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Q05762 (DRTS1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 118. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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 1

Short name=DHFR-TS 1

Including the following 2 domains:

  1. Dihydrofolate reductase
    EC=1.5.1.3
  2. Thymidylate synthase
    EC=2.1.1.45
Gene names
Name:THY-1
Ordered Locus Names:At2g16370
ORF Names:F16F14.13
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length519 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein 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. 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

Subunit structure

Heterodimer or homodimer By similarity. 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

Initiator methionine11Removed Ref.5
Chain2 – 519518Bifunctional dihydrofolate reductase-thymidylate synthase 1 HAMAP-Rule MF_00008
PRO_0000186355

Regions

Domain21 – 198178DHFR
Nucleotide binding33 – 397NADP By similarity
Nucleotide binding71 – 733NADP By similarity
Nucleotide binding92 – 954NADP By similarity
Nucleotide binding135 – 1428NADP By similarity
Nucleotide binding420 – 4245dUMP By similarity
Nucleotide binding462 – 4643dUMP By similarity
Region201 – 23434Hinge HAMAP-Rule MF_00008
Region235 – 519285Thymidylate synthase HAMAP-Rule MF_00008

Sites

Active site4011 By similarity
Binding site251Substrate; via carbonyl oxygen By similarity
Binding site271NADP; via amide nitrogen and carbonyl oxygen By similarity
Binding site471Substrate By similarity
Binding site1341Substrate; via carbonyl oxygen By similarity
Binding site1551Substrate By similarity
Binding site2561dUMP By similarity
Binding site4021dUMP By similarity
Binding site4321dUMP By similarity

Amino acid modifications

Modified residue21N-acetylalanine Ref.5

Experimental info

Sequence conflict1201A → R in AAA32788. Ref.1
Sequence conflict4781L → P in AAA32788. Ref.1
Sequence conflict4851M → L in AAA32788. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q05762 [UniParc].

Last modified May 27, 2002. Version 2.
Checksum: B5EB36A3A936580F

FASTA51958,143
        10         20         30         40         50         60 
MATTTLNDSV TTTLASEPQR TYQVVVAATK EMGIGKDGKL PWNLPTDLKF FKDITLTTSD 

        70         80         90        100        110        120 
SSKKNAVVMG RKTWESIPIK YRPLSGRLNV VLTRSGGFDI ANTENVVTCS SVDSALDLLA 

       130        140        150        160        170        180 
APPYCLSIER VFVIGGGDIL REALNRPSCD AIHLTEIDTS VDCDTFIPAI DTSVYQPWSS 

       190        200        210        220        230        240 
SFPVTENGLR FCFTTFVRVK SSADESSDES NGSQSLQFDG KKFLFLPKMV FDQHEEFLYL 

       250        260        270        280        290        300 
NMVEDIISNG NVKNDRTGTG TLSKFGCQMK FNLRRSFPLL TTKRVFWRGV VEELLWFISG 

       310        320        330        340        350        360 
STNAKVLQEK GIHIWDGNAS REYLDGIGLT EREEGDLGPV YGFQWRHFGA KYTDMHADYT 

       370        380        390        400        410        420 
GQGFDQLVDV IDKIKNNPDD RRIIMSAWNP SDLKLMALPP CHMFAQFYVA EGELSCQMYQ 

       430        440        450        460        470        480 
RSADMGLGVP FNIASYSLLT CMLAHVCDLV PGDFIHVLGD AHVYKTHVRP LQEQLLNLPK 

       490        500        510 
PFPVMKINPE KKQIDSFVAS DFDLTGYDPH KKIEMKMAV 

« Hide

References

« Hide 'large scale' references
[1]"The origin of the bifunctional dihydrofolate reductase-thymidylate synthase isogenes of Arabidopsis thaliana."
Lazar G., Zhang H., Goodman H.M.
Plant J. 3:657-668(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. Landsberg erecta.
[2]"Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana."
Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S., Cronin L.A. expand/collapse author list , Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.
Nature 402:761-768(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[3]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[4]"Empirical analysis of transcriptional activity in the Arabidopsis genome."
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. expand/collapse author list , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[5]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L08593 mRNA. Translation: AAA32788.1.
AC007047 Genomic DNA. Translation: AAD22302.1.
CP002685 Genomic DNA. Translation: AEC06489.1.
AY063968 mRNA. Translation: AAL36324.1.
AY114032 mRNA. Translation: AAM45080.1.
PIRE84539.
RefSeqNP_179230.1. NM_127191.3.
UniGeneAt.27124.

3D structure databases

ProteinModelPortalQ05762.
SMRQ05762. Positions 24-519.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid1492. 1 interaction.
IntActQ05762. 1 interaction.
STRING3702.AT2G16370.1-P.

Proteomic databases

PaxDbQ05762.
PRIDEQ05762.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT2G16370.1; AT2G16370.1; AT2G16370.
GeneID816134.
KEGGath:AT2G16370.

Organism-specific databases

TAIRAT2G16370.

Phylogenomic databases

eggNOGCOG0262.
HOGENOMHOG000257901.
InParanoidQ05762.
KOK13998.
OMAVESNIRH.
PhylomeDBQ05762.
ProtClustDBCLSN2683596.

Enzyme and pathway databases

BioCycARA:AT2G16370-MONOMER.
UniPathwayUPA00077; UER00158.

Gene expression databases

GenevestigatorQ05762.

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...

Other

PROQ05762.

Entry information

Entry nameDRTS1_ARATH
AccessionPrimary (citable) accession number: Q05762
Secondary accession number(s): Q9SIW4
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: May 27, 2002
Last modified: March 19, 2014
This is version 118 of the entry and version 2 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

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names