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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, At2g16370, F16F14.13
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.UniRule annotation

Catalytic activityi

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

Pathwayi

Sites

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

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi33 – 397NADP By similarity
Nucleotide bindingi71 – 733NADP By similarity
Nucleotide bindingi92 – 954NADP By similarity
Nucleotide bindingi135 – 1428NADP By similarity
Nucleotide bindingi420 – 4245dUMP By similarity
Nucleotide bindingi462 – 4643dUMP By 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 1UniRule annotationPRO_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.UniRule annotation

Protein-protein interaction databases

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

Structurei

3D structure databases

ProteinModelPortaliQ05762.
SMRiQ05762. Positions 24-519.

Family & Domainsi

Domains and Repeats

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

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni201 – 23434HingeUniRule annotationAdd
BLAST
Regioni235 – 519285Thymidylate synthaseUniRule annotationAdd
BLAST

Sequence similaritiesi

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

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

MATTTLNDSV TTTLASEPQR TYQVVVAATK EMGIGKDGKL PWNLPTDLKF    50
FKDITLTTSD SSKKNAVVMG RKTWESIPIK YRPLSGRLNV VLTRSGGFDI 100
ANTENVVTCS SVDSALDLLA APPYCLSIER VFVIGGGDIL REALNRPSCD 150
AIHLTEIDTS VDCDTFIPAI DTSVYQPWSS SFPVTENGLR FCFTTFVRVK 200
SSADESSDES NGSQSLQFDG KKFLFLPKMV FDQHEEFLYL NMVEDIISNG 250
NVKNDRTGTG TLSKFGCQMK FNLRRSFPLL TTKRVFWRGV VEELLWFISG 300
STNAKVLQEK GIHIWDGNAS REYLDGIGLT EREEGDLGPV YGFQWRHFGA 350
KYTDMHADYT GQGFDQLVDV IDKIKNNPDD RRIIMSAWNP SDLKLMALPP 400
CHMFAQFYVA EGELSCQMYQ RSADMGLGVP FNIASYSLLT CMLAHVCDLV 450
PGDFIHVLGD AHVYKTHVRP LQEQLLNLPK PFPVMKINPE KKQIDSFVAS 500
DFDLTGYDPH KKIEMKMAV 519
Length:519
Mass (Da):58,143
Last modified:May 27, 2002 - v2
Checksum:iB5EB36A3A936580F
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti120 – 1201A → R in AAA32788. 1 Publication
Sequence conflicti478 – 4781L → P in AAA32788. 1 Publication
Sequence conflicti485 – 4851M → L in AAA32788. 1 Publication

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: June 11, 2014
This is version 120 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

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