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Q05763 (DRTS2_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 116. 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 2

Short name=DHFR-TS 2

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-2
Ordered Locus Names:At4g34570
ORF Names:T4L20.150
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length565 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. 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 caution

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 annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 565565Bifunctional dihydrofolate reductase-thymidylate synthase 2 HAMAP-Rule MF_00008
PRO_0000186356

Regions

Domain65 – 242178DHFR
Nucleotide binding77 – 837NADP By similarity
Nucleotide binding115 – 1173NADP By similarity
Nucleotide binding136 – 1394NADP By similarity
Nucleotide binding179 – 1868NADP By similarity
Nucleotide binding466 – 4705dUMP By similarity
Nucleotide binding508 – 5103dUMP By similarity
Region245 – 28036Hinge HAMAP-Rule MF_00008
Region281 – 565285Thymidylate synthase HAMAP-Rule MF_00008

Sites

Active site4471 By similarity
Binding site691Substrate; via carbonyl oxygen By similarity
Binding site711NADP; via amide nitrogen and carbonyl oxygen By similarity
Binding site911Substrate By similarity
Binding site1781Substrate; via carbonyl oxygen By similarity
Binding site1991Substrate By similarity
Binding site3021dUMP By similarity
Binding site4481dUMP By similarity
Binding site4781dUMP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q05763 [UniParc].

Last modified June 26, 2007. Version 2.
Checksum: C442A1402A591DD9

FASTA56563,209
        10         20         30         40         50         60 
MRCLQNSAKT LPLAFKSALL PLSQRWFCKF SPKPSSLTNI FKVSISTMAN TLNGNVIMTS 

        70         80         90        100        110        120 
KPQSTYQVVV AATKEMGIGK DGKLPWNLPT DLKFFKDLTL STSDSAKKNA VVMGRKTWES 

       130        140        150        160        170        180 
IPKKYRPLSG RLNVVLSRSS GFDIANTENV VTCSSIDSAL DLLAAPPFSL SIEKVFVIGG 

       190        200        210        220        230        240 
GDILREALNK PSCEAIHITE IDTSIDCDTF IPTVDTSAYQ PWCSSFPICE NGLRFSFTTH 

       250        260        270        280        290        300 
VRVKSSSAGE ASDESDGSKV LQVDWKKFSS VLPKMIFDRH EEYLYLNLVK EIISNGNLKD 

       310        320        330        340        350        360 
DRTGTGTLSK FGCQMKFNLR RNFPLLTTKR VFWRGVVEEL LWFISGSTNA KVLQEKGIRI 

       370        380        390        400        410        420 
WDGNASRAYL DGIGLTEREE GDLGPVYGFQ WRHFGAKYTD MHADYTGQGF DQLLDVINKI 

       430        440        450        460        470        480 
KNNPDDRRII MSAWNPSDLK LMALPPCHMF AQFYVANGEL SCQMYQRSAD MGLGVPFNIA 

       490        500        510        520        530        540 
SYSLLTCILA HVCDLVPGDF IHVIGDAHVY KNHVRPLQEQ LENPPKPFPV LKINPEKKDI 

       550        560 
DSFVADDFEL IGYDPHKKID MKMAV 

« 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 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. expand/collapse author list , 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. expand/collapse author list , 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. 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] OF 48-565.
Strain: cv. Columbia.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRT05277.
RefSeqNP_195183.2. NM_119623.4.
UniGeneAt.31491.

3D structure databases

ProteinModelPortalQ05763.
SMRQ05763. Positions 68-565.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING3702.AT4G34570.1-P.

Proteomic databases

PaxDbQ05763.
PRIDEQ05763.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT4G34570.1; AT4G34570.1; AT4G34570.
GeneID829609.
KEGGath:AT4G34570.

Organism-specific databases

TAIRAT4G34570.

Phylogenomic databases

eggNOGCOG0262.
HOGENOMHOG000257901.
InParanoidQ05763.
KOK13998.
OMAFCQFYVA.
PhylomeDBQ05763.
ProtClustDBCLSN2683596.

Enzyme and pathway databases

BioCycARA:AT4G34570-MONOMER.
UniPathwayUPA00077; UER00158.

Gene expression databases

GenevestigatorQ05763.

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 nameDRTS2_ARATH
AccessionPrimary (citable) accession number: Q05763
Secondary accession number(s): Q0WT35
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: June 26, 2007
Last modified: March 19, 2014
This is version 116 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