Skip Header

Contribute Send feedback
Read comments (?) or add your own

O81395 (DRTS_MAIZE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
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
Short name=DHFR-TS

Including the following 2 domains:

  1. Dihydrofolate reductase
    EC=1.5.1.3
  2. Thymidylate synthase
    EC=2.1.1.45
Gene names
Name:DRTS
OrganismZea mays (Maize)
Taxonomic identifier4577 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › Liliopsida › Poales › Poaceae › PACMAD clade › Panicoideae › Andropogoneae › Zea

Protein attributes

Sequence length521 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 By similarity.

Catalytic activity

5,6,7,8-tetrahydrofolate + NADP+ = 7,8-dihydrofolate + NADPH.

5,10-methylenetetrahydrofolate + dUMP = dihydrofolate + dTMP.

Pathway

Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1.

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 annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 521521Bifunctional dihydrofolate reductase-thymidylate synthase
PRO_0000186358

Regions

Domain17 – 194178DHFR
Nucleotide binding29 – 357NADP By similarity
Nucleotide binding67 – 693NADP By similarity
Nucleotide binding88 – 914NADP By similarity
Nucleotide binding131 – 1388NADP By similarity
Nucleotide binding422 – 4265dUMP By similarity
Nucleotide binding464 – 4663dUMP By similarity
Region197 – 521325Thymidylate synthase

Sites

Active site4031 By similarity
Binding site211Substrate; via carbonyl oxygen By similarity
Binding site231NADP; via amide nitrogen and carbonyl oxygen By similarity
Binding site431Substrate By similarity
Binding site1301Substrate; via carbonyl oxygen By similarity
Binding site1511Substrate By similarity
Binding site2581dUMP By similarity
Binding site4041dUMP By similarity
Binding site4341dUMP By similarity

Sequences

Sequence LengthMass (Da)Tools
O81395 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: 81266F8652625F06

FASTA52158,966
        10         20         30         40         50         60 
MAAVLANGDS QGRPQRNYQV VVAGTRDMGI GKDGVLPWKL PGDLKFFKEL TLTTSDPVKK 

        70         80         90        100        110        120 
NAVIMGRKTW ESIPVKSRPL PGRLNVILTR SGSFDFATVE NVVICGSMES ALELLASTPY 

       130        140        150        160        170        180 
CLSIEKVFVI GGGQVLREYL KGPACEAIHL TDIQSSIECD TFIPPVDFSV FQPWYSSFPV 

       190        200        210        220        230        240 
IESNIRHSFV SFVRVRKSVA ETHESNGKES TEVDTKNDKF ETENFSFLPK MVYDRHEEYQ 

       250        260        270        280        290        300 
YLNLVEDIIR SGAQKNDRTG TGTLSKFGCQ MRFNLRKNFP LLTTKRVFWR GVVEELLWFI 

       310        320        330        340        350        360 
SGSTNAKVLQ EKGIHIWDGN ASREYLNSVG LAHREEGDLG PIYGFQWRHF GAEYTDMHAD 

       370        380        390        400        410        420 
YTGKGFDQLM DVIDKIKNDP EDRRIILSAW NPSDLKKMAL PPCHMFAQFY VENGELSCQM 

       430        440        450        460        470        480 
YQRSADMGLG VPFNIASYSL LTYMIAQVCD LSPGDFVHVI GDAHVYRNHV RALEEQIQKM 

       490        500        510        520 
PKPFPILKIN PSKKDIDSFM ASDFKLVGYD PHQKIEMKMA V

« Hide

References

[1]"Mapping and expression of a bifunctional thymidylate synthase, dihydrofolate reductase gene from maize."
Cox K.M., Robertson D., Fites R.C.
Plant Mol. Biol. 41:733-739(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF073488 mRNA. Translation: AAC26003.1.
PIRT01684.
RefSeqNP_001104916.1. NM_001111446.1.
UniGeneZm.482.

3D structure databases

ProteinModelPortalO81395.
SMRO81395. Positions 236-521.
ModBaseSearch...

Proteomic databases

PRIDEO81395.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID541707.
KEGGzma:541707.

Organism-specific databases

GrameneO81395.

Phylogenomic databases

HOGENOMHOG000257901.
KOK13998.

Enzyme and pathway databases

UniPathwayUPA00077; UER00158.

Family and domain databases

Gene3D3.30.572.10. 1 hit.
3.40.430.10. 1 hit.
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. Thymidylat_synth_C. 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 nameDRTS_MAIZE
AccessionPrimary (citable) accession number: O81395
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1998
Last modified: April 3, 2013
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents