NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=427;
DOI=10.1016/0166-6851(95)00059-A; PubMed=8538681 [NCBI, ExPASy, EBI, Israel, Japan]
Gamarro F., Yu P.L., Zhao J., Edman U., Greene P.J., Santi D.;
"Trypanosoma brucei dihydrofolate reductase-thymidylate synthase: gene isolation and expression and characterization of the enzyme.";
Mol. Biochem. Parasitol. 72:11-22(1995).

Comments

CATALYTIC ACTIVITY: 5,10-methylenetetrahydrofolate + dUMP = dihydrofolate + dTMP.
CATALYTIC ACTIVITY: 5,6,7,8-tetrahydrofolate + NADP⁺ = 7,8-dihydrofolate + NADPH.
PATHWAY: Pyrimidine metabolism; dTTP biosynthesis .
PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis; tetrahydrofolate from dihydrofolate: step 1/1 .
SUBUNIT: Homodimer (By similarity).
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

U20781; AAA91362.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

P13100; 1CI7. [HSSP ENTRY / PDB]

ModBase

Q27783.

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

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

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 527`	`527`	`Bifunctional dihydrofolate reductase-thymidylate synthase.`	`PRO_0000186353`
`DOMAIN`	`28 238`	`211`	`DHFR.`
`REGION`	`243 527`	`285`	`Thymidylate synthase.`
`ACT_SITE`	`409 409`		`By similarity.`

Sequence information

Length: 527 AA [This is the length of the unprocessed precursor]

Molecular weight: 58805 Da [This is the MW of the unprocessed precursor]

CRC64: 39982FC553BF7601 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MLSLTRILRK KIPVHELAGK ISRPPLRPFS VVVASDEKGG IGDGGTIPWE IPEDMQYFRR 

        70         80         90        100        110        120 
VTTNLRGKNV KPSPSKRNAV VMGRKTWDSL PPKFRPLSNR LNVVLSRSAT KEQLLAGIPD 

       130        140        150        160        170        180 
PIKRAEAAND VVAVNGGLED ALRMLVSKEH TSSIETVFCI GGGTIYKQAL CAPCVNVLQA 

       190        200        210        220        230        240 
IHRTVVRPAS NSCSVFFDIP AAGTKTPEGL ELVRESITDE RVSTGAGGKK YQFEKLVPRN 

       250        260        270        280        290        300 
SEEEQYLNLV GRIIDEGCTK CDRTGVGTRS LFGAQMRFSL RNNRLPLLTT KRVFWRGVCE 

       310        320        330        340        350        360 
ELLWFLRGET NAKLLSDKGI HIWDGNGSRA FLDSRGLTDY DEMDLGPVYG FQWRHFGADY 

       370        380        390        400        410        420 
ISCKVDSEGK GVDQIANIVK SLIENPDDRR MICTAWNPAA LPRMALPPCH MMAQFYVSNG 

       430        440        450        460        470        480 
ELSCMLYQRS CDMGLGVPFN IASYALLTFL MAKASGLRPG ELVHTLGDAH VYSNHVEPCR 

       490        500        510        520 
KQLKRVPRPF PFIVFKQDKE FLEDFQESDI EVIDYSPYPV ISMEMAV

Q27783 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