P46103 (DRTS_PLAVN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Bifunctional dihydrofolate reductase-thymidylate synthase Short name=DHFR-TS Including the following 2 domains: Dihydrofolate reductase EC=1.5.1.3 Thymidylate synthase EC=2.1.1.45
Organism	Plasmodium vinckei
Taxonomic identifier	5860 [NCBI]
Taxonomic lineage	cellular organisms › Eukaryota › Alveolata › Apicomplexa › Aconoidasida › Haemosporida › Plasmodium › Plasmodium (Vinckeia)

Protein attributes

Sequence length	182 AA.
Sequence status	Fragment.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Bifunctional enzyme. Involved in de novo dTMP biosynthesis. Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, DNA precursor synthesis, and for the conversion of dUMP to dTMP By similarity.
Catalytic activity	5,6,7,8-tetrahydrofolate + NADP+ = 7,8-dihydrofolate + NADPH. 5,10-methylenetetrahydrofolate + dUMP = dihydrofolate + dTMP.
Pathway	Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1.
Subunit structure	Homodimer By similarity.
Sequence similarities	In the N-terminal section; belongs to the dihydrofolate reductase family. In the C-terminal section; belongs to the thymidylate synthase family. Contains 1 DHFR (dihydrofolate reductase) domain.

Ontologies

Keywords
Biological process	Nucleotide biosynthesis One-carbon metabolism
Ligand	NADP
Molecular function	Methyltransferase Oxidoreductase Transferase
Technical term	Multifunctional enzyme
Gene Ontology (GO)
Biological_process	glycine biosynthetic process Inferred from electronic annotation. Source: InterPro nucleotide biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW one-carbon metabolic process Inferred from electronic annotation. Source: UniProtKB-KW tetrahydrofolate biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Molecular_function	NADP binding Inferred from electronic annotation. Source: InterPro dihydrofolate reductase activity Inferred from electronic annotation. Source: EC thymidylate synthase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	‹1 – ›182	›182	Bifunctional dihydrofolate reductase-thymidylate synthase		PRO_0000186350
Regions
	Domain	‹1 – ›182	›182	DHFR
	Nucleotide binding	25 – 31	7	NADP By similarity
	Nucleotide binding	93 – 95	3	NADP By similarity
	Nucleotide binding	114 – 117	4	NADP By similarity
	Nucleotide binding	155 – 162	8	NADP By similarity
Sites
	Binding site	40	1	Substrate By similarity
	Binding site	154	1	Substrate; via carbonyl oxygen By similarity
	Binding site	160	1	Substrate By similarity
	Binding site	175	1	Substrate By similarity
Experimental info
	Non-terminal residue	1	1
	Non-terminal residue	182	1

Sequences

	Sequence		Length	Mass (Da)
	P46103 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: 33CCD27441763198	FASTA	182	20,925
	10 20 30 40 50 60 AICACCKVLN SNEKASCFSN KTFKGLGNAG GLPWKCNSVD MKHFVSVTSY VNENNYIRLK 70 80 90 100 110 120 WKRDKYIKEN NVKVNTDGIP SIDKLQNIVV MGKTSWESIP SKFKPLENRI NIILSRTLKK 130 140 150 160 170 180 ENLAKEYSNV IIIKSVDELF PILKCIKYYK CFIIGGASVY KEFLDRNLIK KIYFTRINNA YT

References

[1]	"The dihydrofolate reductase domain of rodent malarias: point mutations and pyrimethamine resistance." Cheng Q., Saul A. Mol. Biochem. Parasitol. 65:361-363(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	L28121 Genomic DNA. Translation: AAA29582.1.
3D structure databases
ProteinModelPortal	P46103.
SMR	P46103. Positions 1-181.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Enzyme and pathway databases
UniPathway	UPA00077; UER00158.
Family and domain databases
Gene3D	3.40.430.10. 1 hit.
InterPro	IPR012259. DHFR. IPR024072. DHFR-like_dom. IPR017925. DHFR_CS. IPR001796. DHFR_dom. [Graphical view]
Pfam	PF00186. DHFR_1. 1 hit. [Graphical view]
PRINTS	PR00070. DHFR.
SUPFAM	SSF53597. SSF53597. 1 hit.
PROSITE	PS00075. DHFR_1. 1 hit. PS51330. DHFR_2. 1 hit. PS00091. THYMIDYLATE_SYNTHASE. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DRTS_PLAVN

Accession

Primary (citable) accession number: P46103

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	April 3, 2013
This is version 67 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)