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P45350 (DRTS_DAUCA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Bifunctional dihydrofolate reductase-thymidylate synthase

Short name=DHFR-TS

Including the following 2 domains:

  1. Dihydrofolate reductase
    EC=1.5.1.3
  2. Thymidylate synthase
    EC=2.1.1.45
OrganismDaucus carota (Carrot)
Taxonomic identifier4039 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridscampanulidsApialesApiaceaeApioideaeScandiceaeDaucinaeDaucus

Protein attributes

Sequence length528 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Bifunctional enzyme. Involved in de novo dTMP biosynthesis. Key enzyme in folate metabolism. Can play two different roles depending on the source of dihydrofolate: de novo synthesis of tetrahydrofolate or recycling of the dihydrofolate released as one of the end products of the TS catalyzed reaction. Catalyzes an essential reaction for de novo glycine and purine synthesis, DNA precursor synthesis, and for the conversion of dUMP to dTMP By similarity. HAMAP-Rule MF_00008

Catalytic activity

5,6,7,8-tetrahydrofolate + NADP+ = 7,8-dihydrofolate + NADPH. HAMAP-Rule MF_00008

5,10-methylenetetrahydrofolate + dUMP = dihydrofolate + dTMP. HAMAP-Rule MF_00008

Pathway

Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. HAMAP-Rule MF_00008

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 528528Bifunctional dihydrofolate reductase-thymidylate synthase HAMAP-Rule MF_00008
PRO_0000186357

Regions

Domain23 – 200178DHFR
Nucleotide binding35 – 417NADP By similarity
Nucleotide binding73 – 753NADP By similarity
Nucleotide binding94 – 974NADP By similarity
Nucleotide binding137 – 1448NADP By similarity
Nucleotide binding428 – 4325dUMP By similarity
Nucleotide binding470 – 4723dUMP By similarity
Region202 – 528327Thymidylate synthase HAMAP-Rule MF_00008

Sites

Active site4091 By similarity
Binding site271Substrate; via carbonyl oxygen By similarity
Binding site291NADP; via amide nitrogen and carbonyl oxygen By similarity
Binding site491Substrate By similarity
Binding site1361Substrate; via carbonyl oxygen By similarity
Binding site1421Substrate By similarity
Binding site1571Substrate By similarity
Binding site2641dUMP By similarity
Binding site4101dUMP By similarity
Binding site4401dUMP By similarity

Sequences

Sequence LengthMass (Da)Tools
P45350 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 8BE07C221A546A56

FASTA52859,259
        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 

« Hide

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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. Lunga di Amsterdam.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z17306 mRNA. Translation: CAA78954.1.
PIRS35272.

3D structure databases

ProteinModelPortalP45350.
SMRP45350. Positions 242-528.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00077; UER00158.

Family and domain databases

Gene3D3.30.572.10. 1 hit.
3.40.430.10. 1 hit.
HAMAPMF_00008. Thymidy_synth_bact.
InterProIPR024072. DHFR-like_dom.
IPR012262. DHFR-TS.
IPR017925. DHFR_CS.
IPR001796. DHFR_dom.
IPR023451. Thymidate_synth/dCMP_Mease.
IPR000398. Thymidylate_synthase.
IPR020940. Thymidylate_synthase_AS.
[Graphical view]
PfamPF00186. DHFR_1. 1 hit.
PF00303. Thymidylat_synt. 1 hit.
[Graphical view]
PIRSFPIRSF000389. DHFR-TS. 1 hit.
PRINTSPR00108. THYMDSNTHASE.
SUPFAMSSF53597. SSF53597. 1 hit.
SSF55831. SSF55831. 1 hit.
TIGRFAMsTIGR03284. thym_sym. 1 hit.
PROSITEPS00075. DHFR_1. 1 hit.
PS51330. DHFR_2. 1 hit.
PS00091. THYMIDYLATE_SYNTHASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDRTS_DAUCA
AccessionPrimary (citable) accession number: P45350
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: February 19, 2014
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways