Reviewed, UniProtKB/Swiss-Prot P45350 (DRTS_DAUCA)

Names and origin

Protein names	Recommended name:     Bifunctional dihydrofolate reductase-thymidylate synthase       Short name=DHFR-TS Including the following 2 domains:     1- Recommended name:             Dihydrofolate reductase               EC=1.5.1.3     2- Recommended name:             Thymidylate synthase               EC=2.1.1.45
Organism	Daucus carota (Carrot)
Taxonomic identifier	4039 [NCBI]
Taxonomic lineage	Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › asterids › campanulids › Apiales › Apiaceae › Apioideae › Scandiceae › Daucinae › Daucus

Protein attributes

Sequence length	528 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Catalytic activity	5,6,7,8-tetrahydrofolate + NADP+ = 7,8-dihydrofolate + NADPH. 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.
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	dTMP biosynthetic process Inferred from electronic annotation. Source: InterPro glycine biosynthetic process Inferred from electronic annotation. Source: InterPro one-carbon compound metabolic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	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 – 528	528	Bifunctional dihydrofolate reductase-thymidylate synthase		PRO_0000186357
Regions
	Domain	23 – 200	178	DHFR
	Region	202 – 528	327	Thymidylate synthase
Sites
	Active site	409	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	P45350-1 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: 8BE07C221A546A56	FASTA	528	59,259
	10 20 30 40 50 60 MASELLANPT NGSGITRPDP QRTYQVVVAA TQNMGIGKDG KLPWRLPSDM KFFKDVTMTT 70 80 90 100 110 120 SDPLKRNAVI MGRKTWESIP IQHRPLPGRL NVVLTRSGSF DIATVENVVI CGSMISALEL 130 140 150 160 170 180 LAGSPYCVSV EKVFVIGGGQ IYREALNAPG CDAVHITEIE EHIECDTFIP LLDESVFQPW 190 200 210 220 230 240 YSSFPLVENK IRYCFTTYVR VRNSVAELTS QTNGCSSDSK SDSGNFEIQN FSFLPKTVFE 250 260 270 280 290 300 KHEEYLYLGL VENIISNGVT KNDRTRTGTV SIFGCQMRFN LRKSFPLLTT KKVFWRGVVE 310 320 330 340 350 360 ELLWFISGST NAKILKEKGV NIWEGNGSRE YLDSIGLTDR EEGDLGPIYG FQWRHFGARY 370 380 390 400 410 420 TDMHADYSGQ GFDQLLDVIS KIKNNPDDRR IIQSAWNPSD LRLMALPPCH MFAQFYVANG 430 440 450 460 470 480 ELSCQMYQRS ADMGLGVPFN IAAYALLTCM IAHVCDLVPG DFVHSIGDAH VYSNHLSDLF 490 500 510 520 ETSFRMLPKT FPVLKINSGE KDIDSFEAAD FKLIGYDPHQ KIEMKMAV

References

[1]

"Molecular cloning and analysis of a cDNA coding for the bifunctional dihydrofolate reductase-thymidylate synthase of Daucus carota." Luo M., Piffanelli P., Rastelli L., Cella R. Plant Mol. Biol. 22:427-435(1993) [PubMed: 8329682] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Lunga di Amsterdam.

Cross-references

Sequence databases
EMBLGenBankDDBJ	Z17306 mRNA. Translation: CAA78954.1.
PIR	S35272.
3D structure databases
HSSP	HSSP built from PDB template 1JU6 based on UniProtKB P04818.
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.5.1.3. 1081. 2.1.1.45. 1081.
Family and domain databases
InterPro	IPR012262. DHFR-TS. IPR001796. DHFR_reg. IPR017925. Dihydrofolate_reductase_CS. IPR000398. Thymidylat_synth_C. [Graphical view]
Gene3D	G3DSA:3.30.572.10. Thymidylat_synth_C. 1 hit.
PANTHER	PTHR11549:SF2. Thymidylat_synth_C. 1 hit.
Pfam	PF00186. DHFR_1. 1 hit. PF00303. Thymidylat_synt. 1 hit. [Graphical view]
PIRSF	PIRSF000389. DHFR-TS. 1 hit.
PRINTS	PR00108. THYMDSNTHASE.
ProDom	PD001180. Thymidylat_synth. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR03284. thym_sym. 1 hit.
PROSITE	PS00075. DHFR_1. 1 hit. PS51330. DHFR_2. 1 hit. PS00091. THYMIDYLATE_SYNTHASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DRTS_DAUCA

Accession

Primary (citable) accession number: P45350

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	June 16, 2009
This is version 52 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)