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Q07422

- DRTS_TOXGO

UniProt

Q07422 - DRTS_TOXGO

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Protein

Bifunctional dihydrofolate reductase-thymidylate synthase

Gene
N/A
Organism
Toxoplasma gondii
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

Bifunctional enzyme. Involved in de novo dTMP biosynthesis. Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, DNA precursor synthesis, and for the conversion of dUMP to dTMP (By similarity).By similarity

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 sitei8 – 81Substrate; via carbonyl oxygenBy similarity
Binding sitei10 – 101NADP; via amide nitrogen and carbonyl oxygenBy similarity
Binding sitei31 – 311SubstrateBy similarity
Binding sitei157 – 1571SubstrateBy similarity
Binding sitei172 – 1721SubstrateBy similarity
Binding sitei344 – 3441dUMPBy similarity
Active sitei489 – 4891By similarity
Binding sitei490 – 4901dUMPBy similarity
Binding sitei521 – 5211dUMPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi16 – 227NADPBy similarity
Nucleotide bindingi81 – 833NADPBy similarity
Nucleotide bindingi102 – 1054NADPBy similarity
Nucleotide bindingi152 – 1598NADPBy similarity
Nucleotide bindingi509 – 5135dUMPBy similarity
Nucleotide bindingi551 – 5533dUMPBy similarity

GO - Molecular functioni

  1. dihydrofolate reductase activity Source: UniProtKB-EC
  2. thymidylate synthase activity Source: UniProtKB-EC

GO - Biological processi

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

Keywords - Molecular functioni

Methyltransferase, Oxidoreductase, Transferase

Keywords - Biological processi

Nucleotide biosynthesis, One-carbon metabolism

Keywords - Ligandi

NADP

Enzyme and pathway databases

UniPathwayiUPA00077; UER00158.

Names & Taxonomyi

Protein namesi
Recommended name:
Bifunctional dihydrofolate reductase-thymidylate synthase
Short name:
DHFR-TS
Including the following 2 domains:
Dihydrofolate reductase (EC:1.5.1.3)
Thymidylate synthase (EC:2.1.1.45)
OrganismiToxoplasma gondii
Taxonomic identifieri5811 [NCBI]
Taxonomic lineageiEukaryotaAlveolataApicomplexaConoidasidaCoccidiaEucoccidioridaEimeriorinaSarcocystidaeToxoplasma

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 610610Bifunctional dihydrofolate reductase-thymidylate synthasePRO_0000186352Add
BLAST

Interactioni

Structurei

Secondary structure

1
610
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 117Combined sources
Beta strandi16 – 194Combined sources
Beta strandi24 – 263Combined sources
Helixi29 – 4012Combined sources
Beta strandi74 – 807Combined sources
Helixi81 – 866Combined sources
Helixi89 – 913Combined sources
Beta strandi97 – 1026Combined sources
Helixi108 – 1147Combined sources
Beta strandi125 – 1295Combined sources
Helixi130 – 14112Combined sources
Turni142 – 1443Combined sources
Beta strandi145 – 1506Combined sources
Helixi154 – 16310Combined sources
Beta strandi166 – 1749Combined sources
Beta strandi181 – 1833Combined sources
Helixi190 – 1923Combined sources
Beta strandi227 – 2326Combined sources
Beta strandi236 – 2383Combined sources
Beta strandi241 – 25010Combined sources
Turni288 – 2903Combined sources
Helixi291 – 2977Combined sources
Beta strandi318 – 3203Combined sources
Helixi325 – 33713Combined sources
Beta strandi339 – 3413Combined sources
Beta strandi349 – 36012Combined sources
Beta strandi362 – 3643Combined sources
Beta strandi369 – 3713Combined sources
Helixi375 – 38612Combined sources
Helixi393 – 3964Combined sources
Turni397 – 3993Combined sources
Helixi404 – 4063Combined sources
Helixi409 – 4146Combined sources
Helixi429 – 4357Combined sources
Beta strandi450 – 4523Combined sources
Helixi454 – 46411Combined sources
Beta strandi472 – 4743Combined sources
Turni478 – 4803Combined sources
Helixi481 – 4833Combined sources
Beta strandi484 – 4863Combined sources
Beta strandi489 – 4979Combined sources
Beta strandi501 – 51313Combined sources
Turni514 – 5163Combined sources
Helixi517 – 53519Combined sources
Beta strandi539 – 55315Combined sources
Helixi554 – 5563Combined sources
Helixi557 – 5637Combined sources
Beta strandi573 – 5775Combined sources
Helixi579 – 5813Combined sources
Helixi585 – 5873Combined sources
Beta strandi592 – 5976Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4ECKX-ray3.52A/B1-610[»]
4EILX-ray2.20A/B/C/D/E/F/G/H1-610[»]
4KY4X-ray2.79A/B/C/D/E/F/G/H1-610[»]
4KYAX-ray3.26A/B/C/D/E/F/G/H1-610[»]
ProteinModelPortaliQ07422.
SMRiQ07422. Positions 322-610.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini4 – 250247DHFRAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni322 – 610289Thymidylate 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

