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Q05763

- DRTS2_ARATH

UniProt

Q05763 - DRTS2_ARATH

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Protein

Bifunctional dihydrofolate reductase-thymidylate synthase 2

Gene

THY-2

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript 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 sitei69 – 691Substrate; via carbonyl oxygenBy similarity
Binding sitei71 – 711NADP; via amide nitrogen and carbonyl oxygenBy similarity
Binding sitei91 – 911SubstrateBy similarity
Binding sitei178 – 1781Substrate; via carbonyl oxygenBy similarity
Binding sitei199 – 1991SubstrateBy similarity
Binding sitei302 – 3021dUMPBy similarity
Active sitei447 – 4471By similarity
Binding sitei448 – 4481dUMPBy similarity
Binding sitei478 – 4781dUMPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi77 – 837NADPBy similarity
Nucleotide bindingi115 – 1173NADPBy similarity
Nucleotide bindingi136 – 1394NADPBy similarity
Nucleotide bindingi179 – 1868NADPBy similarity
Nucleotide bindingi466 – 4705dUMPBy similarity
Nucleotide bindingi508 – 5103dUMPBy 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:AT4G34570-MONOMER.
UniPathwayiUPA00077; UER00158.

Names & Taxonomyi

Protein namesi
Recommended name:
Bifunctional dihydrofolate reductase-thymidylate synthase 2
Short name:
DHFR-TS 2
Including the following 2 domains:
Dihydrofolate reductase (EC:1.5.1.3)
Thymidylate synthase (EC:2.1.1.45)
Gene namesi
Name:THY-2
Ordered Locus Names:At4g34570
ORF Names:T4L20.150
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 4

Organism-specific databases

TAIRiAT4G34570.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 565565Bifunctional dihydrofolate reductase-thymidylate synthase 2PRO_0000186356Add
BLAST

Proteomic databases

PaxDbiQ05763.
PRIDEiQ05763.

Expressioni

Gene expression databases

GenevestigatoriQ05763.

Interactioni

Subunit structurei

Heterodimer or homodimer.By similarity

Protein-protein interaction databases

STRINGi3702.AT4G34570.1-P.

Structurei

3D structure databases

ProteinModelPortaliQ05763.
SMRiQ05763. Positions 68-565.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini65 – 242178DHFRAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni245 – 28036HingeAdd
BLAST
Regioni281 – 565285Thymidylate 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.
InParanoidiQ05763.
KOiK13998.
OMAiLTCMIAQ.
PhylomeDBiQ05763.

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.

Q05763-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MRCLQNSAKT LPLAFKSALL PLSQRWFCKF SPKPSSLTNI FKVSISTMAN
60 70 80 90 100
TLNGNVIMTS KPQSTYQVVV AATKEMGIGK DGKLPWNLPT DLKFFKDLTL
110 120 130 140 150
STSDSAKKNA VVMGRKTWES IPKKYRPLSG RLNVVLSRSS GFDIANTENV
160 170 180 190 200
VTCSSIDSAL DLLAAPPFSL SIEKVFVIGG GDILREALNK PSCEAIHITE
210 220 230 240 250
IDTSIDCDTF IPTVDTSAYQ PWCSSFPICE NGLRFSFTTH VRVKSSSAGE
260 270 280 290 300
ASDESDGSKV LQVDWKKFSS VLPKMIFDRH EEYLYLNLVK EIISNGNLKD
310 320 330 340 350
DRTGTGTLSK FGCQMKFNLR RNFPLLTTKR VFWRGVVEEL LWFISGSTNA
360 370 380 390 400
KVLQEKGIRI WDGNASRAYL DGIGLTEREE GDLGPVYGFQ WRHFGAKYTD
410 420 430 440 450
MHADYTGQGF DQLLDVINKI KNNPDDRRII MSAWNPSDLK LMALPPCHMF
460 470 480 490 500
AQFYVANGEL SCQMYQRSAD MGLGVPFNIA SYSLLTCILA HVCDLVPGDF
510 520 530 540 550
IHVIGDAHVY KNHVRPLQEQ LENPPKPFPV LKINPEKKDI DSFVADDFEL
560
IGYDPHKKID MKMAV
Length:565
Mass (Da):63,209
Last modified:June 26, 2007 - v2
Checksum:iC442A1402A591DD9
GO

Sequence cautioni

The sequence AAA32789.1 differs from that shown. Reason: Erroneous gene model prediction.
The sequence CAA18836.1 differs from that shown. Reason: Erroneous gene model prediction.
The sequence CAB80174.1 differs from that shown. Reason: Erroneous gene model prediction.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L08594 Genomic DNA. Translation: AAA32789.1. Sequence problems.
AL023094 Genomic DNA. Translation: CAA18836.1. Sequence problems.
AL161585 Genomic DNA. Translation: CAB80174.1. Sequence problems.
CP002687 Genomic DNA. Translation: AEE86394.1.
AK227728 mRNA. Translation: BAE99713.1.
BT003159 mRNA. Translation: AAO24591.1.
PIRiT05277.
RefSeqiNP_195183.2. NM_119623.4.
UniGeneiAt.31491.

Genome annotation databases

EnsemblPlantsiAT4G34570.1; AT4G34570.1; AT4G34570.
GeneIDi829609.
KEGGiath:AT4G34570.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L08594 Genomic DNA. Translation: AAA32789.1 . Sequence problems.
AL023094 Genomic DNA. Translation: CAA18836.1 . Sequence problems.
AL161585 Genomic DNA. Translation: CAB80174.1 . Sequence problems.
CP002687 Genomic DNA. Translation: AEE86394.1 .
AK227728 mRNA. Translation: BAE99713.1 .
BT003159 mRNA. Translation: AAO24591.1 .
PIRi T05277.
RefSeqi NP_195183.2. NM_119623.4.
UniGenei At.31491.

3D structure databases

ProteinModelPortali Q05763.
SMRi Q05763. Positions 68-565.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 3702.AT4G34570.1-P.

Proteomic databases

PaxDbi Q05763.
PRIDEi Q05763.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT4G34570.1 ; AT4G34570.1 ; AT4G34570 .
GeneIDi 829609.
KEGGi ath:AT4G34570.

Organism-specific databases

TAIRi AT4G34570.

Phylogenomic databases

eggNOGi COG0262.
HOGENOMi HOG000257901.
InParanoidi Q05763.
KOi K13998.
OMAi LTCMIAQ.
PhylomeDBi Q05763.

Enzyme and pathway databases

UniPathwayi UPA00077 ; UER00158 .
BioCyci ARA:AT4G34570-MONOMER.

Gene expression databases

Genevestigatori Q05763.

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. "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
    Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B.
    , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
    Nature 402:769-777(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. "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
    Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.
    , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
    Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  5. "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] OF 48-565.
    Strain: cv. Columbia.

Entry informationi

Entry nameiDRTS2_ARATH
AccessioniPrimary (citable) accession number: Q05763
Secondary accession number(s): Q0WT35
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: June 26, 2007
Last modified: October 1, 2014
This is version 119 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