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Q05762

- DRTS1_ARATH

UniProt

Q05762 - DRTS1_ARATH

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Protein

Bifunctional dihydrofolate reductase-thymidylate synthase 1

Gene

THY-1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.

Catalytic activityi

5,6,7,8-tetrahydrofolate + NADP+ = 7,8-dihydrofolate + NADPH.
5,10-methylenetetrahydrofolate + dUMP = dihydrofolate + dTMP.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei25 – 251Substrate; via carbonyl oxygenBy similarity
Binding sitei27 – 271NADP; via amide nitrogen and carbonyl oxygenBy similarity
Binding sitei47 – 471SubstrateBy similarity
Binding sitei134 – 1341Substrate; via carbonyl oxygenBy similarity
Binding sitei155 – 1551SubstrateBy similarity
Binding sitei256 – 2561dUMPBy similarity
Active sitei401 – 4011By similarity
Binding sitei402 – 4021dUMPBy similarity
Binding sitei432 – 4321dUMPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi33 – 397NADPBy similarity
Nucleotide bindingi71 – 733NADPBy similarity
Nucleotide bindingi92 – 954NADPBy similarity
Nucleotide bindingi135 – 1428NADPBy similarity
Nucleotide bindingi420 – 4245dUMPBy similarity
Nucleotide bindingi462 – 4643dUMPBy similarity

GO - Molecular functioni

  1. dihydrofolate reductase activity Source: TAIR
  2. thymidylate synthase activity Source: TAIR

GO - Biological processi

  1. 10-formyltetrahydrofolate biosynthetic process Source: TAIR
  2. dTMP biosynthetic process Source: InterPro
  3. glycine biosynthetic process Source: InterPro
  4. one-carbon metabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Oxidoreductase, Transferase

Keywords - Biological processi

Nucleotide biosynthesis, One-carbon metabolism

Keywords - Ligandi

NADP

Enzyme and pathway databases

BioCyciARA:AT2G16370-MONOMER.
UniPathwayiUPA00077; UER00158.

Names & Taxonomyi

Protein namesi
Recommended name:
Bifunctional dihydrofolate reductase-thymidylate synthase 1
Short name:
DHFR-TS 1
Including the following 2 domains:
Dihydrofolate reductase (EC:1.5.1.3)
Thymidylate synthase (EC:2.1.1.45)
Gene namesi
Name:THY-1
Ordered Locus Names:At2g16370
ORF Names:F16F14.13
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 2

Organism-specific databases

TAIRiAT2G16370.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: TAIR
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 519518Bifunctional dihydrofolate reductase-thymidylate synthase 1PRO_0000186355Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiQ05762.
PRIDEiQ05762.

Expressioni

Gene expression databases

GenevestigatoriQ05762.

Interactioni

Subunit structurei

Heterodimer or homodimer.By similarity

Protein-protein interaction databases

BioGridi1492. 1 interaction.
IntActiQ05762. 1 interaction.
STRINGi3702.AT2G16370.1-P.

Structurei

3D structure databases

ProteinModelPortaliQ05762.
SMRiQ05762. Positions 24-519.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini21 – 198178DHFRAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni201 – 23434HingeAdd
BLAST
Regioni235 – 519285Thymidylate synthaseAdd
BLAST

Sequence similaritiesi

In the N-terminal section; belongs to the dihydrofolate reductase family.Curated
In the C-terminal section; belongs to the thymidylate synthase family.Curated

Phylogenomic databases

eggNOGiCOG0262.
HOGENOMiHOG000257901.
InParanoidiQ05762.
KOiK13998.
OMAiVESNIRH.
PhylomeDBiQ05762.