OMAiLTCMIAQ.

Family and domain databases

Gene3Di3.30.572.10. 1 hit.
3.40.430.10. 2 hits.
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. 2 hits.
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.

Q07422-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MQKPVCLVVA MTPKRGIGIN NGLPWPHLTT DFKHFSRVTK TTPEEASRLN
60 70 80 90 100
GWLPRKFAKT GDSGLPSPSV GKRFNAVVMG RKTWESMPRK FRPLVDRLNI
110 120 130 140 150
VVSSSLKEED IAAEKPQAEG QQRVRVCASL PAALSLLEEE YKDSVDQIFV
160 170 180 190 200
VGGAGLYEAA LSLGVASHLY ITRVAREFPC DVFFPAFPGD DILSNKSTAA
210 220 230 240 250
QAAAPAESVF VPFCPELGRE KDNEATYRPI FISKTFSDNG VPYDFVVLEK
260 270 280 290 300
RRKTDDAATA EPSNAMSSLT STRETTPVHG LQAPSSAAAI APVLAWMDEE
310 320 330 340 350
DRKKREQKEL IRAVPHVHFR GHEEFQYLDL IADIINNGRT MDDRTGVGVI
360 370 380 390 400
SKFGCTMRYS LDQAFPLLTT KRVFWKGVLE ELLWFIRGDT NANHLSEKGV
410 420 430 440 450
KIWDKNVTRE FLDSRNLPHR EVGDIGPGYG FQWRHFGAAY KDMHTDYTGQ
460 470 480 490 500
GVDQLKNVIQ MLRTNPTDRR MLMTAWNPAA LDEMALPPCH LLCQFYVNDQ
510 520 530 540 550
KELSCIMYQR SCDVGLGVPF NIASYSLLTL MVAHVCNLKP KEFIHFMGNT
560 570 580 590 600
HVYTNHVEAL KEQLRREPRP FPIVNILNKE RIKEIDDFTA EDFEVVGYVP
610
HGRIQMEMAV
Length:610
Mass (Da):68,752
Last modified:February 1, 1995 - v1
Checksum:iCFAF564416D04A29
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L08489 Genomic DNA. Translation: AAB00163.1.
PIRiA46005.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L08489 Genomic DNA. Translation: AAB00163.1 .
PIRi A46005.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4ECK X-ray 3.52 A/B 1-610 [» ]
4EIL X-ray 2.20 A/B/C/D/E/F/G/H 1-610 [» ]
4KY4 X-ray 2.79 A/B/C/D/E/F/G/H 1-610 [» ]
4KYA X-ray 3.26 A/B/C/D/E/F/G/H 1-610 [» ]
ProteinModelPortali Q07422.
SMRi Q07422. Positions 322-610.
ModBasei Search...
MobiDBi Search...

Chemistry

BindingDBi Q07422.
ChEMBLi CHEMBL2425.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

OMAi LTCMIAQ.

Enzyme and pathway databases

UniPathwayi UPA00077 ; UER00158 .

Family and domain databases

Gene3Di 3.30.572.10. 1 hit.
3.40.430.10. 2 hits.
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. 2 hits.
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

  1. "Primary structure of the dihydrofolate reductase-thymidylate synthase gene from Toxoplasma gondii."
    Roos D.S.
    J. Biol. Chem. 268:6269-6280(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: RH.

Entry informationi

Entry nameiDRTS_TOXGO
AccessioniPrimary (citable) accession number: Q07422
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: November 26, 2014
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

3D-structure, Multifunctional enzyme

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3