYVDESKYE KLKWKRERYL RMEASQGGGD NTSGGDNTHG GDNADKLQNV VVMGRSSWES 

       130        140        150        160        170        180 
IPKQYKPLPN RINVVLSKTL TKEDVKEKVF IIDSIDDLLL LLKKLKYYKC FIIGGAQVYR 

       190        200        210        220        230        240 
ECLSRNLIKQ IYFTRINGAY PCDVFFPEFD ESQFRVTSVS EVYNSKGTTL DFLVYSKVGG 

       250        260        270        280        290        300 
GVDGGASNGS TATALRRTAM RSTAMRRNVA PRTAAPPMGP HSRANGERAP PRARARRTTP 

       310        320        330        340        350        360 
RQRKTTSCTS ALTTKWGRKT RSTCKILKFT TASRLMQHPE YQYLGIIYDI IMNGNKQGDR 

       370        380        390        400        410        420 
TGVGVMSNFG YMMKFNLSEY FPLLTTKKLF LRGIIEELLW FIRGETNGNT LLNKNVRIWE 

       430        440        450        460        470        480 
ANGTREFLDN RKLFHREVND LGPIYGFQWR HFGAEYTNMH DNYEDKGVDQ LKNVIHLIKN 

       490        500        510        520        530        540 
EPTSRRIILC AWNVKDLDQM ALPPCHILCQ FYVFDGKLSC IMYQRSCDLG LGVPFNIASY 

       550        560        570        580        590        600 
SIFTHMIAQV CNLQPAQFIH ILGNAHVYNN HVDSLKVQLN RIPYPFPTLK LNPEVKNIED 

       610        620 
FTISDFTIEN YVHHDKITME MAA

O02604 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