Family and domain databases

Gene3Di3.30.572.10. 1 hit.
3.40.430.10. 1 hit.
HAMAPiMF_00008. Thymidy_synth_bact.
InterProiIPR024072. 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]
PfamiPF00186. DHFR_1. 1 hit.
PF00303. Thymidylat_synt. 1 hit.
[Graphical view]
PIRSFiPIRSF000389. DHFR-TS. 1 hit.
PRINTSiPR00108. THYMDSNTHASE.
SUPFAMiSSF53597. SSF53597. 1 hit.
SSF55831. SSF55831. 1 hit.
TIGRFAMsiTIGR03284. thym_sym. 1 hit.
PROSITEiPS00075. DHFR_1. 1 hit.
PS51330. DHFR_2. 1 hit.
PS00091. THYMIDYLATE_SYNTHASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q05762-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MATTTLNDSV TTTLASEPQR TYQVVVAATK EMGIGKDGKL PWNLPTDLKF
60 70 80 90 100
FKDITLTTSD SSKKNAVVMG RKTWESIPIK YRPLSGRLNV VLTRSGGFDI
110 120 130 140 150
ANTENVVTCS SVDSALDLLA APPYCLSIER VFVIGGGDIL REALNRPSCD
160 170 180 190 200
AIHLTEIDTS VDCDTFIPAI DTSVYQPWSS SFPVTENGLR FCFTTFVRVK
210 220 230 240 250
SSADESSDES NGSQSLQFDG KKFLFLPKMV FDQHEEFLYL NMVEDIISNG
260 270 280 290 300
NVKNDRTGTG TLSKFGCQMK FNLRRSFPLL TTKRVFWRGV VEELLWFISG
310 320 330 340 350
STNAKVLQEK GIHIWDGNAS REYLDGIGLT EREEGDLGPV YGFQWRHFGA
360 370 380 390 400
KYTDMHADYT GQGFDQLVDV IDKIKNNPDD RRIIMSAWNP SDLKLMALPP
410 420 430 440 450
CHMFAQFYVA EGELSCQMYQ RSADMGLGVP FNIASYSLLT CMLAHVCDLV
460 470 480 490 500
PGDFIHVLGD AHVYKTHVRP LQEQLLNLPK PFPVMKINPE KKQIDSFVAS
510
DFDLTGYDPH KKIEMKMAV
Length:519
Mass (Da):58,143
Last modified:May 27, 2002 - v2
Checksum:iB5EB36A3A936580F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti120 – 1201A → R in AAA32788. (PubMed:8374616)Curated
Sequence conflicti478 – 4781L → P in AAA32788. (PubMed:8374616)Curated
Sequence conflicti485 – 4851M → L in AAA32788. (PubMed:8374616)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
PIRiE84539.
RefSeqiNP_179230.1. NM_127191.3.
UniGeneiAt.27124.

Genome annotation databases

EnsemblPlantsiAT2G16370.1; AT2G16370.1; AT2G16370.
GeneIDi816134.
KEGGiath:AT2G16370.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
PIRi E84539.
RefSeqi NP_179230.1. NM_127191.3.
UniGenei At.27124.

3D structure databases

ProteinModelPortali Q05762.
SMRi Q05762. Positions 24-519.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 1492. 1 interaction.
IntActi Q05762. 1 interaction.
STRINGi 3702.AT2G16370.1-P.

Proteomic databases

PaxDbi Q05762.
PRIDEi Q05762.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT2G16370.1 ; AT2G16370.1 ; AT2G16370 .
GeneIDi 816134.
KEGGi ath:AT2G16370.

Organism-specific databases

TAIRi AT2G16370.

Phylogenomic databases

eggNOGi COG0262.
HOGENOMi HOG000257901.
InParanoidi Q05762.
KOi K13998.
OMAi VESNIRH.
PhylomeDBi Q05762.

Enzyme and pathway databases

UniPathwayi UPA00077 ; UER00158 .
BioCyci ARA:AT2G16370-MONOMER.

Miscellaneous databases

PROi Q05762.

Gene expression databases

Genevestigatori Q05762.

Family and domain databases

Gene3Di 3.30.572.10. 1 hit.
3.40.430.10. 1 hit.
HAMAPi MF_00008. Thymidy_synth_bact.
InterProi IPR024072. 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 ]
Pfami PF00186. DHFR_1. 1 hit.
PF00303. Thymidylat_synt. 1 hit.
[Graphical view ]
PIRSFi PIRSF000389. DHFR-TS. 1 hit.
PRINTSi PR00108. THYMDSNTHASE.
SUPFAMi SSF53597. SSF53597. 1 hit.
SSF55831. SSF55831. 1 hit.
TIGRFAMsi TIGR03284. thym_sym. 1 hit.
PROSITEi PS00075. DHFR_1. 1 hit.
PS51330. DHFR_2. 1 hit.
PS00091. THYMIDYLATE_SYNTHASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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.
    , 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].

Entry informationi

Entry nameiDRTS1_ARATH
AccessioniPrimary (citable) accession number: Q05762
Secondary accession number(s): Q9SIW4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: May 27, 2002
Last modified: October 1, 2014
This is version 121 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3